B-Cell CLL/lymphoma 2 (BCL2) antibody
|Synonyms||Bcl-2, bcl-2, BCL2|
Alternatives Western Blotting (WB), Immunoprecipitation (IP), Flow Cytometry (FACS), Immunohistochemistry (Frozen Sections) (IHC (fro)), Immunofluorescence (IF)
|13 references available|
|Quantity||150 µg (0.25 mg/ml) (Variants)|
|Price||Product not available in this region.|
|Immunogen||Human Bcl-2 Recombinant Protein|
1) 51-1513GR: Purified Hamster Anti-Human Bcl-2.
Quantity: 50 µg (3 ea).
Concentration: 0.25 mg/ml.
Immunogen: Human Bcl-2 Recombinant Protein.
Isotype: Armenian Hamster IgG2, kappa.
Molecular Weight: 26 kDa.
Storage Buffer: Aqueous buffered solution containing BSA, glycerol, and Less or equal than 0.09% sodium azide.
2) 51-16526N: Jurkat Cell Lysate.
Quantity: 50 µg (1 ea).
Concentration: 1.0 mg/ml.
Storage Buffer: SDS-PAGE buffer (62mM Tris pH 6.8, 2% SDS, 0.9% b-mercaptoethanol, 0.003% bromophenol blue, 5% glycerol).
|Description||Bcl-2 is considered to be novel among proto-oncogenes because it blocks apoptosis (programmed cell death) in many cell types. Apoptosis is an active form of cellular suicide that typically requires new RNA and protein synthesis and is associated with distinct morphological changes including cell shrinkage, cytoplasm membrane blebbing, nuclear fragmentation and DNA degradation. The Bcl-2 gene was first found in t(14:18) containing follicular B-cell lymphomas. A high proportion of these lymphomas contains t(14:18) chromosomal translocations involving the human Bcl-2 gene. Translocation of Bcl-2 sequences from chromosome 18 onto the transcriptionally active immunoglobulin locus at chromosome band 14q32 in B-cells deregulates Bcl-2 gene expression, resulting in high levels of Bcl-2 mRNA and protein expression. Because Bcl-2 blocks apoptosis, it may contribute to tumorigenesis by prolonged cell survival rather than by accelerating the rate of cell proliferation. The reduced molecular weight of Bcl-2 is 26 kDa. Additional minor bands at 27-31 kDa and 18-21 kDa may also be observed.|
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Although hamster immunoglobulin isotypes have not been well defined, BD Biosciences Pharmingen has grouped Armenian and Syrian hamster IgG monoclonal antibodies according to their reactivity with a panel of mouse anti-hamster IgG mAbs.
4. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
5. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
|Molecular Weight||26 kDa|
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution containing BSA, glycerol.|
|Preservative||0.09% Sodium azide.|
|Storage||Store both the hamster anti-human Bcl-2 antibody and the Jurkat cell lysate undiluted at -20°C.|
|Research Area||Cancer, Apoptosis/Necrosis|
|Restrictions||For Research Use only|
Hockenbery, Zutter, Hickey et al.: "BCL2 protein is topographically restricted in tissues characterized by apoptotic cell death." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, Issue 16, pp. 6961-5, 1991 (PubMed).
McDonnell, Nunez, Platt et al.: "Deregulated Bcl-2-immunoglobulin transgene expands a resting but responsive immunoglobulin M and D-expressing B-cell population." in: Molecular and cellular biology, Vol. 10, Issue 5, pp. 1901-7, 1990 (PubMed).
Hockenbery, Nuñez, Milliman et al.: "Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death." in: Nature, Vol. 348, Issue 6299, pp. 334-6, 1991 (PubMed).
Hockenbery, Oltvai, Yin et al.: "Bcl-2 functions in an antioxidant pathway to prevent apoptosis." in: Cell, Vol. 75, Issue 2, pp. 241-51, 1993 (PubMed).
Batistatou, Merry, Korsmeyer et al.: "Bcl-2 affects survival but not neuronal differentiation of PC12 cells." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 13, Issue 10, pp. 4422-8, 1993 (PubMed).
Yang, Zha, Jockel et al.: "Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death." in: Cell, Vol. 80, Issue 2, pp. 285-91, 1995 (PubMed).
Núñez, Merino, Grillot et al.: "Bcl-2 and Bcl-x: regulatory switches for lymphoid death and survival." in: Immunology today, Vol. 15, Issue 12, pp. 582-8, 1995 (PubMed).
Chiou, Rao, White: "Bcl-2 blocks p53-dependent apoptosis." in: Molecular and cellular biology, Vol. 14, Issue 4, pp. 2556-63, 1994 (PubMed).
Yin, Oltvai, Korsmeyer: "BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax." in: Nature, Vol. 369, Issue 6478, pp. 321-3, 1994 (PubMed).
Nguyen, Millar, Yong et al.: "Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence." in: The Journal of biological chemistry, Vol. 268, Issue 34, pp. 25265-8, 1994 (PubMed).
Oltvai, Milliman, Korsmeyer: "Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death." in: Cell, Vol. 74, Issue 4, pp. 609-19, 1993 (PubMed).
Veis, Sentman, Bach et al.: "Expression of the Bcl-2 protein in murine and human thymocytes and in peripheral T lymphocytes." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 151, Issue 5, pp. 2546-54, 1993 (PubMed).
Martin, Veis, Korsmeyer et al.: "Latent membrane protein of Epstein-Barr virus induces cellular phenotypes independently of expression of Bcl-2." in: Journal of virology, Vol. 67, Issue 9, pp. 5269-78, 1993 (PubMed).