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Human Transferrin, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Human Transferrin, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Human Transferrin, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.

Human Transferrin Protein, His Tag (MALS verified)

Research Use Only
TRN-H4229
ACRObiosystems
Product group Proteins / Signaling Molecules
Price on request
Packing Size
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Overview

  • Supplier
    ACRObiosystems
  • Product Name
    Human Transferrin Protein, His Tag (MALS verified)
  • Delivery Days Customer
    4
  • Category Supplier
    Cytokines&Growth Factors
  • Certification
    Research Use Only
  • Estimated Purity
    95%
  • Format
    Powder
  • Scientific Description
    Characteristics: This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 76.0 kDa. The protein migrates as 70-90 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. Description: Transferrin is also known as Serotransferrin, Beta-1 metal-binding globulin, TF, and is iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. Although iron bound to transferrin is less than 0.1% (4 mg) of the total body iron, it is the most important iron pool, with the highest rate of turnover (25 mg/24 h). The affinity of transferrin for Fe(III) is extremely high (1023 M−1 at pH 7.4) but decreases progressively with decreasing pH below neutrality.When not bound to iron, it is known as "apo-transferrin”. In humans, transferrin consists of a polypeptide chain containing 679 amino acids. It is a complex composed of alpha helices and beta sheets to form two domains (the first situated in the N-terminus and the second in the C-terminus). The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site. The liver is the main source of manufacturing transferrin, but other sources such as the brain also produce this molecule . Transferrin is also associated with the innate immune system. Transferrin is found in the mucosa and binds iron, thus creating an environment low in free iron that impedes bacteria survival in a process called iron withholding. The level of transferrin decreases in inflammation. The metal binding properties of transferrin have a great influence on the biochemistry of plutonium in humans. Transferrin has a bacteriocidal effect on bacteria, in that it makes Fe3+ unavailable to the bacteria.Carbohydrate deficient transferrin increases in the blood with heavy ethanol consumption and can be monitored via laboratory testing.
  • Shelf life instruction
    ● -20°C to -70°C for 12 months in lyophilized state; ● -70°C for 3 months under sterile conditions after reconstitution. For long term storage, the product should be stored at lyophilized state at -20°C or lower.
  • Source
    Human Transferrin, His Tag (TRN-H4229) is expressed from human 293 cells (HEK293). It contains AA Val 20 - Pro 698 (Accession # AAH59367).
  • Storage Instruction
    -20℃
  • UNSPSC
    12352202