Transferrin Recombinant Protein | TF recombinant protein

Human CellExp Transferrin, human recombinant

Cat. Num. AAA844893

• Gene Names: TF; TFQTL1; PRO1557; PRO2086
• Applications: SDS-Page
• Purity: >=95%
• Synonyms: Transferrin; Human CellExp Transferrin; human recombinant; TF; DKFZp781D0156; PRO1557; PRO2086.; TF recombinant protein

• Host: HEK293 cells
• Purity/Purification: >=95%
• Form/Format: Lyophilized from 0.22 mum filtered solution in 50 mM tris, 100 mM glycine, pH 7.0. Normally Mannitol or Trehalose is added as protectants before lyophilization.; Appearance: Lyophilized
• Sequence Length: 698

• Applicable Applications for TF recombinant protein: SDS-PAGE
• Solubility/Reconstitution Instructions: Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 ug/ml. Do not vortex. This solution can be stored at 2-8 degree C for up to 1 month. For extended storage, it is recommended to store at -20 degree C.
• Endotoxin Level: <1 EU/mug by LAL method
• Handling: Centrifuge the vial prior to opening.
• Preparation and Storage: At -20 degree C; Shelf Life: 12 months

Testing Data

Related Product Information for TF recombinant protein

Background: Transferrin, 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 bactericidal 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.

Product Categories/Family for TF recombinant protein

Proteins and Enzymes; Human cell expressed recombinant proteinsProteins and Enzymes; Proteins and Enzymes (A-Z) Proteins and Enzymes; Other Proteins & Enzymes

NCBI and Uniprot Product Information

• NCBI GI #: 4557871
• NCBI GeneID: 7018
• NCBI Accession #: NP_001054.1
• NCBI GenBank Nucleotide #: NM_001063.3
• UniProt Accession #: P02787; O43890; Q1HBA5; Q9NQB8; Q9UHV0
• Molecular Weight: This protein is fused with a C-terminal 6-His tag, and has a calculated MW of 76 kDa. DTT-reduced protein migrates as 74 kDa in SDS-PAGE due to glycosylation.
• NCBI Official Full Name: serotransferrin
• NCBI Official Synonym Full Names: transferrin
• NCBI Official Symbol: TF
• NCBI Official Synonym Symbols: TFQTL1; PRO1557; PRO2086
• NCBI Protein Information: serotransferrin
• UniProt Protein Name: Serotransferrin
• Protein Family: Transferrin
• UniProt Gene Name: TF
• UniProt Synonym Gene Names: Transferrin
• UniProt Entry Name: TRFE_HUMAN

NCBI Description

This gene encodes a glycoprotein with an approximate molecular weight of 76.5 kDa. It is thought to have been created as a result of an ancient gene duplication event that led to generation of homologous C and N-terminal domains each of which binds one ion of ferric iron. The function of this protein is to transport iron from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. This protein may also have a physiologic role as granulocyte/pollen-binding protein (GPBP) involved in the removal of certain organic matter and allergens from serum. [provided by RefSeq, Sep 2009]

Uniprot Description

TF: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. Defects in TF are the cause of atransferrinemia (ATRAF). Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia. Belongs to the transferrin family.

Protein type: Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 3q22.1

Cellular Component: extracellular space; cell surface; cytoplasmic membrane-bound vesicle; early endosome; extracellular region; coated pit; recycling endosome; perinuclear region of cytoplasm; endocytic vesicle; apical plasma membrane; late endosome; basal plasma membrane; endosome membrane; vesicle

Molecular Function: protein binding; ferric iron binding; ubiquitin protein ligase binding

Biological Process: platelet activation; retinal homeostasis; platelet degranulation; cellular iron ion homeostasis; transferrin transport; blood coagulation; transmembrane transport

Disease: Atransferrinemia