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Purified Mouse Anti-SREBP-1
Product Details
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BD Pharmingen™
Human (QC Testing), Hamster (Tested in Development)
Mouse IgG1, κ
Human SREBP-1 aa. 301-407
Western blot (Routinely Tested), Immunoprecipitation (Tested During Development)
0.5 mg/ml
Aqueous buffered solution containing ≤0.09% sodium azide.

Preparation And Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at 4°C.

Recommended Assay Procedures

The IgG-2A4 antibody may be used for western blot analysis (0.5 to 1 µg/ml) and immunoprecipitation (2 µg/ml). U-937 human histiocytic lymphoma cells (ATCC CRL-1593) or HeLa human cervical carcinoma cells (ATCC CCL-2) are recommended as positive controls for these applications.

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to 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.
557036 Rev. 4
Antibody Details
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SREBP-1 and -2 (sterol-regulatory element binding proteins-1 and -2) are transcription factors which participate in the control of cholesterol homeostasis. SREBPs proteins, which are attached to the endoplasmic reticulum and nuclear envelope, are proteolytically cleaved and thus activated in response to conditions of low cellular sterol. Upon activation of SREBP-1 or -2, an ~480-500 amino acid, N-terminal cleavage fragment of these proteins enters the nucleus and activates transcription of enzymes and other proteins required for cholesterol synthesis. Proteases which cleave SREBPs have been identified and include SCA (SREBP-cleavage activity), as well as a key regulator of apoptotic pathways, caspase-3. SREBP proteins containing point mutations at caspase-3 cleavage sites (Asp460 in SREBP-1 and Asp468 in SREBP-2) do not become cleaved following induction of apoptosis, suggesting that SREBPs may play some role in apoptotic processes. However, sterol-regulated vs. apoptosis-associated cleavage of SREBP proteins appears to be independantly regulated. On SDS-PAGE, sterol-regulated cleavage fragments of SREBP proteins migrate more slowly (i.e., higher molecular weight) than do staurosporin-induced fragments. In addition, staurosporin-induced SREBP cleavage products may appear as a doublet, with the upper band representing a phosphorylated form of SREBP. On SDS-PAGE, full length, precursor forms of SREBP-1 and -2 migrate at ~125 kDa, while proteolytic cleavage fragments may be observed as a cluster of bands between 60 - 70 kDa. The IgG-2A4 antibody recognizes human and hamster SREBP-1. The antibody recognizes the N-terminal (basic helix-loop-helix) domain of human SREBP-1. A fusion protein containing N-terminal amino acids 301-407 (the bHLH/leucine zipper domain), was used as immunogen. The antibody recognizes both the 125 kDa precursor and 60-70 kDa mature, cleaved forms of SREBP-1.

557036 Rev. 4
Format Details
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Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
557036 Rev.4
Citations & References
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View product citations for antibody "557036" on CiteAb

Development References (4)

  1. Sakai J, Nohturfft A, Cheng D, Ho YK, Brown MS, Goldstein JL. Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein. J Biol Chem. 1997; 272(32):20213-20221. (Clone-specific: Western blot). View Reference
  2. Sato R, Yang J, Wang X, et al. Assignment of the membrane attachment, DNA binding, and transcriptional activation domains of sterol regulatory element-binding protein-1 (SREBP-1). J Biol Chem. 1994; 269(25):17267-17273. (Immunogen). View Reference
  3. Wang X, Pai JT, Wiedenfeld EA, et al. Purification of an interleukin-1 beta converting enzyme-related cysteine protease that cleaves sterol regulatory element-binding proteins between the leucine zipper and transmembrane domains. J Biol Chem. 1995; 270(30):18044-18050. (Biology). View Reference
  4. Wang X, Zelenski NG, Yang J, Sakai J, Brown MS, Goldstein JL. Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis. EMBO J. 1996; 15(5):1012-1020. (Clone-specific: Western blot). View Reference
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557036 Rev. 4

Please refer to Support Documents for Quality Certificates

Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described

Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

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