TFRC Human, SF9
Sf9, Baculovirus cells.
Transferrin Receptor, P90, T9, TR, Transferrin Receptor (P90, CD71), Transferrin Receptor Protein 1, CD71 Antigen, IMD46, CD71, TFR1.
Greater than 90.0% as determined by SDS-PAGE.
Description
TFRC produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 669 amino acids (101-760a.a.) and having a molecular mass of 74.9kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). TFRC is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques
Product Specs
Transferrin Receptor, P90, T9, TR, Transferrin Receptor (P90, CD71), Transferrin Receptor Protein 1, CD71 Antigen, IMD46, CD71, TFR1.
Sf9, Baculovirus cells.
ADPLAGTESP VREEPGEDFP AARRLYWDDL KRKLSEKLDS TDFTGTIKLL NENSYVPREA GSQKDENLAL Recombinant Human TFRC Protein Catalog Number: ATGP3825 YVENQFREFK LSKVWRDQHFVKIQVKDSAQ NSVIIVDKNG RLVYLVENPG GYVAYSKAAT VTGKLVHANF GTKKDFEDLY TPVNGSIVIV RAGKITFAEK VANAESLNAI GVLIYMDQTK FPIVNAELSF FGHAHLGTGD PYTPGFPSFN HTQFPPSRSS GLPNIPVQTI SRAAAEKLFG NMEGDCPSDW KTDSTCRMVTSESKNVKLTV SNVLKEIKIL NIFGVIKGFV EPDHYVVVGA QRDAWGPGAA KSGVGTALLL KLAQMFSDMV LKDGFQPSRS IIFASWSAGD FGSVGATEWL EGYLSSLHLK AFTYINLDKA VLGTSNFKVS ASPLLYTLIE KTMQNVKHPV TGQFLYQDSN WASKVEKLTL DNAAFPFLAYSGIPAVSFCF CEDTDYPYLG TTMDTYKELI ERIPELNKVA RAAAEVAGQF VIKLTHDVEL NLDYERYNSQ LLSFVRDLNQ YRADIKEMGL SLQWLYSARG DFFRATSRLT TDFGNAEKTD RFVMKKLNDR VMRVEYHFLS PYVSPKESPF RHVFWGSGSH TLPALLENLK LRKQNNGAFNETLFRNQLAL ATWTIQGAAN ALSGDVWDID NEFHHHHHH.
Product Science Overview
The transferrin receptor (TfR) is a crucial protein involved in iron uptake and regulation within cells. It plays a significant role in cellular iron homeostasis by mediating the uptake of transferrin-bound iron. The recombinant form of the human transferrin receptor, expressed in Sf9 cells (a cell line derived from the fall armyworm), has been extensively studied for its applications in research and biotechnology.
The transferrin receptor is a type 2 transmembrane glycoprotein that forms a disulfide-linked homodimer, with each monomer having a molecular weight of approximately 95 kDa . It is predominantly expressed on erythroid progenitors, muscle cells, and proliferating cells . The receptor binds to transferrin, a bilobal glycoprotein that can reversibly bind iron ions (Fe3+), facilitating the transport of iron into cells .
At physiological pH (7.4), transferrin binds to the transferrin receptor on the cell surface. This complex is then internalized via clathrin-dependent endocytosis . Within the endosome, the acidic environment triggers the release of iron from transferrin, which is then reduced from Fe3+ to Fe2+ . The iron-free transferrin (apo-transferrin) and the receptor are recycled back to the cell surface, where apo-transferrin is released to bind more iron .
The expression of human transferrin receptor in Sf9 cells is a significant advancement in biotechnology. Sf9 cells, derived from the fall armyworm, are commonly used in the baculovirus expression system, which is known for its high yield and proper post-translational modifications of recombinant proteins . The recombinant transferrin receptor produced in Sf9 cells retains its functional properties, making it suitable for various research applications.
Recombinant human transferrin receptor has several applications in biomedical research and biotechnology:
- Cell Culture: It is used in serum-free cell culture media to ensure adequate iron supply, promoting cell proliferation and function .
- Drug Delivery: The receptor is explored as a target for drug delivery systems, particularly in cancer therapy, where it can facilitate the targeted delivery of therapeutic agents to proliferating cancer cells.
- Diagnostics: It is used in diagnostic assays to measure transferrin receptor levels, which can be indicative of iron status and erythropoietic activity in clinical settings.
