medmk

Investigation of product derived lymphoma

Investigation of product derived lymphoma following infusion of piggyBac modified CD19 chimeric antigen receptor T-cells

We carried out a Section I scientific trial of donor derived CD19-specific chimeric antigen receptor T-cells (CAR T-cells) for B-cell malignancy that relapsed or persevered after matched associated allogeneic hemopoietic stem cell transplant. To beat the 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 step by step enlarging retroperitoneal tumor as a result 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 resembling 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 world modifications in transcription predominantly correlated with gene copy quantity moderately 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 document of security so far, 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.

medmk
medmk

EBAG9 Antibody

1-CSB-PA007355GA01HU
  • EUR 716.40
  • EUR 399.60
  • 150ul
  • 50ul
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 100 ug
EUR 419

EBAG9 Antibody

R34393-100UG 100 ug
EUR 399

EP Reagent Biuret Reagent

1011601 1L
EUR 42.18

EP Reagent Iodoplatinate Reagent

1046300 200ML
EUR 360.24

EP Reagent Methoxyphenylacetic Reagent

1053601 100ML
EUR 354.54

EP Reagent Molybdovanadic Reagent

1056700 100ML
EUR 42.18

EP Reagent Phosphomolybdotungstic Reagent

1065000 100ML
EUR 161.88

Automatic CO2 Change Over Unit

INC6176 EACH
EUR 1288.2

Forceps Dissecting Turn Over End

D02129 EACH
EUR 4.67

Gas Change Over Unit 30Psi

GAS1000 EACH
EUR 904.02

Gas Change Over Unit 60Psi

GAS1002 EACH
EUR 905.16

Gas Change Over Unit 100Psi

GAS1004 EACH
EUR 922.26

Bolle TG10 Safety Over Glasses

SAF1106 EACH
EUR 8.39

Human EBAG9 Antibody

32605-05111 150 ug
EUR 313.2

EBAG9 Blocking Peptide

33R-2039 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 100 ul
EUR 369.6

EBAG9 Rabbit pAb

A8385-200ul 200 ul
EUR 550.8

EBAG9 Rabbit pAb

A8385-20ul 20 ul Ask for price

EBAG9 Rabbit pAb

A8385-50ul 50 ul Ask for price

EBAG9 Rabbit pAb

A1935-100ul 100 ul
EUR 369.6

EBAG9 Rabbit pAb

A1935-200ul 200 ul
EUR 550.8

EBAG9 Rabbit pAb

A1935-20ul 20 ul
EUR 219.6

EBAG9 Rabbit pAb

A1935-50ul 50 ul
EUR 267.6

EBAG9 Blocking Peptide

DF6703-BP 1mg
EUR 234

EBAG9 Conjugated Antibody

C38323 100ul
EUR 476.4

EBAG9 cloning plasmid

CSB-CL007355HU1-10ug 10ug
EUR 279.6
Description: A cloning plasmid for the EBAG9 gene.

EBAG9 cloning plasmid

CSB-CL007355HU2-10ug 10ug
EUR 279.6
Description: A cloning plasmid for the EBAG9 gene.

Anti-EBAG9 Antibody

PB9553 100ug/vial
EUR 400.8

Anti-EBAG9 antibody

STJ110683 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 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 100 ug
EUR 435.6
Description: Mouse monoclonal to EBAG9

pCMV-SPORT6-EBAG9

PVT13493 2 ug
EUR 469.2

EP Reagent Sulfomolybdic Reagent R3

1086500 1L
EUR 287.28

DURAN Over-Cap 45mm Black Phenolic

BOT2596 PK10
EUR 25.08

EBAG9 protein (His tag)

80R-1093 100 ug
EUR 268.8
Description: Purified recombinant Human EBAG9 protein

Polyclonal EBAG9 Antibody (Center)

APR06938G 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 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
  • EUR 961.20
  • EUR 1345.20
  • 150 µg
  • 300 µg

Mouse EBAG9 shRNA Plasmid

20-abx974569
  • EUR 961.20
  • EUR 1345.20
  • 150 µg
  • 300 µg

Rat EBAG9 shRNA Plasmid

20-abx989010
  • EUR 961.20
  • EUR 1345.20
  • 150 µg
  • 300 µg

Anti-EBAG9 / RCAS1 antibody

STJ70947 100 µg
EUR 430.8

EBAG9 Recombinant Protein (Human)

RP010096 100 ug Ask for price

EBAG9 Recombinant Protein (Human)

RP010099 100 ug Ask for price

EBAG9 Recombinant Protein (Rat)

RP198968 100 ug Ask for price

EBAG9 Recombinant Protein (Mouse)

RP130676 100 ug Ask for price

BOP reagent

5-02141 25g Ask for price

BOP reagent

5-02142 100g Ask for price

Chymase reagent

30C-CP1129 5 units
EUR 2622
Description: Purified native Human Chymase reagent

Traut's Reagent

2330-1000
EUR 418.8

Traut's Reagent

2330-500
EUR 248.4

MTS Reagent

2808-1000
EUR 1188

MTS Reagent

2808-250
EUR 438

MTT Reagent

2809-1G
EUR 216

MTT Reagent

2809-5G
EUR 652.8

BOP reagent

A7015-100000 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 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 100ml
EUR 73.21

Bluing Reagent

BRT030 30 ml
EUR 72

Bluing Reagent

BRT125 125 ml
EUR 75.6

Bluing Reagent

BRT3800 1 Gal.
EUR 220.8

Bluing Reagent

BRT500 500 ml
EUR 91.2

Bluing Reagent

BRT999 1000 ml
EUR 105.6

Beaucage reagent

HY-100951 10mM/1mL
EUR 151.2

Phosphate Reagent

106199 PK100
EUR 61.29

Chromium Reagent

1206699 EACH
EUR 141.72

Ninhydrin Reagent

MIC6746 EACH
EUR 31.12

Nessler Reagent

NESSR 500ML
EUR 148.2

Thioacetamide Reagent

THIOR01 100ML
EUR 78.66

HEK-293T Telomerase Over-Expressing Cell Pellet

abx069991-1Pellet 1 Pellet
EUR 477.6

Visitor Eye Shield Over Specs - Portwest PW30

SAF1021 EACH
EUR 3.42

Esophagus Lysate

1365 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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.

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 end result for B-cell malignancies. Nevertheless, its software for others resembling Hodgkin lymphoma stays a scientific problem. CD30 antigen, expressed in Hodgkin lymphoma cells, is absent in most wholesome tissues, representing a really 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, we now have developed and examined a novel CD30-CAR T to enhance efficacy of CD30-CAR remedy, utilizing a concentrating on epitope throughout 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, exhibiting 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 examine 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 software of chimeric antigen receptor (CAR) immunotherapy has demonstrated profitable management of B-cell malignancies by CAR-T cells; nevertheless, 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 examine aimed to explain the secure 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. Primarily based on The Chinese language Kids’s Most cancers Group-ALL (CCCG-ALL) examine protocol, minimal residual illness (MRD) by circulation 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 destructive 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 way 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 rapidly, and persevered 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 nicely to thisdate. Total, this report instructed that 4SCAR7 could possibly be a secure and efficient technique for the therapy of pediatric sufferers with high-risk T-cell malignancies.

Affected person-Reported Outcomes for Most cancers Sufferers with Hematological Malignancies Present process Chimeric Antigen Receptor T Cell Remedy: A Systematic Evaluate

Databases have been searched to determine research printed 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 information, three articles overlaying 206 sufferers have been eligible. The information 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 operate amongst adults. The standard of life (QoL) enchancment and talent to finish PROs have been linked to illness standing. About 40% of adults reported not 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 melancholy. For pediatric and adolescent sufferers, emotional dysfunction improves over time. QoL standing improved over time; but, extreme cytokine launch syndrome and neurotoxicity brought on delayed enchancment. Data relating to whether or not the PROs have been built-in into medical information 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 totally different time factors stay unmet wants.

Leave a Reply

Your email address will not be published. Required fields are marked *