Recombinant Human Igg Receptor Fcrn Large Subunit P51 (FCGRT) Protein (His)

Name: Recombinant Human Igg Receptor Fcrn Large Subunit P51 (FCGRT) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02302P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Car-t cell therapy targets, Cluster of differentiation (cd) proteins, Fc receptors, Featured cd protein molecules, Featured fc receptors molecules, Recombinant proteins

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Product Overview

Description	Recombinant Human Igg Receptor Fcrn Large Subunit P51 (FCGRT) Protein (His) is produced by our Mammalian cell expression system. This is a extracellular protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P55899
Target Symbol	FCGRT
Synonyms	Alpha chain; Fc fragment of IgG; receptor transporter; alpha; FCGRN_HUMAN; FCGRT; FcRn alpha chain; FcRn; FCRN; alpha chain; IgG Fc fragment receptor transporter alpha chain; IgG Gc receptor; IgG receptor FcRn large subunit p51; IgG receptor FcRn large subunit p51 precursor; Immunoglobulin receptor; intestinal; heavy chain; Neonatal Fc receptor
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	N-6His
Target Protein Sequence	AESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWYWEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNFDLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPPSMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSLTVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSS
Expression Range	24-297aa
Protein Length	Extracellular Domain
Mol. Weight	34.4kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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	HGNC: 3621 OMIM: 601437 KEGG: hsa:2217 STRING: 9606.ENSP00000221466 UniGene: Hs.111903
Tissue Specificity	Expressed in full-term placenta, heart, lung, liver, muscle, kidney, pancreas, and both fetal and adult small intestine.

Gene Functions References

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
Regulation of the Human Fc-Neonatal Receptor alpha-Chain Gene FCGRT by MicroRNA-3181. PMID: 29302759
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
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
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
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
the localization of FcRn alpha-chain in fixed nasal tissue, was studied. PMID: 26634928
FcRn is involved in transport of aflibercept through REC in vitro. PMID: 27836572
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
This review summarizes the main findings on Fc Receptor neonatal biology, function and distribution throughout different tissues. PMID: 27016466
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
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
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
These data indicate that human FcRn facilitates the transepithelial transport of IgE in the form of IgG anti-IgE/IgE ICs. PMID: 25652137
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
FcRn binding activity of a large set of Fc-fusion samples after thermal stress, was investigated. PMID: 26254986
The neonatal Fc receptor (FcRn) binds independently to both sites of the IgG homodimer with identical affinity. PMID: 25658443
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
The extents of IgG expression in 86 lung cancers were found to associate with clinical stage, pathological grade and lymph node metastasis. PMID: 24853685
Molecular dynamic simulations of human FcRn-Fc binding structures proposed that the protein-protein binding interface is composed of three subsites. PMID: 24057047
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
domain I and III of albumin required for optimal pH-dependent binding to the neonatal Fc receptor PMID: 25344603
Characterization and screening of IgG binding to the neonatal Fc receptor. PMID: 24802048
In intestine, there was an increasing proximal-distal gradient of mucosal FcRn mRNA and protein expression. PMID: 24072267
A cluster of conserved tryptophan residues of FcRn is required for binding to albumin and anti-FcRn albumin blocking antibodies. PMID: 24764301
Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding. PMID: 24652290
The Neonatal Fc receptor (FcRn) enhances human immunodeficiency virus type 1 (HIV-1) transcytosis across epithelial cells. PMID: 24278022
analysis of neonatal Fc receptor-based recycling mechanisms through identification of the human Fc interaction with human FcRn PMID: 24469444
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
Only the unbound receptor or FcRn bound to monomeric IgG is sorted into recycling tubules emerging from early endosomes. PMID: 23741050
Analytical FcRn chromatography allows differentiation of IgG samples and variants by peak pattern and retention time profile. PMID: 23765230
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
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
Data indicate that Fc-neonatal Fc receptor (FcRn) interaction is pH dependent. PMID: 23384837
Human FcRn was visualized in epithelial cells of Tg276 mice, but low serum hIgG levels were obtained PMID: 23220220
genetic polymorphism is associated with the efficiency of Ig replacement therapy in common variable immunodeficiency PMID: 23286945
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
Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor PMID: 22215085
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
Thirty-three genetic variations of FCGRT, including 17 novel ones, were found. PMID: 20930418
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
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
promoter polymorphism is not associted with the rate of maternal-fetal IgG transfer PMID: 20452034
the x-ray crystal structure of a representative monomeric peptide in complex with human FcRn PMID: 20592032
influence of FcRn expression on disease phenotype and the catabolism of therapeutically administered intravenous immunoglobulins in 28 patients with common variable immunodeficiency PMID: 20627700
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
A recombinant truncated HSA variant, HSA(Bartin), does not interact with FcRn, which gives a molecular explanation for the low serum levels. PMID: 20006594
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
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
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

FAQs

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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.