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Bcl-x/BCL2L1 Protein, Human

Bcl-x/BCL2L1 Protein, Human

Catalog Number: UA011327 Brand: UA BIOSCIENCE
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Regular price $160 USD
Regular price Sale price $160 USD
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Product Details

Product Specification


Species Human
Synonyms Bcl2-L-1, Apoptosis regulator Bcl-X, BCL2L, BCLX
Accession Q07817
Amino Acid Sequence

Ser2- Arg212

Expression System E.coli
Molecular Weight 20-30kDa (Reducing)
Purity >90% by SDS-PAGE
Conjugation Unconjugated
Tag No Tag
Physical Appearance Lyophilized powder
Storage Buffer

PBS, PH7.4, 5% trehalose

Reconstitution Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation.
Stability & Storage

· 12 months from date of receipt, lyophilized powder stored at -20 to -80℃.
· 3 months, -20 to -80℃ under sterile conditions after reconstitution.
· 1 week, 2 to 8℃ under sterile conditions after reconstitution.
· Please avoid repeated freeze-thaw cycles.

Reference

1.Boise LH, González-García M, Postema CE, Ding L, Lindsten T, Turka LA, Mao X, Nuñez G, Thompson CB. bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death. Cell. 1993 Aug 27;74(4):597-608.
2.Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, Yoon HS, Nettesheim D, Chang BS, Thompson CB, Wong SL, Ng SL, Fesik SW. X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature. 1996 May 23;381(6580):335-41.
3.Tse C, Shoemaker AR, Adickes J, Anderson MG, Chen J, Jin S, Johnson EF, Marsh KC, Mitten MJ, Nimmer P, Roberts L, Tahir SK, Xiao Y, Yang X, Zhang H, Fesik S, Rosenberg SH, Elmore SW. ABT-263: a potent and orally bioavailable Bcl-2 family inhibitor. Cancer Res. 2008 May 1;68(9):3421-8. 

Background

Bcl-x (BCL2L1) is an important anti-apoptotic protein in the Bcl-2 family, featuring two major isoforms: Bcl-xL (long form, anti-apoptotic) and Bcl-xS (short form, pro-apoptotic). Bcl-xL contains BH1-4 domains and a C-terminal transmembrane region, and inhibits mitochondrial outer membrane permeabilization by sequestering Bax/Bak or BH3-only proteins (such as Bim and Bad). Beyond regulating apoptosis, Bcl-xL suppresses autophagy through binding to Beclin-1 and participates in mitochondrial homeostasis maintenance. Bcl-xL is highly expressed in various solid tumors and is associated with chemotherapy resistance and poor prognosis; although BH3 mimetics targeting Bcl-xL (such as Navitoclax) demonstrate anti-tumor activity, their clinical application is limited by dose-limiting thrombocytopenia, as Bcl-xL is essential for platelet survival. Current research is shifting toward selective Bcl-xL inhibitors or PROTAC degradation strategies to overcome this toxicity.

Picture

SDS-PAGE

1μg (R: reducing condition, N:non-reducing condition).

ELISA

Immobilized BID His Tag Protein, Human (Cat. No. UA016067) at 10.0μg/mL (100μL/well) can bind Biotinylated Bcl-x/BCL2L1 Protein, Human (Cat. No. UA011327) with EC50 of 4.56-7.53 ng/mL.