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ASGR1 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P07306 |
|---|---|
| Clone Names | 100528078 |
| Gene ID | 432 |
|---|---|
| Other Names | Asialoglycoprotein receptor 1, ASGP-R 1, ASGPR 1, C-type lectin domain family 4 member H1, Hepatic lectin H1, HL-1, ASGR1, CLEC4H1 |
| 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 | ASGR1 |
|---|---|
| Synonyms | CLEC4H1 |
| Function | Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N- acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. |
| Cellular Location | [Isoform H1a]: Membrane; Single-pass type II membrane protein |
| Tissue Location | Expressed exclusively in hepatic parenchymal cells. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Partially deglycosylated plasma glycoproteins andimmunoglobulin IgA2 allotypes are efficiently and specificallyremoved from circulation by a receptor-mediated process. Theasialoglycoprotein receptor binds to desialylated(galactosyl-terminal) glycoproteins. It transports theseglycoproteins via a series of membrane vesicles and tubules to anacidic-sorting organelle where the receptor and ligand dissociate.Then the receptor is recycled back to the cell surface and theligand is transported to the lysosomes for degradation.Alternatively spliced transcript variants encoding distinctisoforms have been identified.
References
Yang, J., et al. Arch. Virol. 155(6):881-888(2010)Liu, J., et al. PLoS ONE 5 (9), E12934 (2010) :Sorensen, A.L., et al. Blood 114(8):1645-1654(2009)Oh, J.H., et al. Mamm. Genome 16(12):942-954(2005)Yik, J.H., et al. J. Biol. Chem. 277(43):40844-40852(2002)
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