Optimized DNA sequence encoding Human extracellular domain of human CD32a including a C-terminal 6His tag was expressed in HEK293 cells.
Recombinant CD32a is a monomer protein consisting of 192 amino acid residue subunits, due to glycosylation migrates as an approximately 25 kDa protein on SDS-PAGE.
1ug of Immobilized CD32a was tested to bind human IgG2 in a range of 10-200ng/ml.
>95%, as determined by SDS-PAGE and HPLC
Endotoxin content was assayed using a LAL gel clot method.
Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).
Recombinant CD32a is supplied as a lyophilized 0.2 μm filtered PBS solution, pH7.2 .
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL..It is recommended to add 0.1% BSA for long term storage of reconstituted product.
Lyophilized CD32a , as supplied, should be stored at -20°C to -70°C
Upon reconstitution , working aliquots may be stored at 2° - 8° C for one month, or six months at -20C without detectable loss of activity.It is recommended to add 0.1% BSA for long term storage.
Avoid repeated freeze/thaw cycles.
This product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.
FcγRIIA is expressed on
cells ofboth myeloid and
lymphoid lineages as well as
on cells of non-
origin.Associated with an
elivers an activating signal
upon ligand binding,and
results in the initiation of
nulation and cytokine
production.The responses can
be modulated by signals from
the coexpressed inhibitory
receptors such as
FcγRIIB,and the strength of
the signal is dependent on
the ratio of expression of
the activating and
dynamics of the interaction of human igg subtype immune complexes with cells expressing r and h allelic forms of a low-affinity fc receptor CD32a J. Immunol.,
8216 - 8224.
association of fcriia (CD32a) with lipid rafts regulates ligand binding activity
8026 - 8036.
transgenic expression of human platelet fcriia (CD32a) in mice does not affect the thrombocytopenia associated with wasp deficiency.
Blood (ASH Annual Meeting Abstracts),