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Purified Mouse Anti-Human Bcl-2

BD Pharmingen™ Purified Mouse Anti-Human Bcl-2

Clone 4D7

(RUO)
Purified Mouse Anti-Human Bcl-2
Western blot analysis of bcl-2. Lysate from Jurkat cells was probed with anti-bcl-2 (clone 4D7, Comp. No. 51- 1483GR) at concentrations of 1.0 (lane 1), 0.5 (lane 2), and 0.25 µg/ml (lane 3). Bcl-2 is identified as a band of 26 kDa.
Western blot analysis of bcl-2. Lysate from Jurkat cells was probed with anti-bcl-2 (clone 4D7, Comp. No. 51- 1483GR) at concentrations of 1.0 (lane 1), 0.5 (lane 2), and 0.25 µg/ml (lane 3). Bcl-2 is identified as a band of 26 kDa.
Product Details
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BD Pharmingen™
Human (QC Testing)
Western blot (Routinely Tested), Electron microscopy, Immunoprecipitation (Reported)
RUO
AB_394045


Description

The bcl-2 gene was first discovered in t(14:18) follicular lymphomas. 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. Bcl-2 protein blocks apoptosis (programmed cell death), and thereby may contribute to tomorigenesis by prolonging  cell survival rather than by accelerating the rate of cell proliferation. Abundant evidence implicates this protein in the suppression of apoptosis in many types of cells. Bcl-2 is an intracellular membrane protein and resides primarily in the nuclear envelope, outer mitochondrial membrane and endoplasmic reticulum. The reduced molecular weight of Bcl-2 is 26 kDa.

Clone 4D7 recognizes human Bcl-2. A synthetic peptide containing amino acids 61-76 of the human Bcl-2 protein was used as immunogen. This peptide sequence differs from that of mouse Bcl-2 and hence 4D7 does not cross-react with mouse. 4D7 recognizes Bcl-2 as a 26 kDa band; however, additional higher molecular weight bands have been observed in some cell types. These bands may represent oligomers of Bcl-2, which have been reported to occur with members of the Bcl-2 family during the preparation of nonionic detergent extracts.

Preparation And Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at -20°C.

Recommended Assay Procedures

Jurkat control lysate [50 µg (1 µg/µl)] is provided as a western blot positive control (Comp. No. 51-16526N; store lysate at -20°C). Additional control lysate (Cat. No. 611451) is sold separately. For immunohistochemistry of paraffin-embedded sections, the monoclonal mouse anti-human Bcl-2 (clone Bcl-2/100, Cat. No. 551109) or clone 7/Bcl-2, (Cat. No. 610539)  is recommended.

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
  3. 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.
  4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
551097 Rev. 4
Components
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Description Quantity/Size Part Number EntrezGene ID
Purified Mouse Anti-Human Bcl-2 50 µg (3 ea) 51-1483GR N/A
Jurkat Cell Lysate 50 µg (1 ea) 51-16526N N/A
551097 Rev. 4
Citations & References
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Development References (10)

  1. Hsu YT, Youle RJ. Nonionic detergents induce dimerization among members of the Bcl-2 family. J Biol Chem. 1997; 272(21):13829-13834. (Biology). View Reference
  2. Krajewski S, Tanaka S, Takayama S, Schibler MJ, Fenton W, Reed JC. Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res. 1993; 53(19):4701-4714. (Clone-specific: Electron microscopy). View Reference
  3. Pezzella F, Tse AG, Cordell JL, Pulford KA, Gatter KC, Mason DY. Expression of the bcl-2 oncogene protein is not specific for the 14;18 chromosomal translocation. Am J Pathol. 1990; 137(2):225-232. (Biology). View Reference
  4. Reed JC, Meister L, Tanaka S, et al. Differential expression of bcl2 protooncogene in neuroblastoma and other human tumor cell lines of neural origin. Cancer Res. 1991; 51(24):6529-6538. (Biology). View Reference
  5. Reed JC, Tanaka S, Cuddy M, et al. A strategy for generating monoclonal antibodies against recombinant baculovirus-produced proteins: application to the Bcl-2 oncoprotein. Anal Biochem. 1992; 205(1):70-76. (Immunogen: Western blot). View Reference
  6. Reed JC, Tsujimoto Y, Alpers JD, Croce CM, Nowell PC. Regulation of bcl-2 proto-oncogene expression during normal human lymphocyte proliferation. Science. 1987; 236(4806):1295-1299. (Biology). View Reference
  7. Tanaka S, Saito K, Reed JC. Structure-function analysis of the Bcl-2 oncoprotein. Addition of a heterologous transmembrane domain to portions of the Bcl-2 beta protein restores function as a regulator of cell survival. J Biol Chem. 1993; 268(15):10920-10926. (Clone-specific: Immunoprecipitation). View Reference
  8. Teixeira C, Reed JC, Pratt MA. Estrogen promotes chemotherapeutic drug resistance by a mechanism involving Bcl-2 proto-oncogene expression in human breast cancer cells. Cancer Res. 1995; 55(17):3902-3907. (Clone-specific: Western blot). View Reference
  9. Tsujimoto Y, Cossman J, Jaffe E, Croce CM. Involvement of the bcl-2 gene in human follicular lymphoma. Science. 1985; 228(4706):1440-1443. (Biology). View Reference
  10. Wang HG, Millan JA, Cox AD, et al. R-Ras promotes apoptosis caused by growth factor deprivation via a Bcl-2 suppressible mechanism. J Cell Biol. 1995; 129(4):1103-1114. (Clone-specific: Immunoprecipitation). View Reference
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551097 Rev. 4

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For Research Use Only. Not for use in diagnostic or therapeutic procedures.