Recombinant Human Fc gamma RIIA/CD32a Avi His Protein, CF Summary
Additional Information |
Biotinylated Avi-tag His-tag |
Details of Functionality |
Measured by its binding ability in a functional ELISA. 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 binds with an ED50 of 1.00-8.00 μg/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human Fc gamma RIIA/CD32a protein Human Fc gamma RIIA (Ala36-Ile218) Accession # AAA35827.1 | Avi-tag | 6-His tag | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Ala36 |
Structure / Form |
Biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
24 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. |
SDS-PAGE |
32-39 kDa, under reducing conditions. |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Fc gamma RIIA/CD32a Avi His Protein, CF
Background
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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