SCAP Antibody - BSA Free Summary
Immunogen |
This antibody was developed against Recombinant Protein corresponding to amino acids: EVWDAIEGVLCCSSEEVSSGITALVFLDKRIVAARLNGSLDFFSLETHTALSPLQFRGTPGRGSSPASPVYSSSDTVACHLTHTVPCAHQKPITALKAAAGRLVTGSQDHTLRVFRLED |
Predicted Species |
Mouse (91%), Rat (94%). Backed by our 100% Guarantee. |
Isotype |
IgG |
Clonality |
Polyclonal |
Host |
Rabbit |
Gene |
SCAP |
Purity |
Immunogen affinity purified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- Immunohistochemistry 1:20 - 1:50
- Immunohistochemistry-Paraffin 1:20 - 1:50
|
Application Notes |
For IHC-Paraffin, HIER pH 6 retrieval is recommended. |
Control Peptide |
|
Packaging, Storage & Formulations
Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
Buffer |
PBS (pH 7.2) and 40% Glycerol |
Preservative |
0.02% Sodium Azide |
Purity |
Immunogen affinity purified |
Alternate Names for SCAP Antibody - BSA Free
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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