Recombinant Mouse Transferrin Receptor Protein (His Tag)

Name: Recombinant Mouse Transferrin Receptor Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-4633
Availability: InStock

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Mouse
Accession	Q62351
Synonym	2610028K12Rik, AI195355, AI426448, AU015758, CD71, E430033M20Rik, Mtvr-1, Mtvr1, p90, TFR, TFR1, TR, Trfr
Background	Transferrin receptor protein 1, also known as transferrin receptor, Trfr, p9, CD71 and TFRC, is a single-pass type II membrane protein which belongs to thepeptidase M28 family and M28B subfamily. TFRC / CD71 is a membrane-bound protein expressed in larger amounts in proliferating. The specific expression of TFRC can represent a diagnostic tool or a therapeutic target in solid tumours expressing this antigen. Transferrin receptor is necessary for development of erythrocytes and the nervous system. TFRC / CD71 is regulated by cellular iron levels through binding of the iron regulatory proteins, IRP1 and IRP2, to iron-responsive elements in the 3'-UTR. Up-regulated upon mitogenic stimulation. TFRC / CD71 represents a marker of malignant transformation in the pancreas that could be applied as potential diagnostic and therapeutic target.
Description	A DNA sequence encoding the extracellular domain of mouse TFRC (Q62351) (Cys 89-Phe 763) was fused with a His tag at the N-terminus.
Source	HEK293
Predicted N Terminal	His
AA Sequence	Cys 89-Phe 763
Molecular Weight	The recombinant mouse TFRC comprises 694 a.a. and predicts a molecular mass of 78.3 kDa. The apparent molecular mass of mouse TFRC is approximately 80 kDa in SDS-PAGE under reducing conditions.
Purity	>92% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
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	Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Upon stimulation, positively regulates T and B cell proliferation through iron uptake. Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway. When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion. When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2.
Subcellular Location	Cell membrane; Single-pass type II membrane protein. Melanosome.
Protein Families	Peptidase M28 family, M28B subfamily
Database References	KEGG: mmu:22042 STRING: 10090.ENSMUSP00000023486 UniGene: Mm.28683

Gene Functions References

duodenal Regnase-1 controls the expression of PHD3, which impairs duodenal iron uptake via HIF2alpha suppression. PMID: 28538180
role in the development of hypoxia-induced pulmonary vascular remodeling PMID: 26419445
Knock-out of TFR1 in Purkinje cells reduces mGlu1 expression at synapses and impairs motor coordination. PMID: 29054881
decreasing TfR1 expression during beta-thalassemic erythropoiesis, either directly via induced haploinsufficiency or via exogenous apotransferrin, decreases ineffective erythropoiesis and provides an endogenous mechanism to upregulate hepcidin, leading to sustained iron-restricted erythropoiesis and preventing systemic iron overload in beta-thalassemic mice PMID: 28151426
our study reveals that TFR functions as a novel regulator to control AMPA trafficking efficiency and synaptic plasticity PMID: 26880306
We found that iron assimilation via Tfr1 was critical for skeletal muscle metabolism, and that iron deficiency in muscle led to dramatic changes, not only in muscle, but also in adipose tissue and liver. PMID: 26870796
Mice lacking Tfr1 in the heart died in the second week of life and had cardiomegaly, poor cardiac function, failure of mitochondrial respiration, and ineffective mitophagy. PMID: 26456827
Transferrin Receptor 1 Facilitates Poliovirus Permeation of Mouse Brain Capillary Endothelial Cells. PMID: 26637351
Erythrocytic iron deficiency enhances susceptibility to Plasmodium chabaudi infection in mice carrying a missense mutation in tfr1. PMID: 26303393
Tfr1 has a role in homeostatic maintenance of the intestinal epithelium, acting through a role that is independent of its iron-uptake function PMID: 26324903
Analysis by qPCR showed changes in mRNA levels of iron-responsive genes, indicating moderately increased iron in the RPE of 10-month HID mice. PMID: 26275132
characterization of erythropoiesis, iron status, and hepcidin expression in mice with global or hematopoietic cell-specific haploinsufficiency of transferrin receptor 1 provides initial supporting data for this model PMID: 25782630
high levels of TfRs such as those found on activated lymphocytes were found to be associated with decreased KLRG1 inhibitory function, indicating that TfRs may sequester KLRG1 from interacting with cadherins. PMID: 24752778
data further demonstrate that the inhibitory activity of KLRG1 is decreased in T cells expressing high levels of TfR, indicating that association of KLRG1 with TfR hinders KLRG1-mediated silencing. PMID: 24515870
high-affinity anti-TfR alters TfR trafficking, which dramatically impacts the capacity for TfR to mediate blood-brain barrier transcytosis PMID: 24470444
Data indicate increased levels of reactive oxygen species (ROS) were detected in bone marrow nucleated cells (BMNC) that express CD71 in in NUP98-HOXD13 (NHD13) transgenic mice, a murine model for myelodysplastic syndromes (MDS). PMID: 23958061
Knockdown of Rab12 increased transferrin receptor level and reduced M98K-induced cell death. PMID: 23357852
results suggest that TfR1 would be highly expressed by neurons rather than astroglia to play a negative role in the neurite outgrowth after the incorporation of circulating transferrin in the brain PMID: 22019713
In a model of celiac disease, gluten induces enterocyte CD71 overexpression. PMID: 22330344
TfR is constitutively degraded by a Rab12-dependent pathway (presumably from recycling endosomes to lysosomes), which is independent of the conventional degradation pathway. PMID: 21718402
5-aza-2'-deoxycytidine activates iron uptake and heme biosynthesis by increasing c-Myc nuclear localization and binding to the E-boxes of transferrin receptor 1 (TfR1) and ferrochelatase (Fech) genes. PMID: 21903580
Vitamin C increases the expression of the iron-regulated hormone hepcidin and decreases transferrin receptor 1 (TfR1) expression in liver. PMID: 21078691
TfR1 in colon cancer-bearing mice exhibited a 24-hour rhythm in mRNA and protein levels. Experiments suggest that the clock-controlled gene c-MYC rhythmically activated the transcription of the TfR1 gene. PMID: 20631077
used phenotypic screening of the T31 mouse/hamster radiation hybrid panel to map the MMTV cell entry receptor gene and subsequently found that it is transferrin receptor 1 PMID: 12218182
soluble transferrin receptor represents a valuable quantitative assay of marrow erythropoietic activity as well as a marker of tissue iron deficiency PMID: 12589962
both adult erythropoiesis and lymphopoiesis require TfR; TfR is necessary for the normal maturation of thymocytes, but that B-cell development is less severely affected by the absence of TfR PMID: 12881306
Direct binding of mouse mammary tumor virus to TLR4 up regulated expression of the MMTV entry receptor (CD71) on bone marrow derived dendritic cells PMID: 14694089
hepcidin transgene expression decreases transferrin receptor 1 mRNA level in placenta PMID: 15358563
Dcytb, DMT1, Ireg1 and transferrin receptor 1 have roles in iron transport and hemolysis PMID: 15469906
TfR1 expression is attenuated in a cell-density-dependent manner in human lung cancer H1299 cells and in murine B6 fibroblasts as the result of a marked decrease in mRNA content. PMID: 16092918
the site of interaction with MMTV maps to two segments physically disparate from the TfR and HFE binding sites PMID: 16481319
HFE and TFR2 interact in cells; this interaction is not abrogated by disease-associated mutations of HFE and TFR2; and that TFR2 competes with TFR1 for binding to HFE PMID: 16893896
These data indicate that rapid transferrin recycling is defective after pSec15l1 has mutated. PMID: 17087999
Although expression of high levels of sTfR1 significantly increased serum iron levels, repeated experiments showed that neither hsTfR1 nor msTfR1 gene expression had any effect on iron absorption or hepcidin mRNA expression levels. PMID: 17119325
Mammalian cells utilize transferrin-dependent mechanisms to acquire iron via transferrin receptors 1 and 2 (TfR1 and TfR2) by receptor-mediated endocytosis. PMID: 17121833
The modified vectors containing Q-dots demonstrated 32-fold greater tumor-targeting efficiency than wild-type HVJ-E. PMID: 17961511
comparison of the abilities of TfR1 orthologs from different species to support arenavirus entry found that the human and feline receptors were able to enhance entry of the pathogenic strains, but that neither the murine or canine forms were functional. PMID: 18003730
Iron chelation alters expression of Tfrc. PMID: 18029550
Suggest that Hfe induces hepcidin expression when it is not in complex with Tfr1. PMID: 18316026
an interplay of the HIF-1 and NF-kappaB pathways controls TfR1 transcription in inflammation PMID: 18519569
increased mitochondrial Fe in the myocardium of mutants was due to marked transferrin Fe uptake, which was the result of enhanced transferrin receptor 1 expression PMID: 18621680
Transferrin receptor can be used as a specific target for molecular imaging in CIA mouse, and 99mTc-Tf scintigraphy detects synovial inflammation prior to significant clinical findings in collagen-induced arthritis mouse. PMID: 18696076
Mouse mammary tumor virus uses TfR1 for all steps of entry: cell attachment, induction of the conformational changes in Env required for membrane fusion and internalization to an appropriate acidic compartment PMID: 18829060
Results indicate that TfR promotes glioma progression by two mechanisms, an increase in proliferation rate and glutamate production, the latter mechanism providing space for the progressing tumor mass. PMID: 19066835

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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.

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