Synthetic peptide corresponding to aa20-49, VPDKTVRWCAVSEHEATKCQSFRDHMKSVI, of human Transferrin at N-terminal, different from the related mouse and rat sequences by 5aa.
Transferrins are iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. In humans, it is encoded by the TF gene. Transferrin consists of a polypeptide chain containing 679aa in humans. The protein is composed of alpha helices and beta sheets to form two domains. The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site. Transferrin is a glycoprotein that binds iron very tightly but reversibly. Although iron bound to transferrin is less than 0.1% (4mg) of the total body iron, it is the most important iron pool, with the highest rate of turnover (25mg/24h). And Transferrin has a molecular weight of around 80kD and contains 2 specific high-affinity Fe(III) binding sites. The affinity of transferrin for Fe(III) is extremely high (1023M-1 at pH 7.4) but decreases progressively with decreasing pH below neutrality. Applications: Suitable for use in Western Blot, Immunohistochemistry. Other applications not tested. Recommended Dilution: Western Blot: 0.1-0.5ug/ml Immunohistochemistry (paraffin): 0.5-1ug/ml Optimal dilutions to be determined by the researcher. Storage and Stability: Lyophilized powder may be stored at -20C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Supplied as a lyophilized powder in 5mg BSA, 0.9mg sodium chloride, 0.2mg Na2HPO4, 0.05mg sodium azide. Reconstitute with 200ul sterile dH2O to ~0.5mg/ml.
* VAT and and shipping costs not included. Errors and price changes excepted
