250 μg
USD 1000
In stock 
5x 250 μg
USD 4000
In stock
Low affinity immunoglobulin gamma Fc receptor IIa, also known as FcγRIIa or CD32a, is a type I integral membrane glycoprotein. CD32a is a member of the immunoglobulin superfamily and is expressed on macrophages, monocytes, neutrophils, eosinophils and dendritic cells, epithelial cells, platelets and activated CD4+ T cells. CD32a binds monomeric IgG with low affinity but is very efficient at binding immune complexes and is involved in phagocytosis and clearing of immune complexes. CD32a is structurally composed of two extracellular immunoglobulin domains of the C2-type that interact with the IgG Fc domain, a transmembrane domain and a short cytoplasmic tail containing the immunoreceptor tyrosine-based activation (ITAM) motif. The product provided only contains the extracellular portion of CD32a.
CD32a has two allotypic variants differing at amino acid position 167, one containing histidine (H167) and the other arginine (R167). H167 exhibits a higher affinity to human IgG1 and IgG2 than the R167 does and is thought to be primarily responsible for the phagocytosis of IgG-opsonized bacteria.
CD32, CD32A, Fc gamma R2, Fc gamma R2a, Fc gamma RII, Fc gamma RIIa, Fcg R2, Fcg R2a, Fcg RII, Fcg RIIa, FCGR2, FCGR2A, FCGRII, FCGRIIA, FCR2, FCR2A, FCRII, FCRIIA, IGFR2, IGFR2A, IGFRII, IGFRIIA
Pig
XP_020945179.1
Not applicable
Unconjugated (no label). The protein contains an AVI tag but this has not been biotinlyated in this product.
>95% monomer purity as determined by SDS-PAGE and SEC-HPLC.
<1.0 EU per mg as determined by the LAL method.
The sequence of the extracellular domain of porcine CD32a (Ala 1-Gln 185) was fused with a C-terminal tag consisting of the AVI tag, TEV protease recognition sequence and a 10-His tag. The full protein sequence can be downloaded from the product webpage.
The recombinant pig CD32a including tag consists of 223 amino acids and has a theoretical mass of 25236 Da.
Human embryonic kidney (HEK) 293 cells.
Lyophilized from sterile PBS, pH 7.4. No preservatives or cryoprotectants have been added.
To obtain a final concentration of 1 mg/ml reconstitute 250 μg vials with 250 μl water and 1.0 mg vials with 1.0 ml water. Solubilize for 30 to 60 minutes at room temperature with occasional gentle mixing. Do not vortex.
All recombinant proteins are provided as lyophilized powder and shipped at ambient temperature.
Lyophilized proteins are stable at ambient temperature for at least 2 weeks. If the protein is not to be used immediately then the protein should be stored in lyophilized form at -20 °C for up 12 months. Once the protein has been reconstituted we recommend storage at 4 °C for up to one week. For longer term storage of protein in solution we recommend aliquoting into smaller vials to avoid repeated freeze-thaw cycles and storage at -20 or -80 °C for up to 3 months. To avoid surface adsorption loss and inactivation we strongly recommend that the protein should not be aliquoted in less than 10 μg per vial.
The below images are examples of data for one batch of this product. Every batch of recombinant proteins is assessed by the same methods and batch specific data is provided in the respective certificate of analysis (COA). COAs can be downloaded from the documentation at the top of this page.
Pig Fc gamma RIIa / CD32a on Coomassie Blue stained SDS-PAGE under non-reducing (NR) and reducing (R) conditions. The purity of the protein is greater than 95%.
Assessment of protein purity for pig Fc gamma RIIa / CD32a by SEC-HPLC. The protein is greater than 95% pure.
Assessment of binding of pig Fc gamma RIIa / CD32a, immobilized on a CM5 chip via an anti-His antibody, to a human IgG1 Fc fusion protein using a Biacore 8K instrument. The protein binds with an affinity constant (KD) of 31 nM.
Low affinity immunoglobulin gamma Fc receptor II, also known as FcγRII or CD32, is actually a collection of three highly related isoforms: FcγRIIa, b and c. They all consist of two extracellular immunoglobulin domains, a transmembrane domain and a cytoplasmic tail with an intrinsic signaling motif. FcγRIIa and FcγRIIc contain an activatory motif (ITAM) and FcγRIIb contains an inhibitory motif (ITAM).
FcγRIIa is the most widely expressed isoform and is found on monocytes, macrophages, dendritic cells, granulocytes and platelets. FcγRIIa binds monomeric IgG with low affinity but is very efficient at binding immune complexes and is involved in phagocytosis and clearing of immune complexes. FcγRIIa has two allotypic variants differing at amino acid position 167, one containing histidine (H167) and the other arginine (R167). H131 exhibits a higher affinity to human IgG1 and IgG2 than the R167 does and is thought to be primarily responsible for the phagocytosis of IgG-opsonized bacteria.
FcγRIIb is highly expressed on B-cells, where is it the only surface expressed FcγR, and at much lower levels on monocytes, macrophages, dendritic cells. CD32b binds monomeric IgG with low affinity but is efficient at binding immune complexes and is a negative regulator of cell activation, proliferation, endocytosis, phagocytosis, and degranulation.
For further information on the structure and functions of all Fc receptors please see our Fc receptors resource page.
Table of human Fc gamma receptor classes, structures, allotypes, specificities, expression profiles and function.
For the cartoon structure images, C-terminal extracellular domains are shown as colored ovals with activatory and inhibitory motifs (ITAM and ITIM) shown as green and red rectangles respectively.
FcγRIIc was long thought to be a pseudogene and so much less is known about its role and expression profile. It is the result of an unequal crossover event between FcγRIIa and FcγRIIb, resulting in a protein with the extracellular domains of FcγRIIb and intracellular activatory motif of FcγRIIa.
|
FcɣRI CD64 |
FcɣRlla CD32a |
FcɣRllb CD32b |
FcɣRllc CD32c |
FcɣRllIa CD16a |
FcɣRIlIb CD16b |
|||
|---|---|---|---|---|---|---|---|---|
| Structure |  |
 |
 |
 |
 |
 |
 |
|
|
Allotypes (*not in the ECD) |
167H167R | 232I*232T* | 57Q57stop | 176F176V | NA1NA2SH* | |||
|
Affinity |
High | Low | Low | Low | Low | Low | Low | |
|
Relative |
lgG1:+++lgG2:-lgG3:+++lgG4:+++ |
lgG1:+++lgG2:+lgG3:++lgG4:+
167H has↑bindingto IgG1/2/3
|
lgG1:+lgG2:+/-lgG3:+lgG4:+ | lgG1:+lgG2:+/-lgG3:+lgG4:+ |
lgG1:+++lgG2:+lgG3:++lgG4:+
176v has ↑ binding to all lgG |
|||
|
Expression |
B-cell | – | – | + | – | – | – | – |
| T-cell | – | – | – | – | – | – | – | |
| NK cell | – | – | Genotype | Genotype | + | – | – | |
| DC | + | + | + | Genotype | + | – | – | |
| Macro | + | + | + | Genotype | + | – | – | |
| Mono | + | + | Subsets | Genotype | Subsets | – | – | |
| Neutro | Induced | + | Genotype | Genotype | – | – | + | |
| Eosino | Induced | + | – | – | – | – | induced | |
| Baso | – | + | + | – | + | + | – | |
| Mast | Induced | + | Subsets | Genotype | + | + | – | |
| Platelet | – | + | – | – | – | – | – | |
| Function |
Activation |
Activation |
Inhibition |
Activation |
Activation |
Decoy |
||
FcγRI
High affinity immunoglobulin gamma Fc receptor I, also known as FcgRI or CD64, is a type I integral membrane glycoprotein. CD64 is a member of the immunoglobulin superfamily and is expressed on monocytes, macrophages, dendritic cells and activated granulocytes. CD64 binds with high affinity to the Fc domain of IgG and it plays a role in antigen capture, phagocytosis of IgG/antigen complexes, and antibody-dependent cellular cytotoxicity (ADCC). CD64 is structurally composed of three extracellular immunoglobulin domains of the C2-type that interact with the IgG Fc domain, a transmembrane domain and a short cytoplasmic tail. CD64 is associated with a dimer of the common Fc receptor gamma-chain which contains the immunoreceptor tyrosine-based activation (ITAM) motif. The product provided only contains the extracellular portion of CD64.
Synonyms: CD64, CD64A, Fc gamma R1, Fc gamma RI, Fcg R1, Fcg RI, FCGR1, FCGR1A, FCGRI, FCGRIA, FCR1, FCRI, IGFR1, IGFRI
FcγRII
Low affinity immunoglobulin gamma Fc receptor II, also known as FcgRII or CD32, is actually a collection of three highly related isoforms: FcgRIIa (CD32a), FcgRIIb (CD32b) and FcgRIIc (CD32c). They all consist of two extracellular immunoglobulin domains, a transmembrane domain and a cytoplasmic tail with an intrinsic signaling motif. CD32a and CD32c contain an activatory motif (ITAM) and FcγRIIb contains an inhibitory motif (ITAM).
CD32a is the most widely expressed isoform and is found on monocytes, macrophages, dendritic cells, granulocytes and platelets. FcγRIIa binds monomeric IgG with low affinity but is very efficient at binding immune complexes and is involved in phagocytosis and clearing of immune complexes. CD32a has two allotypic variants differing at amino acid position 167, one containing histidine (H167) and the other arginine (R167). H131 exhibits a higher affinity to human IgG1 and IgG2 than the R167 does and is thought to be primarily responsible for the phagocytosis of IgG-opsonized bacteria.
Synonyms: CD32, CD32A, Fc gamma R2, Fc gamma R2a, Fc gamma RII, Fc gamma RIIa, Fcg R2, Fcg R2a, Fcg RII, Fcg RIIa, FCGR2, FCGR2A, FCGRII, FCGRIIA, FCR2, FCR2A, FCRII, FCRIIA
CD32b is highly expressed on B-cells, where is it the only surface expressed FcγR, and at much lower levels on monocytes, macrophages, dendritic cells. CD32b binds monomeric IgG with low affinity but is efficient at binding immune complexes and is a negative regulator of cell activation, proliferation, endocytosis, phagocytosis, and degranulation.
Synonyms: CD32, CD32B, CD32b/c, Fc gamma R2, Fc gamma R2b, Fc gamma RII, Fc gamma RIIb, Fcg R2, Fcg R2b, Fcg RII, Fcg RIIb, FCGR2, FCGR2B, Fcgr2b/c, FCGRII, FCGRIIB, FCR2, FCR2B, FCRII, FCRIIB
FcγRIII
Low affinity immunoglobulin gamma Fc receptor III, also known as FcgRIII or CD16, has two isoforms: FcgRIIIa (CD16a) and FcgRIIIb (CD16b).
CD16a is composed of two extracellular immunoglobulin domains, a transmembrane domain and a shot cytoplasmic tail. On basophils and mast cells it associates with a heterodimer of γ/ζ chains and an extra β chain, whereas on other cell types it associates with a dimer of the common Fc receptor γ-chain. FcgRIIIa binds monomeric IgG with low affinity but is efficient at binding immune complexes and functions in NK cell activation, phagocytosis and antibody-dependent cellular cytotoxicity (ADCC). CD16a has two allotypic variants differing at amino acid position 176, one containing phenylalanine (F176) and the other valine (V176). The V176 variant has a greater affinity for all the IgG subclasses and thus results in greater effector function.
Synonyms: CD16, CD16A, Fc gamma R3, Fc gamma R3a, Fc gamma RIII, Fc gamma RIIIa, Fcg R3, Fcg R3a, Fcg RIII, Fcg RIIIa, FCGR3, FCGR3A, FCGRIII, FCGRIIIA, FCR3, FCR3A, FCRIII, FCRIIIA
Unlike other Fc gamma receptors, FcgRIIIb (CD16b) is a GPI-anchored protein containing two extracellular immunoglobulin domains and no intracellular signaling motif. It acts primarily as a decoy receptor and is expressed only on neutrophils and eosinophils. CD16b has two allotypic variants, referred to as human neutrophil antigen 1 (NA1 or HNA1a) and 2 (NA2 or HNA1b). The allotypes have differing affinities to human IgG1 and IgG3 with the NA1 form capable of better ingestion of IgG1 or opsonized IgG3 particles than NA2.
Synonyms: CD16, CD16B, Fc gamma R3, Fc gamma R3b, Fc gamma RIII, Fc gamma RIIIb, Fcg R3, Fcg R3b, Fcg RIII, Fcg RIIIb, FCGR3, FCGR3B, FCGRIII, FCGRIIIB, FCR3, FCR3B, FCRIII, FCRIIIB
250 μg
USD 1000
In stock
5x 250 μg
USD 4000
In stock
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