This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogen
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.
EBP
Reaktivität: Human
WB
Wirt: Kaninchen
Polyclonal
unconjugated
Applikationshinweise
WB: 1:1000. WB: 1:1000
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Buffer
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C,-20 °C
Haltbarkeit
6 months
Ausavarat, Tanpaiboon, Tongkobpetch, Suphapeetiporn, Shotelersuk: "Two novel EBP mutations in Conradi-Hünermann-Happle syndrome." in: European journal of dermatology : EJD, Vol. 18, Issue 4, pp. 391-3, (2008) (PubMed).
Lu, Dollé, Imholz, van t Slot, Verschuren, Wijmenga, Feskens, Boer: "Multiple genetic variants along candidate pathways influence plasma high-density lipoprotein cholesterol concentrations." in: Journal of lipid research, Vol. 49, Issue 12, pp. 2582-9, (2008) (PubMed).
Steijlen, van Geel, Vreeburg, Marcus-Soekarman, Spaapen, Castelijns, Willemsen, van Steensel: "Novel EBP gene mutations in Conradi-Hünermann-Happle syndrome." in: The British journal of dermatology, Vol. 157, Issue 6, pp. 1225-9, (2007) (PubMed).
Target
EBP
(Emopamil Binding Protein (Sterol Isomerase) (EBP))
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).