Native Bovine TF Protein TF-01B

Native Bovine TF Protein

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Native Bovine TF Protein

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Cat.No. : TF-01B
Product Overview : Native Bovine TF Protein
Description : Transferrins are iron binding transport proteins which can bind two Fe3+ 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.
Species : Bovine
Form : Sterile Filtered Pink lyophilized (freeze-dried) powder.
Molecular Mass : 80 kDa
Purity : > 97% as determined by Cellulose Acetate.
Applications : Bovine Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.
Storage : Lyophilized Bovine HTF although stable at room temperature for 3 weeks, should be stored desiccated below -18 centigrade. Upon reconstitution Bovine HTF should be stored at 4 centigrade between 2-7 days and for future use below -18 centigrade.Please prevent freeze-thaw cycles.
Concentration : 1 mg/mL
Gene Name : TF transferrin [ Bos taurus (cattle) ]
Official Symbol : TF
Synonyms : TF; transferrin; serotransferrin; beta-1 metal-binding globulin; siderophilin
Gene ID : 280705
mRNA Refseq : NM_177484
Protein Refseq : NP_803450
UniProt ID : Q29443
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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