Recombinant Human BCL2 Protein
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human BCL2 Protein is a Human Fragment protein, in the 1 to 211 aa range, expressed in HEK 293 cells, with >95%, <0.005 EU/µg endotoxin level.
View Alternative Names
Apoptosis regulator Bcl-2, BCL2
- Mass Spec
Supplier Data
Mass Spectrometry - Recombinant Human BCL2 Protein (AB290060)
Mass determination by ESI-TOF.
Predicted MW is 23364.35 Da. (+/- 10 Da by ESI-TOF). Observed MW is 23364.81 Da.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human BCL2 Protein (AB290060)
SDS-PAGE analysis of ab290060
- HPLC
Supplier Data
HPLC - Recombinant Human BCL2 Protein (AB290060)
HPLC analysis of ab290060
You may be interested in:
Why is this recommended?
We recommend this product because it’s often used in the same experiment or related research.
We advise that you always check the datasheet to ensure it fits your experiments, or contact ourtechnical teamfor help.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The role of Bcl-2 extends to maintaining cell survival and balancing apoptotic signals. It functions as an anti-apoptotic molecule within the cell primarily involved in forming complexes with pro-apoptotic members of the Bcl-2 family like Bax and Bak. These interactions prevent mitochondrial membrane permeabilization which is an important step in apoptotic signal transduction. As an important regulator of apoptosis Bcl-2 helps in cellular homeostasis and appropriate immune responses under physiological conditions.
Pathways
Bcl-2 plays a critical role in the intrinsic or mitochondrial pathway of apoptosis. Within this pathway Bcl-2 interacts with other proteins such as cytochrome c and APAF-1 to inhibit apoptosis. This pathway involves a network of Bcl-2 family proteins where Bcl-2's anti-apoptotic role counteracts the pro-apoptotic activity of proteins like Bax. These interactions help fine-tune the apoptotic response to various internal stimuli maintaining cellular integrity and function.
Specifications
Form
Lyophilized
General info
Function
Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells (PubMed : 1508712, PubMed : 8183370). Regulates cell death by controlling the mitochondrial membrane permeability (PubMed : 11368354). Appears to function in a feedback loop system with caspases (PubMed : 11368354). Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1) (PubMed : 11368354). Also acts as an inhibitor of autophagy : interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function (PubMed : 18570871, PubMed : 20889974, PubMed : 21358617). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed : 17418785).
Sequence similarities
Belongs to the Bcl-2 family.
Post-translational modifications
Phosphorylation/dephosphorylation on Ser-70 regulates anti-apoptotic activity (PubMed:11368354). Growth factor-stimulated phosphorylation on Ser-70 by PKC is required for the anti-apoptosis activity and occurs during the G2/M phase of the cell cycle (PubMed:11368354). In the absence of growth factors, BCL2 appears to be phosphorylated by other protein kinases such as ERKs and stress-activated kinases (PubMed:11368354). Phosphorylated by MAPK8/JNK1 at Thr-69, Ser-70 and Ser-87, which stimulates starvation-induced autophagy (PubMed:10567572, PubMed:18570871). Dephosphorylated by protein phosphatase 2A (PP2A) (By similarity).. Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity, causes the release of cytochrome c into the cytosol promoting further caspase activity.. Monoubiquitinated by PRKN, leading to an increase in its stability (PubMed:20889974). Ubiquitinated by SCF(FBXO10), leading to its degradation by the proteasome (PubMed:23431138). Ubiquitinated by XIAP, leading to its degradation by the proteasome (PubMed:29020630).
Subcellular localisation
Mitochondrion outer membrane
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com