|Application ||WB, E|
|Calculated MW||26353 Da|
|Antigen Region||201-230 aa|
|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|
|Target/Specificity||This EBP antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 201-230 amino acids from the C-terminal region of human EBP.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||EBP Antibody(C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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.
The protein encoded by this gene is an integral membrane protein of the endoplasmic reticulum. It is a high affinity binding protein for the antiischemic phenylalkylamine Ca2+ antagonist [3H]emopamil and the photoaffinity label [3H]azidopamil. It is similar to sigma receptors and may be a member of a superfamily of high affinity drug-binding proteins in the endoplasmic reticulum of different tissues. This protein shares structural features with bacterial and eukaryontic drug transporting proteins. It has four putative transmembrane segments and contains two conserved glutamate residues which may be involved in the transport of cationic amphiphilics. Another prominent feature of this protein is its high content of aromatic amino acid residues (>23%) in its transmembrane segments. These aromatic amino acid residues have been suggested to be involved in the drug transport by the P-glycoprotein. Mutations in this gene cause Chondrodysplasia punctata 2 (CDPX2; also known as Conradi-Hunermann syndrome).
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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