Recombinant Human FCGRT & B2M Heterodimer Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2008

Recombinant Human FCGRT & B2M Heterodimer Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2008
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Product Overview

Tag His
Host Species Human
Accession P55899
Synonym alpha-chain, FCRN
Description A DNA sequence encoding the extracellular domain (Met 1-Ser 297) of human FCGRT (P55899) was fused with a His tag at the C-terminus, constructed the plasmid 1; A DNA sequence encoding the human B2M (P61769) (Met 1-Met 119) constructed the plasmid 2. The two plasmids were co-expressed and the FCGRT / B2M heterodimer was purified.
Source HEK293
Predicted N Terminal Ala 24 & Ile 21
AA Sequence Met 1-Ser 297
Molecular Weight The recombinant heterodimer of human FCGRT/B2M comprises 385 (285 + 100) a.a. and has a calculated molecular mass of 43.5 (31.8 + 11.7) kDa. The apparent molecular mass of rh FCGRT/B2M heterodimer is approximately 35 & 12 kDa respectively in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its ability to bind human IgG1 in a functional ELISA.
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Cell surface receptor that transfers passive humoral immunity from the mother to the newborn. Binds to the Fc region of monomeric immunoglobulin gamma and mediates its selective uptake from milk. IgG in the milk is bound at the apical surface of the intestinal epithelium. The resultant FcRn-IgG complexes are transcytosed across the intestinal epithelium and IgG is released from FcRn into blood or tissue fluids. Throughout life, contributes to effective humoral immunity by recycling IgG and extending its half-life in the circulation. Mechanistically, monomeric IgG binding to FcRn in acidic endosomes of endothelial and hematopoietic cells recycles IgG to the cell surface where it is released into the circulation. In addition of IgG, regulates homeostasis of the other most abundant circulating protein albumin/ALB.; (Microbial infection) Acts as an uncoating receptor for a panel of echoviruses including Echovirus 5, 6, 7, 9, 11, 13, 25 and 29.
Subcellular Location Cell membrane; Single-pass type I membrane protein. Endosome membrane.
Protein Families Immunoglobulin superfamily
Database References
Tissue Specificity Expressed in full-term placenta, heart, lung, liver, muscle, kidney, pancreas, and both fetal and adult small intestine.

Gene Functions References

  1. As expected, recombinant factor IX (without albumin fusion) and an FcRn interaction-defective albumin variant localized to the lysosomal compartments of both FcRn-expressing and nonexpressing cells. These results indicate that FcRn-mediated recycling via the albumin moiety is a mechanism for the half-life extension of rIX-FP observed in clinical studies. PMID: 29523681
  2. Regulation of the Human Fc-Neonatal Receptor alpha-Chain Gene FCGRT by MicroRNA-3181. PMID: 29302759
  3. we have demonstrated that loss of FcRn expression promotes tumor cell growth and proliferation. Our data support a model in which FcRn-mediated recycling of albumin reduces amino acid availability to fuel metabolic pathways. PMID: 27974681
  4. An arginine-to-histidine replacement at residue 435 in the binding domain of IgG3 to FcRn increases the transplacental transfer and half-life of malaria-specific IgG3 in young infants and is associated with reduced risk of clinical malaria during infancy. PMID: 28991911
  5. these findings establish a novel mechanism of humoral protection in the eye involving FcRn and may facilitate vaccine and therapeutic development for other ocular surface diseases PMID: 28760885
  6. Data suggest that, unlike albumin with low FcRn-binding affinity, albumin with high FcRn-binding affinity (due to genetic variation/genetic engineering) is directed less to lysosomes and more to endosomes, suggestive of FcRn-directed albumin salvage from lysosomal degradation. (FcRn = neonatal Fc receptor) PMID: 28637874
  7. the localization of FcRn alpha-chain in fixed nasal tissue, was studied. PMID: 26634928
  8. FcRn is involved in transport of aflibercept through REC in vitro. PMID: 27836572
  9. this study shows that FcRn may be associated with the transport and metabolism of IgG in thyrocytes and that transport is independent of IgG type, and that FcRn may be involved in Hashimoto's thyroiditis pathogenesis PMID: 28081504
  10. This review summarizes the main findings on Fc Receptor neonatal biology, function and distribution throughout different tissues. PMID: 27016466
  11. The results suggest that regardless of hyperglycemia degree, it decreases FcRn expression in placenta and blood cells and compromises the production and transfer of antibodies from maternal blood to newborns. PMID: 27469170
  12. Data indicate improved pharmacokinetics through enhanced neonatal Fc receptor (FcRn) interactions were apparent for a complementarity-determining region (CDR) charge-patch normalized monoclonal antibody (mAb) which was affected by non-specific clearance. PMID: 26337808
  13. analysis of binding motifs in the hFCGRT promoter that interact with their corresponding (Sp1, Sp2, Sp3, c-Fos, c-Jun, YY1, and C/EBPbeta or C/EBPdelta) transcription factors (TFs) suggests their involvement in regulation of human FCGRT gene expression PMID: 26252948
  14. These data indicate that human FcRn facilitates the transepithelial transport of IgE in the form of IgG anti-IgE/IgE ICs. PMID: 25652137
  15. Critical Role of the Neonatal Fc Receptor (FcRn) in the Pathogenic Action of Antimitochondrial Autoantibodies Synergizing with Anti-desmoglein Autoantibodies in Pemphigus Vulgaris. PMID: 26260795
  16. FcRn binding activity of a large set of Fc-fusion samples after thermal stress, was investigated. PMID: 26254986
  17. The neonatal Fc receptor (FcRn) binds independently to both sites of the IgG homodimer with identical affinity. PMID: 25658443
  18. These results suggest that hFcRn Tgm are a valuable and useful tool for pharmacokinetic screening of mAbs and Fc-fusion proteins in the preclinical stage. PMID: 25030041
  19. The extents of IgG expression in 86 lung cancers were found to associate with clinical stage, pathological grade and lymph node metastasis. PMID: 24853685
  20. Molecular dynamic simulations of human FcRn-Fc binding structures proposed that the protein-protein binding interface is composed of three subsites. PMID: 24057047
  21. This mAb panel provides a powerful resource for probing the biology of human FcRn and for the evaluation of therapeutic FcRn blockade strategies. PMID: 22453095
  22. domain I and III of albumin required for optimal pH-dependent binding to the neonatal Fc receptor PMID: 25344603
  23. Characterization and screening of IgG binding to the neonatal Fc receptor. PMID: 24802048
  24. In intestine, there was an increasing proximal-distal gradient of mucosal FcRn mRNA and protein expression. PMID: 24072267
  25. A cluster of conserved tryptophan residues of FcRn is required for binding to albumin and anti-FcRn albumin blocking antibodies. PMID: 24764301
  26. Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding. PMID: 24652290
  27. The Neonatal Fc receptor (FcRn) enhances human immunodeficiency virus type 1 (HIV-1) transcytosis across epithelial cells. PMID: 24278022
  28. analysis of neonatal Fc receptor-based recycling mechanisms through identification of the human Fc interaction with human FcRn PMID: 24469444
  29. FcRn has the potential to interact with IgG-Fc domains in the ciliary epithelium and retinal and choroidal vasculature, which might affect the half-life and distribution of intravitreally injected Fc-carrying molecules. PMID: 24550358
  30. Only the unbound receptor or FcRn bound to monomeric IgG is sorted into recycling tubules emerging from early endosomes. PMID: 23741050
  31. Analytical FcRn chromatography allows differentiation of IgG samples and variants by peak pattern and retention time profile. PMID: 23765230
  32. The FCGRT promoter VNTR may influence mAbs' distribution in the body. CNV of FCGRT cannot be used as a relevant pharmacogenetic marker because of its low frequency. PMID: 23751752
  33. Studies indicate that high levels of endogenous IgG can compete with the monoclonal antibodies (mAbs) for binding to the neonatal Fc receptor (FcRn). PMID: 23917469
  34. Data indicate that Fc-neonatal Fc receptor (FcRn) interaction is pH dependent. PMID: 23384837
  35. Human FcRn was visualized in epithelial cells of Tg276 mice, but low serum hIgG levels were obtained PMID: 23220220
  36. genetic polymorphism is associated with the efficiency of Ig replacement therapy in common variable immunodeficiency PMID: 23286945
  37. Serum half-life of IgG is controlled by the neonatal Fc receptor (FcRn) that interacts with the IgG Fc region and may be increased or decreased as a function of altered FcRn binding. PMID: 22570488
  38. Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor PMID: 22215085
  39. FcRn transgene blockade is a primary contributing factor toward reduction in arthritis severity; engineering of antibody Fc regions to generate potent FcRn blockers holds promise for the therapy of antibody-mediated autoimmunity in experimental arthritis. PMID: 21690327
  40. Thirty-three genetic variations of FCGRT, including 17 novel ones, were found. PMID: 20930418
  41. These studies demonstrate that FcRn-mediated transport is a mechanism by which IgG can act locally in the female genital tract in immune surveillance and in host defense against sexually transmitted diseases. PMID: 21368166
  42. Methionine (Met) oxidation can result in a significant reduction of the serum circulation half-life and the magnitude of the change correlates well with the extent of Met oxidation and changes in FcRn binding affinities. PMID: 21256596
  43. promoter polymorphism is not associted with the rate of maternal-fetal IgG transfer PMID: 20452034
  44. the x-ray crystal structure of a representative monomeric peptide in complex with human FcRn PMID: 20592032
  45. influence of FcRn expression on disease phenotype and the catabolism of therapeutically administered intravenous immunoglobulins in 28 patients with common variable immunodeficiency PMID: 20627700
  46. No binding of albumin was observed at physiological pH to neonatal Fc receptor. At acidic pH, a 100-fold difference in binding affinity was observed. PMID: 20018855
  47. A recombinant truncated HSA variant, HSA(Bartin), does not interact with FcRn, which gives a molecular explanation for the low serum levels. PMID: 20006594
  48. Affinities to FcRn of clinically used therapeutic proteins are closely correlated with the serum half-lives reported from clinical studies, and suggest an important role of FcRn in regulating the serum half-lives of the therapeutic proteins. PMID: 20083659
  49. Human FcRn binds selectively to human, rabbit and guinea pig IgG but not significantly to rat, bovine, sheep or mouse IgG (except for weak binding to mouse IgG2b). PMID: 11717196
  50. Assembly of the FcRn alpha-chain with beta(2)microglobulin is important for both transport of FcRn from the ER to the cell surface and efficient pH-dependent IgG binding. PMID: 12006623


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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