FCMR Human
Fas apoptotic inhibitory molecule 3, IgM Fc fragment receptor, Regulator of Fas-induced apoptosis Toso, FAIM3, TOSO.
Greater than 95.0% as determined by SDS-PAGE.
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Description
FCMR Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 18-250) containing 243 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 27.2kDa (calculated).
Product Specs
Fas apoptotic inhibitory molecule 3 (FCMR) plays a role in immune system processes. FCMR protects cells from apoptosis induced by the proteins FADD, FAS, and TNF alpha, without overexpressing apoptosis inhibitors like BCLXL or BCL2. Instead of blocking apoptotic signals downstream, FCMR activates an inhibitory pathway that prevents CASP8 activation.
Recombinant human FCMR, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 243 amino acids (a.a 18-250), including a 10 a.a N-terminal His tag. The calculated molecular mass is 27.2 kDa.
FCMR is filtered (0.4 µm) and lyophilized from a solution of 50 mM acetate buffer, pH 4, at a concentration of 0.5 mg/ml.
To prepare a working stock solution of approximately 0.5 mg/ml, add 0.1 M acetate buffer (pH 4) to the lyophilized pellet and allow it to dissolve completely. Please note that the solubility of this antigen is limited at higher concentrations.
Purity is determined to be greater than 95.0% by SDS-PAGE analysis.
Fas apoptotic inhibitory molecule 3, IgM Fc fragment receptor, Regulator of Fas-induced apoptosis Toso, FAIM3, TOSO.
MKHHHHHHAS RILPEVKVEG ELGGSVTIKC PLPEMHVRIY LCREMAGSGT CGTVVSTTNF IKAEYKGRVT LKQYPRKNLF LVEVTQLTES DSGVYACGAG MNTDRGKTQK VTLNVHSEYE PSWEEQPMPE TPKWFHLPYL FQMPAYASSS KFVTRVTTPA QRGKVPPVHH SSPTTQITHR PRVSRASSVA GDKPRTFLPS TTASKISALE GLLKPQTPSY NHHTRLHRQR ALDYGSQSGR EGQ.
Product Science Overview
The Fc fragment of IgM receptor, also known as FcμR, is a crucial component of the immune system. It is the newest member of the Fc receptor family, having been identified in 2009 . This receptor is uniquely expressed by lymphocytes, which suggests it has distinct functions compared to other Fc receptors that are expressed by various immune and non-hematopoietic cells .
The FcμR is a membrane-bound receptor that specifically binds to the Fc region of Immunoglobulin M (IgM) antibodies. IgM is the first antibody to emerge during phylogeny, ontogeny, and immune responses, serving as a first line of defense . The Fc region of IgM contains three heavy chain constant domains (Cμ2-Cμ4) in each polypeptide chain . The interaction between FcμR and the Fc region of IgM is critical for mediating various immune responses.
FcμR plays a significant role in regulating B cell tolerance. Studies involving FcμR-deficient mice have shown a propensity to produce autoantibodies of both IgM and IgG isotypes, indicating a regulatory function of FcμR in maintaining immune homeostasis . Additionally, FcμR is involved in protecting cells from apoptosis induced by proteins such as FADD, FAS, and TNF alpha, without overexpressing inhibitors of apoptosis like BCLXL or BCL2 .
Elevated levels of a soluble FcμR isoform have been observed in serum samples from patients with chronic lymphocytic leukemia and antibody-mediated autoimmune disorders . This suggests that persistent B cell receptor stimulation can lead to increased levels of soluble FcμR, which may have implications in the pathogenesis of these diseases.
Understanding the role of FcμR in immune regulation opens up potential therapeutic avenues. Targeting FcμR could be a strategy for modulating immune responses in autoimmune diseases and certain types of leukemia. Further research is needed to fully elucidate the mechanisms by which FcμR functions and its potential as a therapeutic target.
