Reactivity | MuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. Immobilized Recombinant Mouse SR‑AI/MSR at 5 µg/mL (100 µL/well) can bind biotinylated advanced glycation endproducts of bovine serum albumin (AGE-BSA) with a linear range of 2-100 ng/mL. |
Source | Mouse myeloma cell line, NS0-derived mouse SR-AI/MSR protein Trp79-Ser454, with an N-terminal 9-His tag |
Accession # | |
N-terminal Sequence | His |
Protein/Peptide Type | Recombinant Proteins |
Gene | Msr1 |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 42 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 60-70 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
The scavenger receptor (SR) family comprises a group of functionally defined membrane receptors that share the common ability to bind and internalize modified forms of Low Density Lipoproteins (mLDL) (1 - 3). Family members are classified alphabetically. The A class include four proteins: the three subtypes of SR-A (AI, AII, and AIII) that are generated by alternative splicing of the same gene, and a structurally similar protein named MARCO (4). All A class SRs are multidomain trimeric type II membrane proteins. SR-AI has an N-terminal cytoplasmic domain, a transmembrane domain, a spacer domain, an alpha -helical coiled coil, a collagen-like domain and a C-terminal cysteine-rich domain. SR-A is expressed by most tissue macrophages, dendritic cells and Kupffer cells. It is also highly expressed by microglia in neonatal as well as Alzheimer’ Disease brains. SR-AI binds a broad range of polyanionic ligands including modified proteins (e.g. Oxidized, acetylated or maleylated LDL, Advanced glycation end-product proteins), polyribonucleotides (polyguanosine and polyinosine), polysaccharides (dextran sulfate, fucoidan), phospholipids (phosphatidylserine), bacterial products (lipopolysaccharide and lipoteichoic acid) and selected chemical compounds (silica, crocidolite asbestos). The ligand-binding region has been localized to a positively charged region in the carboxyl end of the collagen-like domain. Based on its ligand binding characteristics, SR-AI is implicated in many physiological and pathophysiological functions. Studies using SR-A knockout mouse have also suggested roles of SR-A in atherogenesis, host defense and innate immunity, acquired immune responses, macrophage adhesion, and phagocytosis of apoptotic cells (1 - 3).
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