Bcl2

Expression system: E. coli
Length: 5-205, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-236, Full Length
Activity: Not Tested

BCL2 (B-cell leukemia lymphoma 2, N-Histidine-tagged), also known as Bcl-2, belongs to the Bcl-2 family. Bcl-2 family proteins regulate and contribute to programmed cell death or apoptosis. It is a large protein family and all members contain at least one of four BH (bcl-2 homology) domains. Certain members such as Bcl-2, Bcl-xl and Mcl1 are anti-apoptotic, whilst others are pro-apoptotic. Most Bcl-2 family members contain a C-terminal transmembrane domain that functions to target these proteins to the outer mitochondrial and other intracellular membranes. It is expressed in a variety of tissues. BCL2 blocks the apoptotic death of some cells such as lymphocytes. It also regulates cell death by controlling the mitochondrial membrane permeability and inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and or by binding to the apoptosis-activating factor. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

Expression system: E. coli
Length: 147-227, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-152, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-450, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-321, Partial
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 1-321, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-187, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-156, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-448, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-283, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-464, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 18-262, Extracellular Domain
Activity: Not Tested

Tumor necrosis factor receptor superfamily member 1A (Tnfrsf1a) is a member of the tumor necrosis factor receptor superfamily. Tnfrsf1a is one of the major receptors for the tumor necrosis factor-alpha. It can activate the transcription factor NF-κB, mediate apoptosis, and function as a regulator of inflammation. Antiapoptotic protein BCL2-associated athanogene 4 (BAG4 SODD) and adaptor proteins TRADD and TRAF2 have been shown to interact with this receptor, and thus play regulatory roles in the signal transduction mediated by the receptor. Germline mutations of the extracellular domains of this receptor were found to be associated with the human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS) or periodic fever syndrome

Bcl-2-like protein 2 (BCL2L2) belongs to the Bcl-2 family. BCL2L2 is highly expressed in thebrain, spinal cord, testis, pancreas, heart, spleen, and mammary glands. BCL2L2 is a peripheral membrane protein containing three motifs, BH1, BH2 and BH4. The BH4 motif appears to be involved in the anti-apoptotic function. The BH1 and BH2 motifs form a hydrophobic groove which acts as a docking site for the BH3 domain of some pro-apoptotic proteins. BCL2L2 promotes cell survival and blocks dexamethasone-induced apoptosis. Furthermore, BCL2L2 mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.

Expression system: E. coli
Length: 1-172, Partial
Activity: Not Tested

The deletion of BNIP3L results in retention of mitochondria during lens fiber cell remodeling, and that deletion of BNIP3L also results in the retention of endoplasmic reticulum and Golgi apparatus. BNIP3L localizes to the endoplasmic reticulum and Golgi apparatus of wild-type newborn mouse lenses and is contained within mitochondria, endoplasmic reticulum and Golgi apparatus isolated from adult mouse liver. As the cells become packed with keratin bundles, Bnip3L expression triggers mitophagy to rid the cells of the last remaining 'living' characteristic, thus completing the march from 'living' to 'dead' within the hair follicle. during retinal development tissue hypoxia triggers HIF1A HIF-1 stabilization, resulting in increased expression of the mitophagy receptor BNIP3L NIX. BNIP3L-dependent mitophagy results in a metabolic shift toward glycolysis essential for RGC neurogenesis. BNIP3L could be a potential therapeutic target for ischemic stroke

BCL-XL Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 25.2 kDa and the accession number is Q07817.

Expression system: E. coli
Length: 1-212, Partial
Activity: ELISA

Expression system: E. coli
Length: 1-184, Full length
Activity: Not Tested

BCL2L11, also known as Bim, belongs to the BCL-2 protein family. Members of this family form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. BCL2L11 contains a Bcl-2 homology domain 3 (BH3). It has been shown to interact with other members of the BCL-2 protein family, including BCL2, BCL2L1 BCL-X(L), and MCL1, and to act as an apoptotic activator. BCL2L11 gene functions as an essential initiator of apoptosis in thymocyte-negative selection.