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Product Name
Mouse CD36/SCARB3 (His & Fc Tag) recombinant protein
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Description
Binds to collagen, thrombospondin, anionic phospholipids and oxidized low-density lipoprotein (oxLDL). May function as a cell adhesion molecule. Directly mediates cytoadherence of Plasmodium falciparum parasitized erythrocytes. Binds long chain fatty acids and may function in the transport and/or as a regulator of fatty acid transport (By similarity). Receptor for thombospondins, THBS1 AND THBS2, mediating their antiangiogenic effects (By similarity). As a coreceptor for TLR4-TLR6, promotes inflammation in monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid-beta 42 binding, rapidly induces the formation of a heterodimer of TLR4 and TLR6, which is internalized and triggers inflammatory signals, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion.
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Protein name
Platelet glycoprotein 4
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Protein short names
CHDS7; PAS IV; BDPLT10; FAT; SCARB3; GP4; GPIV; GPIIIB; PASIV; GP3B; CD36; PAS-4
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Uniprot ID
Q8C6Z4
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Gene Name
Cd36
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Source/Expression Host
Human Cells
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Expression Plasmid/cDNA
A DNA sequence encoding the extracellular domain of mouse CD36 (NP_001153030.1) (Gly 30-Lys 439) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.
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Protein Species
Mouse
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Molecular weight
The recombinant mouse CD36/Fc chimera is a disulfide-linked homodimer. The reduced monomer consists of 658 amino acids and has a calculated molecular mass of 74.5 kDa. As a result of glycosylation, the apparent molecular mass of rmCD36/Fc monomer is approximately 110-120 kDa in SDS-PAGE under reducing conditions.
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Purity
> 88 % as determined by SDS-PAGE
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Activity
Measured by its binding ability in a functional ELISA. Immobilized human RSPO1 at 20 μg/ml (100 μl/well) can bind mouse CD36 Fc chimera with a linear ranger of 6.4-800 ng/ml.
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Validations
Mouse CD36 / SCARB3 Protein (His & Fc Tag) SDS-PAGE
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