SOAT2 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O75908 |
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Clone Names | 100525313 |
Gene ID | 8435 |
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Other Names | Sterol O-acyltransferase 2, Acyl-coenzyme A:cholesterol acyltransferase 2, ACAT-2, Cholesterol acyltransferase 2, SOAT2, ACACT2, ACAT2 |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | SOAT2 (HGNC:11178) |
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Synonyms | ACACT2, ACAT2 |
Function | Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol (PubMed:16647063, PubMed:11294643). Plays a role in lipoprotein assembly and dietary cholesterol absorption (PubMed:11294643). Utilizes oleoyl-CoA ((9Z)- octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl- CoA) as substrates (PubMed:11294643). May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa (PubMed:11294643). |
Cellular Location | Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O88908}; Multi-pass membrane protein |
Tissue Location | Expression seems confined in hepatocytes and enterocytes. |
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Provided below are standard protocols that you may find useful for product applications.
Background
SOAT2 plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.
References
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Guey, L.T., et al. Eur. Urol. 57(2):283-292(2010)Hosgood, H.D. III, et al. Respir Med 103(12):1866-1870(2009)Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)Chen, S.N., et al. BMC Med. Genet. 10, 111 (2009) :
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