Product nameBcl-2 peptide
See all Bcl-2 proteins and peptides
Amino Acid Sequence
Our Abpromise guarantee covers the use of ab45606 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
- Apoptosis regulator Bcl 2
- Apoptosis regulator Bcl-2
- Apoptosis regulator Bcl2
FunctionSuppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. 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). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785).
Tissue specificityExpressed in a variety of tissues.
Involvement in diseaseA chromosomal aberration involving BCL2 has been found in chronic lymphatic leukemia. Translocation t(14;18)(q32;q21) with immunoglobulin gene regions. BCL2 mutations found in non-Hodgkin lymphomas carrying the chromosomal translocation could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions.
Sequence similaritiesBelongs to the Bcl-2 family.
DomainBH1 and BH2 domains are required for the interaction with BAX and for anti-apoptotic activity.
The BH4 motif is required for anti-apoptotic activity and for interaction with RAF1 and EGLN3.
The loop between motifs BH4 and BH3 is required for the interaction with NLRP1.
modificationsPhosphorylation/dephosphorylation on Ser-70 regulates anti-apoptotic activity. 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. In the absence of growth factors, BCL2 appears to be phosphorylated by other protein kinases such as ERKs and stress-activated kinases. Phosphorylated by MAPK8/JNK1 at Thr-69, Ser-70 and Ser-87, wich stimulates starvation-induced autophagy. Dephosphorylated by protein phosphatase 2A (PP2A).
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 PARK2, leading to increase its stability. Ubiquitinated by SCF(FBXO10), leading to its degradation by the proteasome.
Cellular localizationMitochondrion outer membrane. Nucleus membrane. Endoplasmic reticulum membrane.
- Information by UniProt
ab45606 has not yet been referenced specifically in any publications.