Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
express system | HEK293 |
product tag | C-His-Avi |
purity | > 95% as determined by Tris-Bis PAGE |
background | Immunoglobulin G (IgG) Fc receptors play a critical role in linking IgG antibody-mediated immune responses with cellular effector functions. A high resolution map of the binding site on human IgG1 for human Fc gamma RI, Fc gamma RIIA, Fc gamma RIIB, Fc gamma RIIIA, and FcRn receptors has been determined.A common set of IgG1 residues is involved in binding to all Fc gamma R; Fc gamma RII and Fc gamma RIII also utilize residues outside this common set. |
molecular weight | The protein has a predicted MW of 23.97 kDa. Due to glycosylation, the protein migrates to 40-50 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Biotinylated Mouse Fc gamma RIII/CD16 Protein 2171
$525.00 – $1,750.00
Summary
- Expression: HEK293
- Binding assay: Yes (SPR)
- Amino Acid Range: Leu32-Thr215
Biotinylated Mouse Fc gamma RIII/CD16 Protein 2171
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Immunoglobulin G (IgG) Fc receptors play a critical role in linking IgG antibody-mediated immune responses with cellular effector functions. A high resolution map of the binding site on human IgG1 for human Fc gamma RI, Fc gamma RIIA, Fc gamma RIIB, Fc gamma RIIIA, and FcRn receptors has been determined.A common set of IgG1 residues is involved in binding to all Fc gamma R; Fc gamma RII and Fc gamma RIII also utilize residues outside this common set. |
Protein names Fc gamma receptor III |
Gene names Fcgr3,Fcgr3 |
Mass 10090Da |
Target Relevance information above includes information from UniProt accession: Q5D5I8 |
The UniProt Consortium |
Publications
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We haven't added any publications to our database yet. |
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