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EBP Antibody(C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q15125 |
|---|---|
| Clone Names | 100318237 |
| Gene ID | 10682 |
|---|---|
| Other Names | 3-beta-hydroxysteroid-Delta(8), Delta(7)-isomerase, Cholestenol Delta-isomerase, Delta(8)-Delta(7) sterol isomerase, D8-D7 sterol isomerase, Emopamil-binding protein, EBP |
| 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 | EBP (HGNC:3133) |
|---|---|
| Function | Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. |
| Cellular Location | Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus envelope Cytoplasmic vesicle. Note=During interphase, detected on the endoplasmic reticulum and the nuclear envelope. During mitosis, detected on cytoplasmic vesicles |
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Provided below are standard protocols that you may find useful for product applications.
Background
The protein encoded by this gene is an integral membraneprotein of the endoplasmic reticulum. It is a high affinity bindingprotein for the antiischemic phenylalkylamine Ca2+ antagonist[3H]emopamil and the photoaffinity label [3H]azidopamil. It issimilar to sigma receptors and may be a member of a superfamily ofhigh affinity drug-binding proteins in the endoplasmic reticulum ofdifferent tissues. This protein shares structural features withbacterial and eukaryontic drug transporting proteins. It has fourputative transmembrane segments and contains two conservedglutamate residues which may be involved in the transport ofcationic amphiphilics. Another prominent feature of this protein isits high content of aromatic amino acid residues (>23%) in itstransmembrane segments. These aromatic amino acid residues havebeen suggested to be involved in the drug transport by theP-glycoprotein. Mutations in this gene cause Chondrodysplasiapunctata 2 (CDPX2; also known as Conradi-Hunermann syndrome).
References
Lu, Y., et al. J. Lipid Res. 49(12):2582-2589(2008)Ausavarat, S., et al. Eur J Dermatol 18(4):391-393(2008)Steijlen, P.M., et al. Br. J. Dermatol. 157(6):1225-1229(2007)Guggenberger, C., et al. J. Steroid Biochem. Mol. Biol. 104 (3-5), 105-109 (2007) :Rakheja, D., et al. Pediatr. Dev. Pathol. 10(2):142-148(2007)
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