Cynomolgus FCGRT & B2M Heterodimer Protein (His Tag)

Cynomolgus FCGRT & B2M Heterodimer Protein Datasheet

FCGRT & B2M Protein Heterodimer Product Information

• Synonym: FCGRT FCRN & B2M
• Protein Construction: A DNA sequence encoding the extracellular domain (Met 1- Ser 297) of cyno FCGRT(Q8SPV9) was fused with a polyhistidine tag at the C-terminus, constructed the plasmid 1; A DNA sequence encoding the cyno B2M (Q6V7J5) (Met 1- Met 119) constructed the plasmid 2. The two plasmids were co-expressed and the FCGRT/B2M heterodimer was purified.
• Source: Cynomolgus monkey
• Expression Host: Human Cells

FCGRT & B2M Heterodimer Protein QC Testing

• Purity: > 98 % as determined by SDS-PAGE
• Bio-activity: Measured by its ability to bind human IgG1 in functional ELISA.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Ala 24 & Ile 21
• Molecular Mass: The recombinant heterodimer of cyno FCGRT&B2M comprises 384 (285+99) amino acids and has a calculated molecular mass of 43.5 (31.9+ 11.6) KDa. The apparent molecular mass of cyno FCGRT&B2M heterodimer is approximately 35 & 12 KDa respectively in SDS-PAGE
• Formulation: Lyophilized from sterile PBS, pH7.4.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: FCGRT & B2M Heterodimer protein

FCGRT & B2M Heterodimer Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

FCGRT & B2M Heterodimer Protein Description

IgG receptor FcRn large subunit p51, also known as IgG Fc fragment receptor transporter alpha chain, Neonatal Fc receptor, FCGRT and FCRN, is a single-pass type I membrane protein which belongs to the immunoglobulin superfamily. FcRn / FCGRT is a MHC class I like molecule that functions to protect IgG and albumin from catabolism. FcRn / FCGRT binds to the Fc region of monomeric immunoglobulins gamma. It mediates the uptake of IgG from milk. It may play a role in transfer of immunoglobulin G from mother to fetus. Beta-2-microglobulin, also known as B2M, is a secreted protein which belongs to the beta-2-microglobulin family. It contains one Ig-like C1-type (immunoglobulin-like) domain. Beta-2 microglobulin (B2M) plays a pivotal role in the biology of mammals. B2M forms the small invariable light chain subunit of class I HLA antigens on the cell membrane of all nucleated cells. During the continuous turnover of the HLA molecules. B2M is shed from the cell membrane into blood. Lymphocytes are the main source of serum free B2M. It associates not only with the alpha chain of MHC class I molecules, but also with class I-like molecules. B2M is necessary for cell surface expression of MHC class I and stability of the peptide binding groove. In fact, in the absence of B2M, very limited amounts of MHC class I (classical and non-classical) molecules can be detected on the surface. FcRn complex consist of two subunits: p51, and p14 which is equivalent to beta-2-microglobulin (B2M). It forms an MHC class I-like heterodimer. B2M is a component of the class I major histocompatibility complex (MHC). B2M is also an integral component of the FcRn heterodimer. Failure of passive transfer (FPT) is a condition in which neonates do not acquire protective serum levels of maternal antibodies. A principal component of antibody transport is the neonatal receptor for the Fc portion of immunoglobulin, a heterodimer of a MHC-1 alpha-chain homolog ( FcRn ) and beta-2-microglobulin ( B2M ).

References

1. He XH. et al., 2004, Sheng Wu Gong Cheng Xue Bao. 20: 99-103.
2. Clawson ML. et al., 2004, Mamm Genome. 15 (3): 227-36.
3. Kihara M. et al., 2006, J Biol Chem. 281: 31061-9.
4. Ricagno S. et al., 2009, Biochem Biophys Res Commun. 380: 543-7.
5. Kuo TT. et al., 2010, J Clin Immunol. 30 (6): 777-89.