mouse monoclonal IgG2b; SCAP Antibody (9D5) is an IgG2b κ mouse monoclonal SCAP antibody (also designated SREBF Chaperone antibody, or Sterol Regulatory Element-Binding Protein Cleavage-Activating Protein antibody) that detects the SCAP protein of hamster origin by WB and IP. SCAP Antibody (9D5) is available as both the non-conjugated anti-SCAP antibody form, as well as multiple conjugated forms of anti-SCAP antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. The transcription factors SREBPs (sterol regulatory element binding proteins) span the ER membrane, and in response to sterol depletion, the N-terminal domain of SREBPs are proteolytically activated, released from the membrane and then translocate to the nucleus where they induce the expression of genes regulating cholesterol metabolism. This proteolytic activation requires the sequential cleavage of SREBPs at Site-1, within the lumen of the ER, followed by cleavage at Site-2, within the first transmembrane domain. The cleavage at Site-1 separates the N-terminal and C-terminal domains of the protein and it requires the serine protease, S1P (Site-1 protease). Site-2 is subsequently processed by a putative zinc metalloprotease S2P, which releases the activated N-terminal domain for nuclear translocation (2,5). This proteolytic pathway is tightly regulated by sterol levels and is under the control of SCAP (SREBP cleavage-activating protein). SCAP, a sterol sensor, is latently bound to the C-terminal regulatory domains of the SREBPs, and it regulates cleavage of SREBPs at Site-1 (1,7). Sterol levels influence the activity of SCAP, as SCAP is activated only in sterol-depleted cells, and it is inhibited by sterol accumulation.