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Description
NPC1 His Tag Protein, HumanProduct Specification Species Human Synonyms NPC1, NPC Protein Accession O15118 1 Amino Acid Sequence Arg372 Phe622, with N terminal His Expression System HEK293 Molecular Weight 40 50 kDa (Reducing) Purity 95% by SDS PAGE & >95% by SEC HPLC Endotoxin <0. 1EU g Conjugation Unconjugated Tag His Tag Physical Appearance Lyophilized Powder Storage Buffer PBS, pH7. 4,5% trehalose Reconstitution Reconstitute at 0. 1 1 mg ml according to the size in
Product Specification
| Species | Human |
| Synonyms | NPC1, NPC Protein |
| Accession | O15118-1 |
| Amino Acid Sequence | Arg372-Phe622, with N-terminal His |
| Expression System | HEK293 |
| Molecular Weight | 40-50 kDa (Reducing) |
| Purity | ＞95% by SDS-PAGE & >95% by SEC-HPLC |
| Endotoxin | <0.1EU/μg |
| Conjugation | Unconjugated |
| Tag | His Tag |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | PBS, pH7.4,5% trehalose |
| Reconstitution | Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation. |
| Stability & Storage | · 12 months from date of receipt, lyophilized powder stored at -20 to -80℃. · 3 months, -20 to -80℃ under sterile conditions after reconstitution. · 1 week, 2 to 8℃ under sterile conditions after reconstitution. · Please avoid repeated freeze-thaw cycles. |
| Reference | J P Davies, Y A Ioannou. Dupilumab for the treatment of asthma. Topological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and sterol regulatory element binding protein cleavage-activating protein.J Biol Chem. 2000 Aug 11;275(32):24367-74. |
Background
The Niemann-Pick C1 (NPC1) protein is predicted to be a polytopic glycoprotein, and it contains a region with extensive homology to the sterol-sensing domains (SSD) of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-R) and sterol regulatory element binding protein cleavage-activating protein (SCAP). To aid the functional characterization of NPC1, a model of NPC1 topology was evaluated by expression of epitope-tagged NPC1 proteins and investigation of epitope accessibility in selectively permeabilized cells. These results were further confirmed by expression of NPC1 and identification of glycosylated domains that are located in the lumen of the endoplasmic reticulum. Our data indicate that this glycoprotein contains 13 transmembrane domains, 3 large and 4 small luminal loops, 6 small cytoplasmic loops, and a cytoplasmic tail. Furthermore, our data show that the putative SSD of NPC1 is oriented in the same manner as those of HMG-R and SCAP, providing strong evidence that this domain is functionally important.
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