Recombinant Rat Fc gamma RIIA/CD32a Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Rat Fc gamma RIIA/CD32a is immobilized on
an anti-His Tag Antibody coated plate, it binds Biotinylated Rat IgG. The
concentration
of Biotinylated Rat IgG that
produces 50% of the optimal binding response is 1.25-6.25 μg/mL |
Source |
Human embryonic kidney cell, HEK293-derived rat Fc gamma RIIA/CD32a protein Asp37-His220, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Asp37 |
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 |
22 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 |
29-44 kDa, 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. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 100 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 Rat Fc gamma RIIA/CD32a Protein, CF
Background
Receptors
for the Fc region of IgG (Fc gamma Rs) are members of the Ig superfamily that
function in the activation or inhibition of immune responses such as
degranulation, phagocytosis, cytokine release, and B cell proliferation. There are three classes of Fc gamma Rs, based on close relationships in their
extracellular domains: Fc gamma RI/CD64,
Fc gamma RII/CD32, and Fc gamma RIII/CD16.
Each group may be encoded by multiple genes and exists in different
isoforms depending on species and cell type (1-3). In humans, there are three
Fc gamma RII genes that encode multiple transcripts that
differ in their cytoplasmic tails. Only
one murine Fc gamma RII
gene has been identified which has two transcripts that are homologues of the
human Fc gamma RIIB (4).
Fc gamma RIIA
is not expressed in mice. Approximately
40 kDa, Fc gamma RIIA
is a type 1 transmembrane glycoprotein that is expressed on different cell
types, including, neutrophils, monocytes, dendritic cells, and is the only Fc gamma R expressed on human platelets (5). The mature protein consists of an extracellular
domain (ECD), a transmembrane segment, and a cytoplasmic domain. Within the
ECD, rat Fc gamma RIIA
shares 52% amino acid sequence identity with human Fc gamma RIIA. The Fc gamma RI/CD64 proteins are high affinity receptors
(~10
-8-10
-9 M) capable of binding monomeric IgG,
whereas the Fc gamma RII/CD32
and Fc gamma RIII/CD16 proteins bind IgG with lower affinities
(~10
-6-10
-7 M) only recognizing IgG aggregates
surrounding multivalent antigens (1, 6). Fc gamma Rs that deliver an activating
signal either have an intrinsic immunoreceptor tyrosine-based activation motif
(ITAM) within their cytoplasmic domains or associate with one of the
ITAM-bearing adapter subunits, Fc R gamma or zeta (3, 7). The only
inhibitory member in human and mouse, Fc gamma RIIb, has an intrinsic
cytoplasmic immunoreceptor tyrosine-based inhibitory motif (ITIM). The
coordinated functioning of activating and inhibitory receptors is necessary for
successful initiation, amplification, and termination of immune responses (7).
-
Van de Winkel, J. and P. Capel (1993) Immunol. Today. 14:215.
- Raghavan, M. and P. Bjorkman (1996) Annu. Rev. Cell Dev. Biol. 12:181.
- Ravetch, J.V. and S. Bolland (2001) Annu. Rev. Immunol. 19:275.
- Ravetch, J.V. and J.P. Kinet (1991) Annu. Rev. Immunol. 9:457.
- Arman, M. and K. Krauel (2015) J. Thromb. Haemost. 13:893.
- Takai, T. (2002) Nature Rev. Immunol. 2:580.
- Ravetch, J. and L. Lanier (2000) Science 290:84.
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