Investigation of product derived lymphoma following infusion of piggyBac modified CD19 chimeric antigen receptor T-cells
We carried out a Part I scientific trial of donor derived CD19-specific chimeric antigen receptor T-cells (CAR T-cells) for B-cell malignancy that relapsed or endured after matched associated allogeneic hemopoietic stem cell transplant. To beat the associated fee and transgene capability limitations of conventional viral vectors, CAR T-cells have been produced utilizing the piggyBac transposon system of genetic modification. Following CAR T-cell infusion, one affected person developed a progressively enlarging retroperitoneal tumor on account of a CAR expressing CD4+ T-cell lymphoma. Screening of different sufferers led to the detection of a second CAR T-cell tumor in thoracic para-aortic lymph nodes in an asymptomatic affected person.
Evaluation of the primary lymphoma confirmed a excessive transgene copy quantity, however no insertion into typical oncogenes. There have been additionally structural modifications comparable to altered genomic copy quantity and level mutations unrelated to the insertion websites. Transcriptome evaluation confirmed transgene promoter pushed upregulation of transcription of surrounding areas regardless of insulator sequences surrounding the transgene. Nevertheless, marked international modifications in transcription predominantly correlated with gene copy quantity slightly than insertion websites.
In each sufferers, the CAR T-cell derived lymphoma progressed and one affected person died. We describe the primary two instances of malignant lymphoma derived from CAR gene modified T-cells. Though CAR T-cells have an enviable report of security to this point, our outcomes emphasize the necessity for warning and common comply with up of CAR T recipients, particularly when novel strategies of gene switch are used to create genetically modified immune therapies. The trial was registered at www.anzctr.org.au as ACTRN12617001579381.
Reminiscence stem T cells modified with a redesigned CD30-chimeric antigen receptor present an enhanced antitumor impact in Hodgkin lymphoma
Goals: Adoptive cell remedy (ACT) with mature T cells modified with a chimeric antigen receptor has demonstrated improved consequence for B-cell malignancies. Nevertheless, its utility for others comparable to Hodgkin lymphoma stays a scientific problem. CD30 antigen, expressed in Hodgkin lymphoma cells, is absent in most wholesome tissues, representing a perfect goal of ACT for this illness. Regardless of that, efficacy of CD30-chimeric antigen receptor (CAR) T cells for Hodgkin lymphoma stays modest. Right here, now we have developed and examined a novel CD30-CAR T to enhance efficacy of CD30-CAR remedy, utilizing a concentrating on epitope inside the non-cleavable a part of CD30 receptor, and reminiscence stem T cells (TSCM) to enhance engraftment, persistence and antitumor exercise.
Strategies: TSCM-like cultures have been generated and expanded ex vivo and transduced at day 1 or 2 with a lentiviral vector encoding the CD30-CAR. Therapeutic in vivo experiments have been carried out utilizing NSG mice injected with L540 (sc) or L428 (iv) and handled with CD30-CAR T cells when the tumor was established.
Outcomes: CD30-CAR TSCM-like cells generated and expanded ex vivo, regardless of CD30 expression and fratricide killing of CD30+ CAR T cells, weren’t impaired by soluble CD30 and utterly eradicated Hodgkin lymphoma in vivo, displaying excessive persistence and long-lasting immunity. As well as, extremely enriched CD30-CAR TSCM-like merchandise confer a survival benefit in vivo, in distinction to extra differentiated CAR T cells, with greater tumor infiltration and enhanced antitumor impact.
Conclusion: This research helps using a refined CD30-CAR T cells with extremely enriched TSCM-like merchandise to enhance scientific efficacy of CAR T for Hodgkin lymphoma.
Chimeric antigen receptor T cells concentrating on CD7 in a toddler with high-risk T-cell acute lymphoblastic leukemia
Efficient systemic therapies for relapsed or refractory T-cell acute lymphoblastic leukemia (T-ALL) are restricted. Current scientific utility of chimeric antigen receptor (CAR) immunotherapy has demonstrated profitable management of B-cell malignancies by CAR-T cells; nonetheless, designing CARs for T-ALL stays a problem. CD7 overexpression in T-cell malignancies could also be a horny goal for immunotherapy in T-ALL. This research aimed to explain the protected and efficient use of autologous CD7-CAR T cells (4SCAR7) for the therapy of T-ALL with induction failure in an 11-year-old affected person. Based mostly on The Chinese language Youngsters’s Most cancers Group-ALL (CCCG-ALL) research protocol, minimal residual illness (MRD) by move cytometry (FC) evaluation was detected on days 19 and 46 of remission induction.
On the finish of remission-induction chemotherapy, the affected person achieved morphologic full remission, although with MRD 16.13% and RT-PCR of KMT2A-MLLT1 fusion constructive, which indicated induction failure. The cerebrospinal fluid (CSF) was damaging for blasts at identified. CAR-T remedy and allogeneic transplant have been really helpful as the subsequent therapy choices. CD3+ lymphocytes have been collected from the affected person 18 days after the high-dose MTX chemotherapy by means of leukapheresis. The 4SCAR7 CD7-targeting CAR-T cells have been generated thereafter.
The affected person acquired lymphodepleting chemotherapy previous to 4SCAR7 infusion. Oral administration of itraconazole and sulfamethoxazole was carried out from day zero after CAR-T cell infusion. The affected person didn’t have hypotension, hypoxia, or severe biochemical change or abnormality, however had fever on day 9. Though grade 1 cytokine-release syndrome (CRS) was identified, it was efficiently handled with ibuprofen. Anti-CD7 CAR transgene copy numbers in peripheral blood have been decided by qPCR, which confirmed efficient enlargement initially, then dropped shortly, and endured at a low stage. Though skilled cytopenia from days 14 to 21, the affected person achieved remission on day 17. After full remission, the affected person acquired hematopoietic stem cell transplantation (HSCT) and has recovered effectively to thisdate. Total, this report advised that 4SCAR7 might be a protected and efficient technique for the therapy of pediatric sufferers with high-risk T-cell malignancies.

EBAG9 Antibody |
|||
1-CSB-PA007355GA01HU | Cusabio |
|
|
Description: A polyclonal antibody against EBAG9. Recognizes EBAG9 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC |
EBAG9 Antibody |
|||
R31790 | NSJ Bioreagents | 100 ug | EUR 419 |
EBAG9 Antibody |
|||
R34393-100UG | NSJ Bioreagents | 100 ug | EUR 399 |
EP Reagent Biuret Reagent |
|||
1011601 | Scientific Laboratory Supplies | 1L | EUR 42.18 |
EP Reagent Iodoplatinate Reagent |
|||
1046300 | Scientific Laboratory Supplies | 200ML | EUR 360.24 |
EP Reagent Methoxyphenylacetic Reagent |
|||
1053601 | Scientific Laboratory Supplies | 100ML | EUR 354.54 |
EP Reagent Molybdovanadic Reagent |
|||
1056700 | Scientific Laboratory Supplies | 100ML | EUR 42.18 |
EP Reagent Phosphomolybdotungstic Reagent |
|||
1065000 | Scientific Laboratory Supplies | 100ML | EUR 161.88 |
Automatic CO2 Change Over Unit |
|||
INC6176 | Scientific Laboratory Supplies | EACH | EUR 1288.2 |
Forceps Dissecting Turn Over End |
|||
D02129 | Scientific Laboratory Supplies | EACH | EUR 4.67 |
Gas Change Over Unit 30Psi |
|||
GAS1000 | Scientific Laboratory Supplies | EACH | EUR 904.02 |
Gas Change Over Unit 60Psi |
|||
GAS1002 | Scientific Laboratory Supplies | EACH | EUR 905.16 |
Gas Change Over Unit 100Psi |
|||
GAS1004 | Scientific Laboratory Supplies | EACH | EUR 922.26 |
Bolle TG10 Safety Over Glasses |
|||
SAF1106 | Scientific Laboratory Supplies | EACH | EUR 8.39 |
Human EBAG9 Antibody |
|||
32605-05111 | AssayPro | 150 ug | EUR 313.2 |
EBAG9 Blocking Peptide |
|||
33R-2039 | Fitzgerald | 100 ug | EUR 216 |
Description: A synthetic peptide for use as a blocking control in assays to test for specificity of EBAG9 antibody, catalog no. 70R-9916 |
EBAG9 Rabbit pAb |
|||
A8385-100ul | Abclonal | 100 ul | EUR 369.6 |
EBAG9 Rabbit pAb |
|||
A8385-200ul | Abclonal | 200 ul | EUR 550.8 |
EBAG9 Rabbit pAb |
|||
A8385-20ul | Abclonal | 20 ul | Ask for price |
EBAG9 Rabbit pAb |
|||
A8385-50ul | Abclonal | 50 ul | Ask for price |
EBAG9 Rabbit pAb |
|||
A1935-100ul | Abclonal | 100 ul | EUR 369.6 |
EBAG9 Rabbit pAb |
|||
A1935-200ul | Abclonal | 200 ul | EUR 550.8 |
EBAG9 Rabbit pAb |
|||
A1935-20ul | Abclonal | 20 ul | EUR 219.6 |
EBAG9 Rabbit pAb |
|||
A1935-50ul | Abclonal | 50 ul | EUR 267.6 |
EBAG9 Blocking Peptide |
|||
DF6703-BP | Affbiotech | 1mg | EUR 234 |
EBAG9 Conjugated Antibody |
|||
C38323 | SAB | 100ul | EUR 476.4 |
EBAG9 cloning plasmid |
|||
CSB-CL007355HU1-10ug | Cusabio | 10ug | EUR 279.6 |
Description: A cloning plasmid for the EBAG9 gene. |
EBAG9 cloning plasmid |
|||
CSB-CL007355HU2-10ug | Cusabio | 10ug | EUR 279.6 |
Description: A cloning plasmid for the EBAG9 gene. |
Anti-EBAG9 Antibody |
|||
PB9553 | BosterBio | 100ug/vial | EUR 400.8 |
Anti-EBAG9 antibody |
|||
STJ110683 | St John's Laboratory | 100 µl | EUR 332.4 |
Description: This gene was identified as an estrogen-responsive gene. Regulation of transcription by estrogen is mediated by estrogen receptor, which binds to the estrogen-responsive element found in the 5'-flanking region of this gene. The encoded protein is a tumor-associated antigen that is expressed at high frequency in a variety of cancers. Alternate splicing results in multiple transcript variants. A pseudogene of this gene has been defined on chromosome 10. |
Anti-EBAG9 antibody |
|||
STJ23462 | St John's Laboratory | 100 µl | EUR 332.4 |
Description: This gene was identified as an estrogen-responsive gene. Regulation of transcription by estrogen is mediated by estrogen receptor, which binds to the estrogen-responsive element found in the 5'-flanking region of this gene. The encoded protein is a tumor-associated antigen that is expressed at high frequency in a variety of cancers. Alternate splicing results in multiple transcript variants. A pseudogene of this gene has been defined on chromosome 10. |
Anti-EBAG9 (4A10) |
|||
YF-MA16699 | Abfrontier | 100 ug | EUR 435.6 |
Description: Mouse monoclonal to EBAG9 |
pCMV-SPORT6-EBAG9 |
|||
PVT13493 | Lifescience Market | 2 ug | EUR 469.2 |
EP Reagent Sulfomolybdic Reagent R3 |
|||
1086500 | Scientific Laboratory Supplies | 1L | EUR 287.28 |
DURAN Over-Cap 45mm Black Phenolic |
|||
BOT2596 | Scientific Laboratory Supplies | PK10 | EUR 25.08 |
EBAG9 protein (His tag) |
|||
80R-1093 | Fitzgerald | 100 ug | EUR 268.8 |
Description: Purified recombinant Human EBAG9 protein |
Polyclonal EBAG9 Antibody (Center) |
|||
APR06938G | Leading Biology | 0.1ml | EUR 580.8 |
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human EBAG9 (Center). This antibody is tested and proven to work in the following applications: |
Polyclonal EBAG9 Antibody (Center) |
|||
APR04492G | Leading Biology | 0.1ml | EUR 580.8 |
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human EBAG9 (Center). This antibody is tested and proven to work in the following applications: |
Human EBAG9 shRNA Plasmid |
|||
20-abx956064 | Abbexa |
|
|
Mouse EBAG9 shRNA Plasmid |
|||
20-abx974569 | Abbexa |
|
|
Rat EBAG9 shRNA Plasmid |
|||
20-abx989010 | Abbexa |
|
|
Anti-EBAG9 / RCAS1 antibody |
|||
STJ70947 | St John's Laboratory | 100 µg | EUR 430.8 |
EBAG9 Recombinant Protein (Human) |
|||
RP010096 | ABM | 100 ug | Ask for price |
EBAG9 Recombinant Protein (Human) |
|||
RP010099 | ABM | 100 ug | Ask for price |
EBAG9 Recombinant Protein (Rat) |
|||
RP198968 | ABM | 100 ug | Ask for price |
EBAG9 Recombinant Protein (Mouse) |
|||
RP130676 | ABM | 100 ug | Ask for price |
BOP reagent |
|||
5-02141 | CHI Scientific | 25g | Ask for price |
BOP reagent |
|||
5-02142 | CHI Scientific | 100g | Ask for price |
Chymase reagent |
|||
30C-CP1129 | Fitzgerald | 5 units | EUR 2622 |
Description: Purified native Human Chymase reagent |
Traut's Reagent |
|||
2330-1000 | Biovision | EUR 418.8 |
Traut's Reagent |
|||
2330-500 | Biovision | EUR 248.4 |
MTS Reagent |
|||
2808-1000 | Biovision | EUR 1188 |
MTS Reagent |
|||
2808-250 | Biovision | EUR 438 |
MTT Reagent |
|||
2809-1G | Biovision | EUR 216 |
MTT Reagent |
|||
2809-5G | Biovision | EUR 652.8 |
BOP reagent |
|||
A7015-100000 | ApexBio | 100 g | EUR 240 |
Description: A peptide coupling reagent. Can be used in the preparation of phenyl esters of amino acids which have been shown to be valuable as blocked derivatives of amino acids in the field of peptide synthesis. |
BOP reagent |
|||
A7015-25000 | ApexBio | 25 g | EUR 135.6 |
Description: A peptide coupling reagent. Can be used in the preparation of phenyl esters of amino acids which have been shown to be valuable as blocked derivatives of amino acids in the field of peptide synthesis. |
Bradford reagent |
|||
BDE641 | Bio Basic | 100ml | EUR 73.21 |
Bluing Reagent |
|||
BRT030 | ScyTek Laboratories | 30 ml | EUR 72 |
Bluing Reagent |
|||
BRT125 | ScyTek Laboratories | 125 ml | EUR 75.6 |
Bluing Reagent |
|||
BRT3800 | ScyTek Laboratories | 1 Gal. | EUR 220.8 |
Bluing Reagent |
|||
BRT500 | ScyTek Laboratories | 500 ml | EUR 91.2 |
Bluing Reagent |
|||
BRT999 | ScyTek Laboratories | 1000 ml | EUR 105.6 |
Beaucage reagent |
|||
HY-100951 | MedChemExpress | 10mM/1mL | EUR 151.2 |
Phosphate Reagent |
|||
106199 | Scientific Laboratory Supplies | PK100 | EUR 61.29 |
Chromium Reagent |
|||
1206699 | Scientific Laboratory Supplies | EACH | EUR 141.72 |
Ninhydrin Reagent |
|||
MIC6746 | Scientific Laboratory Supplies | EACH | EUR 31.12 |
Nessler Reagent |
|||
NESSR | Scientific Laboratory Supplies | 500ML | EUR 148.2 |
Thioacetamide Reagent |
|||
THIOR01 | Scientific Laboratory Supplies | 100ML | EUR 78.66 |
HEK-293T Telomerase Over-Expressing Cell Pellet |
|||
abx069991-1Pellet | Abbexa | 1 Pellet | EUR 477.6 |
Visitor Eye Shield Over Specs - Portwest PW30 |
|||
SAF1021 | Scientific Laboratory Supplies | EACH | EUR 3.42 |
Esophagus Lysate |
|||
1365 | ProSci | 0.1 mg | EUR 229.2 |
Description: Esophagus tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Ileum Lysate |
|||
1367 | ProSci | 0.1 mg | EUR 229.2 |
Description: Ileum tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Rectum Lysate |
|||
1373 | ProSci | 0.1 mg | EUR 229.2 |
Description: Rectum tissue lysate was prepared by homogenization in homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Skin Lysate |
|||
1376 | ProSci | 0.1 mg | EUR 229.2 |
Description: Skin tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Thyroid Lysate |
|||
1380 | ProSci | 0.1 mg | EUR 229.2 |
Description: Thyroid tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Spleen Lysate |
|||
1406 | ProSci | 0.1 mg | EUR 229.2 |
Description: Spleen tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Bladder Lysate |
|||
1410 | ProSci | 0.1 mg | EUR 229.2 |
Description: Bladder tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Cerebellum Lysate |
|||
1412 | ProSci | 0.1 mg | EUR 229.2 |
Description: Cerebellum tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Cerebrum Lysate |
|||
1413 | ProSci | 0.1 mg | EUR 229.2 |
Description: Cerebrum tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Pancreas Lysate |
|||
1414 | ProSci | 0.1 mg | EUR 229.2 |
Description: Pancreas tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Stomach Lysate |
|||
1415 | ProSci | 0.1 mg | EUR 229.2 |
Description: Stomach tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Testis Lysate |
|||
1416 | ProSci | 0.1 mg | EUR 229.2 |
Description: Testis tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Adrenal Lysate |
|||
1417 | ProSci | 0.1 mg | EUR 229.2 |
Description: Adrenal tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Skin Lysate |
|||
1419 | ProSci | 0.1 mg | EUR 229.2 |
Description: Skin tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Eye Lysate |
|||
1420 | ProSci | 0.1 mg | EUR 229.2 |
Description: Eye tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Trachea Lysate |
|||
1422 | ProSci | 0.1 mg | EUR 229.2 |
Description: Trachea tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Lung Lysate |
|||
1462 | ProSci | 0.1 mg | EUR 229.2 |
Description: Lung tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Liver Lysate |
|||
1464 | ProSci | 0.1 mg | EUR 229.2 |
Description: Liver tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Kidney Lysate |
|||
1465 | ProSci | 0.1 mg | EUR 229.2 |
Description: Kidney tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Spleen Lysate |
|||
1466 | ProSci | 0.1 mg | EUR 229.2 |
Description: Spleen tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
L1210 Lysate |
|||
1284 | ProSci | 0.1 mg | EUR 229.2 |
Description: L1210 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The L1210 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
C2C12 Lysate |
|||
1285 | ProSci | 0.1 mg | EUR 229.2 |
Description: C2C12 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The C2C12 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
P815 Lysate |
|||
1286 | ProSci | 0.1 mg | EUR 229.2 |
Description: P815 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The P815 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
EL4 Lysate |
|||
1287 | ProSci | 0.1 mg | EUR 229.2 |
Description: EL4 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The EL4 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Lung Lysate |
|||
1302 | ProSci | 0.1 mg | EUR 229.2 |
Description: Lung tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Spleen Lysate |
|||
1306 | ProSci | 0.1 mg | EUR 229.2 |
Description: Spleen tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Placenta Lysate |
|||
1309 | ProSci | 0.1 mg | EUR 229.2 |
Description: Placenta tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Melanoma Lysate |
|||
20-101 | ProSci | 0.1 mg | EUR 632.4 |
Description: Melanoma lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human melanoma tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the melanoma tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The melanoma tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Trachea Lysate |
|||
20-102 | ProSci | 0.1 mg | EUR 500.1 |
Description: Human trachea lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human trachea tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the trachea tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The trachea tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Jurkat Lysate |
|||
1205 | ProSci | 0.1 mg | EUR 229.2 |
Description: Jurkat lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The Jurkat lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
MOLT4 Lysate |
|||
1206 | ProSci | 0.1 mg | EUR 229.2 |
Description: MOLT4 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The MOLT4 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
HL60 Lysate |
|||
1209 | ProSci | 0.1 mg | EUR 229.2 |
Description: HL60 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The HL60 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
T24 Lysate |
|||
1213 | ProSci | 0.1 mg | EUR 229.2 |
Description: T24 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The T24 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
U937 Lysate |
|||
1215 | ProSci | 0.1 mg | EUR 229.2 |
Description: U937 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The U937 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
MCF7 Lysate |
|||
1219 | ProSci | 0.1 mg | EUR 229.2 |
Description: MCF7 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The MCF7 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Ramos Lysate |
|||
1225 | ProSci | 0.1 mg | EUR 229.2 |
Description: Ramos lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The Ramos lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Kidney Lysate |
|||
21-104 | ProSci | 0.1 mg | EUR 342.6 |
Description: Bovine kidney tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The bovine kidney tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the kidney tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The kidney tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Liver Lysate |
|||
21-105 | ProSci | 0.1 mg | EUR 342.6 |
Description: Bovine liver tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The bovine liver tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the liver tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The liver tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Heart Lysate |
|||
21-115 | ProSci | 0.1 mg | EUR 342.6 |
Description: Guinea Pig heart tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The guinea pig heart tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the heart tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The heart tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Affected person-Reported Outcomes for Most cancers Sufferers with Hematological Malignancies Present process Chimeric Antigen Receptor T Cell Remedy: A Systematic Assessment
Databases have been searched to establish research revealed over the previous 10 years that addressed the utility of patient-reported outcomes (PROs) in sufferers receiving chimeric antigen receptor (CAR) T cell remedy in sufferers with hematological malignancies. Amongst 280 data, three articles masking 206 sufferers have been eligible. The info have been prospectively collected at a number of time factors. The compliance charges have been 70% to 94%. There was an inverse relationship between fatigue and social perform amongst adults. The standard of life (QoL) enchancment and skill to finish PROs have been linked to illness standing. About 40% of adults reported no less than some cognitive difficulties, with a detrimental influence on psychological and bodily well being standing. In adults, probably the most generally reported cognitive impairment was reminiscence difficulties.
Melancholy was related to cognitive difficulties. Youthful adults have been at greater threat of long-term poor psychological well being, anxiousness, and despair. For pediatric and adolescent sufferers, emotional dysfunction improves over time. QoL standing improved over time; but, extreme cytokine launch syndrome and neurotoxicity precipitated delayed enchancment. Info concerning whether or not the PROs have been built-in into medical data and scientific tips is missing. Using PROs in sufferers on CAR T cell remedy appears possible and informative. Research using bigger pattern sizes and utilizing validated PRO instruments at completely different time factors stay unmet wants.