Western Blot:SCAP Antibody [NBP2-04113] -Whole cell lysate (10 ug) from HEK293T, Hep-G2, HeLa,Jurkat, and K-562 cells prepared using NETN lysis buffer.Antibody: Affinity purified rabbit anti-SCAP antibody used for WB at ...read more
Immunoprecipitation:SCAP Antibody [NBP2-04113] -Whole cell lysate (1.0 mgper IP reaction; 20% of IP loaded) from HEK293T cellsprepared using NETN lysis buffer. Antibodies: Affinitypurified rabbit anti-SCAP antibody ...read more
The immunogen recognized by this antibody maps to a region between residue 450 and 500 of human Sterol Regulatory Element Binding Protein Ceavage-Activating Protein using the numbering given in entry NP_036367.2 (GeneID 22937).
Isotype
IgG
Clonality
Polyclonal
Host
Rabbit
Gene
SCAP
Purity
Immunogen affinity purified
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sterol regulatory element binding protein cleavage-activating protein
Background
Sterol regulatory element binding protein (SREBP) cleavage-activating protein (SCAP) is a molecular chaperone that plays a role in the biosynthesis of cholesterol and triglycerides (1). SCAP is a membrane protein that helps shuttle SREBP from the endoplasmic reticulum (ER) via coat protein II (COPII) vesicles to the golgi where SREBP is cleaved via protease S1P and S2P, becomes activated, and is translocated to the nucleus for transcription (1-3). The SCAP protein has a theoretical molecular weight of 140 kDa and is comprised of 1276 amino acids with an N-terminal domain containing 8 transmembrane alpha helices, where transmembrane 2-6 consist of a sterol-sensing domain, and a C-terminal domain with WD40 motif repeats (1,3). The SCAP-SREBP association plays a pivotal role in regulating lipid metabolism and lipogenesis (1,4). SREBP activation via SCAP is associated with accumulation of triglycerides and cholesterol leading to metabolic disorders including diabetes, atherosclerosis, and nonalcoholic fatty liver disease (NAFLD) (1,4). Animal models have revealed that inhibition or blocking of SCAP using antagonists may be a potential therapeutic target for hyperlipidemia and hypertriglyceridemia (1,4).
References
1. Lee, S. H., Lee, J. H., & Im, S. S. (2020). The cellular function of SCAP in metabolic signaling. Experimental & molecular medicine, 52(5), 724-729. https://doi.org/10.1038/s12276-020-0430-0
2. Cheng, X., Li, J., & Guo, D. (2018). SCAP/SREBPs are Central Players in Lipid Metabolism and Novel Metabolic Targets in Cancer Therapy. Current topics in medicinal chemistry, 18(6), 484-493. https://doi.org/10.2174/1568026618666180523104541
3. Brown, M. S., Radhakrishnan, A., & Goldstein, J. L. (2018). Retrospective on Cholesterol Homeostasis: The Central Role of Scap. Annual review of biochemistry, 87, 783-807. https://doi.org/10.1146/annurev-biochem-062917-011852
4. Moon Y. A. (2017). The SCAP/SREBP Pathway: A Mediator of Hepatic Steatosis. Endocrinology and metabolism (Seoul, Korea), 32(1), 6-10. https://doi.org/10.3803/EnM.2017.32.1.6
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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