Bcl-2 Antibody (YA3469)
(Synonyms: BCL2; Apoptosis regulator Bcl-2)Bcl-2 Antibody (YA3469) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Bcl-2.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, IHC-P, IHC-F, ICC/IF
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Reactivity :
Human, Chicken
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Formulation:
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide, pH 7.3.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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IHC-F
IHC-F: Immunohistochemistry-Frozen
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 1:50-1:100 | 1:50-1:100 | 1:50-1:200 |
Product Details
Bcl-2 Antibody (YA3469) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Bcl-2.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Chicken
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Observed Molecular WeightObserved band size: 26 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 26 kDa
Synthetic Peptide of Bcl-2.
affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide, pH 7.3.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Bcl-2 (B-cell lymphoma 2) is a central anti-apoptotic regulator that preserves mitochondrial integrity by preventing mitochondrial outer membrane permeabilization (MOMP), a critical checkpoint controlling cytochrome c release and caspase activation during intrinsic apoptosis[1][2]. Mechanistically, Bcl-2 functions through direct interactions with pro-apoptotic BCL-2 family proteins, including Bax and Bak, thereby suppressing their oligomerization and limiting mitochondrial membrane disruption[3][4]. The protein also integrates signals transmitted by BH3-only proteins, which regulate the balance between cell survival and programmed cell death under physiological and pathological stress conditions[3][5]. Dysregulated Bcl-2 expression contributes to apoptosis resistance in multiple malignancies and supports tumor cell survival by maintaining mitochondrial homeostasis despite cellular stress[6][7]. In disease models, the anti-apoptotic activity of Bcl-2 is closely linked to mitochondrial apoptosis pathways that represent major therapeutic targets in hematologic and solid cancers[6][8]. Compared with related anti-apoptotic isoforms such as Mcl-1 and Bcl-B, Bcl-2 displays broader interactions with both Bax and Bak, whereas Mcl-1 and Bcl-B show preferential regulation of Bak- and Bax-dependent apoptotic pathways, respectively[4]. For experimental applications, BH3-mimetic inhibitors disrupt the interaction between Bcl-2 and pro-apoptotic partners, thereby restoring mitochondrial apoptosis and providing a widely used strategy for mechanistic studies and targeted cancer research[7][8].
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Subcellular Localization
Mitochondrion outer membrane; Single-pass membrane protein; Nucleus membrane; Single-pass membrane protein; Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasm
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Expression
Tissue_specificity:Expression in multiple organizations -
Isoforms & Post-Translational Modification
P10415 has 2 isomers: P10415-1: 26266 Da (predicted); P10415-2: 22337 Da (predicted).
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) -
Subunit
Forms homodimers, and heterodimers with BAX, BAD, BAK and Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2 motifs, and is necessary for anti-apoptotic activity (PubMed:25609812, PubMed:8183370).
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SwissProt ID
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Synonyms
BCL2; Apoptosis regulator Bcl-2
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Research Field
Cell Biology
Documentation
References
[4]. Zhai D, et al. Differential regulation of Bax and Bak by anti-apoptotic Bcl-2 family proteins Bcl-B and Mcl-1. J Biol Chem. 2008 Apr 11;283(15):9580-6. [Content Brief]
[5]. Lomonosova E, et al. BH3-only proteins in apoptosis and beyond: an overview. Oncogene. 2008 Dec;27 Suppl 1(Suppl 1):S2-19. [Content Brief]
[8]. Kang MH, et al. Bcl-2 inhibitors: targeting mitochondrial apoptotic pathways in cancer therapy. Clin Cancer Res. 2009 Feb 15;15(4):1126-32. [Content Brief]