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Anti-SCARB1 Picoband Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB |
|---|---|
| Primary Accession | Q61009 |
| Host | Rabbit |
| Reactivity | Mouse, Rat |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for Scavenger receptor class B member 1 (SCARB1) detection. Tested with WB in Mouse;Rat. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 20778 |
|---|---|
| Other Names | Scavenger receptor class B member 1, SRB1, SR-BI, Scarb1, Srb1 |
| Calculated MW | 56754 MW KDa |
| Application Details | Western blot, 0.1-0.5 µg/ml, Mouse, Rat |
| Subcellular Localization | Cell membrane ; Multi-pass membrane protein . Membrane, caveola ; Multi-pass membrane protein . Predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane, called caveolae. . |
| Tissue Specificity | Expressed primarily in liver and non-placental steroidogenic tissues. |
| Protein Name | Scavenger receptor class B member 1 |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
| Immunogen | A synthetic peptide corresponding to a sequence at the C-terminus of mouse SCARB1 (478-509aa KKGSQDKEAIQAYSESLMSPAAKGTVLQEAKL), different from the related rat sequence by one amino acid. |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
| Name | Scarb1 |
|---|---|
| Synonyms | Srb1 |
| Function | Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells (By similarity). Both isoform 1 and isoform 2 act as receptors for HDL, mediating selective uptake of cholesteryl ether and HDL-dependent cholesterol efflux (PubMed:9254074, PubMed:9614139). Also facilitates the flux of free and esterified cholesterol between the cell surface and apoB-containing lipoproteins and modified lipoproteins, although less efficiently than HDL. May be involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity (By similarity). |
| Cellular Location | Cell membrane; Multi-pass membrane protein Membrane, caveola; Multi-pass membrane protein. Note=Predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane, called caveolae. [Isoform 2]: Cell membrane. Membrane, caveola |
| Tissue Location | Expressed primarily in liver, ovary and adrenal gland, and, at lower levels in other non-placental steroidogenic tissues, including adipose tissue, mammary gland and testis (at protein level) (PubMed:8560269, PubMed:9254074, PubMed:9614139). Isoform 2 is expressed at lower levels than isoform 1 in liver, testis and adrenal gland (PubMed:9614139). At the mRNA, but not at the protein level, isoform 2 is the predominant isoform in testis (80%) (PubMed:9254074) |
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Provided below are standard protocols that you may find useful for product applications.
Background
Scavenger receptor class B member 1 (SRB1), also known as SR-BI, is a protein that in humans is encoded by the SCARB1 gene. SR-BI functions as a receptor for high-density lipoprotein. Scavenger receptor class B, type I (SR-BI) is an integral membrane protein found in numerous cell types/tissues, including the liver and adrenal. It is best known for its role in facilitating the uptake of cholesteryl esters from high-density lipoproteins in the liver. This process drives the movement of cholesterol from peripheral tissues towards the liver for excretion. This movement of cholesterol is known as reverse cholesterol transport and is a protective mechanism against the development of atherosclerosis, which is the principal cause of heart disease and stroke. SR-BI has also been identified in the livers of non-mammalian species (turtle, goldfish, shark, chicken, frog, and skate), suggesting it emerged early in vertebrate evolutionary history. The turtle also seems to upregulate SB-RI during egg development, indicating that cholesterol efflux may be at peak levels during developmental stages.
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