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TFRC Antibody

Mouse Monoclonal Antibody (Mab)

     
  • 1 - TFRC Antibody AM2075B
    All lanes : Anti-CD71 Antibody (C-term) at 1:1000 dilution Lane 1: HT-1080 whole cell lysate Lane 2: Hela whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-mouse IgM, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 85 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 1 - TFRC Antibody AM2075B
    TFRC Antibody (Cat. #AM2075b) western blot analysis in WiDr cell line lysates (35μg/lane).This demonstrates the TFRC antibody detected the TFRC protein (arrow).
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession P02786
Other Accession NP_001121620.1
Reactivity Human
Host Mouse
Clonality Monoclonal
Isotype IgM
Clone Names 514CT23.4.1
Calculated MW 84871 Da
Antigen Region 649-677 aa
Additional Information
Gene ID 7037
Other Names Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, p90, CD71, Transferrin receptor protein 1, serum form, sTfR, TFRC
Target/Specificity This TFRC antibody is generated from mice immunized with a KLH conjugated synthetic peptide between 649-677 amino acids from human TFRC.
Dilution WB~~1:500~1000
E~~Use at an assay dependent concentration.
Format Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Euglobin precipitation followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsTFRC Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name TFRC
Function Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (PubMed:26214738). 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 (By similarity). A second ligand, the hereditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C- terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (PubMed:26214738). 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 (PubMed:26214738). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (PubMed:26214738). Mediates uptake of NICOL1 into fibroblasts where it may regulate extracellular matrix production (By similarity).
Cellular Location Cell membrane; Single-pass type II membrane protein Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

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 (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site.

REFERENCES

Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Ucisik-Akkaya, E., et al. Mol. Hum. Reprod. 16(10):770-777(2010)
Blonde-Cynober, F., et al. Ann. Biol. Clin. (Paris) 68(5):569-575(2010)
Marsee, D.K., et al. Am. J. Clin. Pathol. 134(3):429-435(2010)
Fernandez-Real, J.M., et al. Eur. J. Clin. Invest. 40(7):600-607(2010)

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