Recombinant Mouse TfR Protein (N-8His)

Name: Recombinant Mouse TfR Protein (N-8His)
Brand: Beta LifeScience
SKU: BL-1839NP
Availability: InStock

BL-1839NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, High-quality recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

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	KEGG: mmu:22042 STRING: 10090.ENSMUSP00000023486 UniGene: 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

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.