Recombinant Human Fc gamma RIIA/CD32a Avi His Protein, CF
Recombinant Human Fc gamma RIIA/CD32a Avi His Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
Human Fc gamma RIIA (Ala36-Ile218) Accession # AAA35827.1 | Avi-tag | 6-His tag |
N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
AVI1330
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
When Human IgG is immobilized at 5.00 µg/mL (100 µL/well), Biotinylated Recombinant Human Fc gamma RIIA/CD32a Avi-tag His-tag Protein (Catalog # AVI1330) binds with an ED50 of 1.00-8.00 μg/mL.
2 μg/lane of Biotinylated Recombinant Human Fc gamma RIIA/CD32a Avi-tag His-tag Protein (Catalog # AVI1330) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 32-39 kDa.
Reconstitution Calculator
Background: Fc gamma RIIA/CD32a
Receptors for the Fc region of IgG (Fc gamma R) are members of the Ig superfamily that function in the activation or inhibition of immune responses. Three classes of human Fc gamma Rs: RI (CD64), RII (CD32), and RIII (CD16), which generate multiple isoforms, are recognized (1-3). The activating-type receptor either has or associates non-covalently with an accessory subunit (FcR gamma or zeta chain) that has an immunoreceptor tyrosine-based activation motif (ITAM) in its cytoplasmic domain. In contrast, the inhibitory receptor (Fc gamma RIIB) has a built-in immunoreceptor tyrosine-based inhibitory motif (ITIM) in its own cytoplasmic domain. Fc gamma RI is a high-affinity receptor that binds monomeric IgG, and Fc gamma RII and RIII are low-affinity receptors that bind aggregated or immune complexed IgG (IC). The extracellular domain of human Fc gamma RIIA shares approximately 90% amino acid sequence homology with human Fc gamma RIIB and Fc gamma RIIC. Fc gamma RIIA is expressed on many immune cell types (macrophage, neutrophil, eosinophils, platelets, dendritic cells and Langerhan cells) where inhibitory ITIM-bearing receptors may also be co-expressed and co-engaged by specific ligands. Signaling through Fc gamma RIIA results in the initiation of inflammatory responses (cytolysis, phagocytosis, degranulation and cytokine production) that can be modulated by signals from the inhibitory receptors. The strength of the signal is dependent on the ratio of expression of the activating and inhibitory receptors. Besides IC, Fc gamma RII A also binds C-reactive protein (CRP) (4, 5). Two allelic variants (R167 and H167) of Fc gamma RIIA that differ in their ability to ligate human IgG2 or CRP exist. The H167 allele has been found to have a protective effect against lupus nephritis. Our Avi-tag Biotinylated Fc gamma RIIA/CD32a protein features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- van de Winkel, J. and P. Capes (1993) Immunol. Today 14:215.
- Ravetch, J.V. and S. Bolland (2001) Annu. Rev. Immunol. 19:275.
- Takai, T. (2002) Nature Rev. Immunol. 2:580.
- Chi, M. et al. (2002) J. Immunol. 168:1413.
- Zuniga, R. et al. (2003) Arthritis Rheum. 48:460.
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