LSS Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P48449 |
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Clone Names | 81202087 |
Gene ID | 4047 |
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Other Names | Lanosterol synthase, 3-epoxysqualene--lanosterol cyclase, Oxidosqualene--lanosterol cyclase, OSC, hOSC, LSS, OSC |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP9165b was selected from the C-term region of human LSS. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
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 | LSS |
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Synonyms | OSC |
Function | Key enzyme in the cholesterol biosynthesis pathway. Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus (PubMed:14766201, PubMed:7639730, PubMed:26200341). Through the production of lanosterol may regulate lens protein aggregation and increase transparency (PubMed:26200341). |
Cellular Location | Endoplasmic reticulum membrane; Peripheral membrane protein |
Tissue Location | Widely expressed. Expressed in the hair bulb, the outer root sheath and hair matrix of the hair follicle epithelium. Also detected in dermal papilla, epidermis, sweat glands, sebaceous glands, and blood vessels. |
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Provided below are standard protocols that you may find useful for product applications.
Background
The protein catalyzes the conversion of (S)-2,3 oxidosqualene to lanosterol. The encoded protein is a member of the terpene cyclase/mutase family and catalyzes the first step in the biosynthesis of cholesterol, steroid hormones, and vitamin D.
References
Dang,H., et.al., J. Biol. Chem. 284 (10), 6218-6226 (2009)Lu,Y., et.al., J. Lipid Res. 49 (12), 2582-2589 (2008)
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