Recombinant Mouse TfR Protein (N-8His)

Beta LifeScience SKU/CAT #: BL-1839NP
BL-1839NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-1839NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Mouse TfR Protein (N-8His)

Beta LifeScience SKU/CAT #: BL-1839NP
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Product Overview

Description Recombinant Mouse Transferrin Receptor Protein 1 is produced by our Mammalian expression system and the target gene encoding Cys89-Phe763 is expressed with a 8His tag at the N-terminus.
Accession Q62351
Synonym Transferrin receptor protein 1; TR; TfR; TfR1; Trfr; CD71; Tfrc
Gene Background Transferrin receptor protein 1 (TFRC) belongs to the peptidase M28 family that is synthesized as a 172 amino acid (aa). TFRC regulated by cellular iron levels through binding of the iron regulatory proteins, IRP1 and IRP2, to iron-responsive elements in the 3'-UTR. It binds one transferrin or HFE molecule per subunit and binds the HLA class II histocompatibility antigen, DR1. It Interacts with SH3BP3 and STEAP3, facilitates TFRC endocytosis in erythroid precursor cells. 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. A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. It positively regulates T and B cell proliferation through iron uptake.
Molecular Mass 77 KDa
Apmol Mass 90 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 5% Trehalose, 5% Mannitol, 0.01% tween80, pH 7.4.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

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

Gene Functions References

  1. duodenal Regnase-1 controls the expression of PHD3, which impairs duodenal iron uptake via HIF2alpha suppression. PMID: 28538180
  2. role in the development of hypoxia-induced pulmonary vascular remodeling PMID: 26419445
  3. Knock-out of TFR1 in Purkinje cells reduces mGlu1 expression at synapses and impairs motor coordination. PMID: 29054881
  4. 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
  5. our study reveals that TFR functions as a novel regulator to control AMPA trafficking efficiency and synaptic plasticity PMID: 26880306
  6. 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
  7. 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
  8. Transferrin Receptor 1 Facilitates Poliovirus Permeation of Mouse Brain Capillary Endothelial Cells. PMID: 26637351
  9. Erythrocytic iron deficiency enhances susceptibility to Plasmodium chabaudi infection in mice carrying a missense mutation in tfr1. PMID: 26303393
  10. 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
  11. 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
  12. 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
  13. 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
  14. 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
  15. high-affinity anti-TfR alters TfR trafficking, which dramatically impacts the capacity for TfR to mediate blood-brain barrier transcytosis PMID: 24470444
  16. 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
  17. Knockdown of Rab12 increased transferrin receptor level and reduced M98K-induced cell death. PMID: 23357852
  18. 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
  19. In a model of celiac disease, gluten induces enterocyte CD71 overexpression. PMID: 22330344
  20. 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
  21. 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
  22. Vitamin C increases the expression of the iron-regulated hormone hepcidin and decreases transferrin receptor 1 (TfR1) expression in liver. PMID: 21078691
  23. 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
  24. 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
  25. soluble transferrin receptor represents a valuable quantitative assay of marrow erythropoietic activity as well as a marker of tissue iron deficiency PMID: 12589962
  26. 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
  27. 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
  28. hepcidin transgene expression decreases transferrin receptor 1 mRNA level in placenta PMID: 15358563
  29. Dcytb, DMT1, Ireg1 and transferrin receptor 1 have roles in iron transport and hemolysis PMID: 15469906
  30. 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
  31. the site of interaction with MMTV maps to two segments physically disparate from the TfR and HFE binding sites PMID: 16481319
  32. 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
  33. These data indicate that rapid transferrin recycling is defective after pSec15l1 has mutated. PMID: 17087999
  34. 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
  35. Mammalian cells utilize transferrin-dependent mechanisms to acquire iron via transferrin receptors 1 and 2 (TfR1 and TfR2) by receptor-mediated endocytosis. PMID: 17121833
  36. The modified vectors containing Q-dots demonstrated 32-fold greater tumor-targeting efficiency than wild-type HVJ-E. PMID: 17961511
  37. 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
  38. Iron chelation alters expression of Tfrc. PMID: 18029550
  39. Suggest that Hfe induces hepcidin expression when it is not in complex with Tfr1. PMID: 18316026
  40. an interplay of the HIF-1 and NF-kappaB pathways controls TfR1 transcription in inflammation PMID: 18519569
  41. 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
  42. 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
  43. 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
  44. 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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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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