Reactivity | MuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | |||||||
Source | Chinese Hamster Ovary cell line, CHO-derived mouse CD36/SR-B3 protein
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Accession # | |||||||
N-terminal Sequence | Gly30 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | Cd36 |
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Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 72.9 kDa (monomer). 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 | 100-130 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 | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
CD36 (alternatively known as platelet membrane glycoprotein IV (GPIV), thrombospondin receptor, fatty acid translocase (FAT), and scavenger receptor class B, member 3 (SR-B3)) is an 88 kDa, integral membrane glycoprotein that belongs to the class B scavenger receptor family (1, 2). The molecule is described as being ditopic, with two transmembrane segments connected by an extracellular loop (3). Mouse CD36 is synthesized as a 472 amino acid (aa) protein that contains a 6 aa N-terminal cytoplasmic domain, a 22 aa N-terminal transmembrane segment, a 420 aa extracellular “loop”, a 22 aa C-terminal transmembrane segment, and a 9 aa C-terminal cytoplasmic tail (4). Both cytoplasmic tails are palmitoylated, with the C-terminal tail involved in oxidized LDL binding (5, 6). With respect to the extracellular loop, the N-terminal region is believed to bind both thrombospondin-1 and Plasmodium-infected erythrocytes. Other ligands for CD36 include long-chain fatty acids, collagen, phospholipids and apoptotic cells (1). The extracellular loop of mouse CD36 is 94%, 92%, 84% and 84% aa identical to the extracellular loops of rat, hamster, human and bovine CD36, respectively. Cells known to express CD36 include capillary endothelium, adipocytes, skeletal muscle cells, intestinal epithelium, smooth muscle cells and hematopoietic cells such as RBC’s, platelets and monocytes (1). On the surface of cells, CD36 is suggested to exist as a dimer in response to ligation (7). CD36 is reported to regulate fatty uptake, act as an angiogenic with TSP-1, and participate in the clearance of apoptotic phagocytes (1, 8).
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