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Biotinylated Human Fc gamma RIIB/CD32b Protein 4842

$525.00$1,750.00

Summary

  • Expression: HEK293
  • Binding assay: Yes (SPR)
  • Amino Acid Range: Ala46-Pro217
Weight1 lbs
Dimensions9 × 5 × 2 in
product tag

C-His-Avi, also biotinylated

Biotinylated Human Fc gamma RIIB/CD32b Protein 4842

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
The Fc gamma Rs have been divided into three classes based on close relationships in their extracellular domains; these groups are designated Fc gamma RI (also known as CD64), Fc gamma RII (CD32), and Fc gamma RIII (CD16). Each group may be encoded by multiple genes and exist in different isoforms depending on species and cell type. The CD64 proteins are high affinity receptors (~10e-8-10e-9 M) capable of binding monomeric IgG, whereas the CD16 and CD32 proteins bind IgG with lower affinities (~10e-6-10e-7 M) only recognizing IgG aggregates surrounding multivalent antigens.
Protein names
Low affinity immunoglobulin gamma Fc region receptor II-b (IgG Fc receptor II-b) (CDw32) (Fc-gamma RII-b) (Fc-gamma-RIIb) (FcRII-b) (CD antigen CD32)
Gene names
FCGR2B,FCGR2B CD32 FCG2 IGFR2
Mass
9606Da
Function
FUNCTION: Receptor for the Fc region of complexed or aggregated immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B-cells. Binding to this receptor results in down-modulation of previous state of cell activation triggered via antigen receptors on B-cells (BCR), T-cells (TCR) or via another Fc receptor. Isoform IIB1 fails to mediate endocytosis or phagocytosis. Isoform IIB2 does not trigger phagocytosis.
Subellular location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
Tissues
TISSUE SPECIFICITY: Is the most broadly distributed Fc-gamma-receptor. Expressed in monocyte, neutrophils, macrophages, basophils, eosinophils, Langerhans cells, B-cells, platelets cells and placenta (endothelial cells). Not detected in natural killer cells.
Structure
SUBUNIT: Interacts with INPP5D/SHIP1. Interacts with FGR. Interacts with LYN. {ECO:0000269|PubMed:8327512, ECO:0000269|PubMed:9232445}.; SUBUNIT: (Microbial infection) Isoform IIB1 interacts with measles virus protein N. Protein N is released in the blood following lysis of measles infected cells. This interaction presumably block inflammatory immune response. {ECO:0000269|PubMed:15914856}.
Post-translational modification
PTM: Phosphorylated by the SRC-type Tyr-kinases LYN and BLK. {ECO:0000269|PubMed:8756631}.
Domain
DOMAIN: Co
Target Relevance information above includes information from UniProt accession : P31994
The UniProt Consortium

Data

SPR with Biotinylated Human Fc gamma RIIB/CD32b Protein
Biotinylated Human Fc gamma RIIB, His-Avi Tag captured on CM5 Chip via Anti-his antibody can bind Rituximab with an affinity constant of 5.87 µM as determined in SPR assay (Biacore T200) (QC Test).
SPR with Biotinylated Human Fc gamma RIIB/CD32b Protein
Rituximab captured on CM5 Chip via Protein A can bind Biotinylated Human Fc gamma RIIB, His-Avi Tag with an affinity constant of 3.97 µM as determined in SPR assay (Biacore T200).
HPLC of Biotinylated Human Fc gamma RIIB/CD32b Protein
The purity of Biotinylated Human Fc gamma RIIB is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Biotinylated Human Fc gamma RIIB/CD32b Protein
Biotinylated Human Fc gamma RIIB on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.




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