€505.00 €429.25
Fc?RIIb, also known as CD32B, is a low-affinity IgG receptor that binds the Fc region of IgG.{57316,57317} It is composed of two immunoglobulin-like (Ig-like) extracellular domains, a transmembrane domain, and a cytoplasmic tail domain containing an immunoreceptor tyrosine-based inhibitory motif (ITIM), which is important for its signaling activity.{57317} The Fc?RIIb isoform is generated via alternative splicing and has a shorter cytoplasmic tail than the Fc?RIIa isoform, which allows the Fc?RIIb isoform to be endocytosed. Fc?RIIb is predominantly expressed on myeloid-derived cells, whereas the Fc?RIIa isoform is primarily expressed on B cells. Fc?RIIb is a co-inhibitory receptor that, when phosphorylated at the ITIM region, inhibits the activation of activating Fc?Rs on myeloid cells and of B cell receptors but can also inhibit B cell receptor activation in the absence of ITIM phosphorylation. It inhibits the pathogen clearing activity mediated by activating Fc?Rs, including reducing phagocytosis and cytokine release by myeloid cells, and reduces immune complex-mediated cellular activation, such as inhibiting B cell activation or inducing apoptosis of self-reactive B cells.{57316} A SNP in FCGR2B, the gene encoding Fc?RIIb, is associated with susceptibility to systemic lupus erythematosus (SLE), and SNPs in FCGR2B are also associated with rheumatoid arthritis and immune thrombocytopenic purpura (ITP).{57318} Cayman’s Fc?RIIb/CD32B (human, recombinant) protein can be used for binding assay applications. This protein consists of 183 amino acids and has a calculated molecular weight of 20.8 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 29 kDa due to glycosylation.
Territorial Availability: Available through Bertin Technologies only in France
| Size | 1 mg, 100 µg |
|---|---|
| Shipping | dry ice |
| Molecular weight | |
| Host | CHO cells |
| Custom code | 3504.00 |
| Formulation | Lyophilized from sterile PBS, pH 7.4 |
| Purity | ≥97% estimated by SDS-PAGE |
| UNSPSC code | 12352204 |
Cayman Chemical’s mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.
Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.
Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.
Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.
Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009
Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.
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