Albumin, Human Serum, Recombinant, Pichia (HSA)

Contains 584 amino acid residues derived from the prototypical human serum albumin sequence, Gene Bank accession number M12523, with a single deletion of the N-terminal residue. The N-terminal deletion of Asp reduces the affinity by which nickel and copper bind to the protein. The biological properties are identical as for the full length protein.\n\nImportant Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological. inert substance used as a diluent or vehicle for a drug), culture media and chromatographic applications. Eliminating blood borne pathogens, rHSA provides major regulatory advantages and batch to batch consistency in quality and performance. Highly purified and homogeneous rHSA is produced as a single allotype.\n\nApplications:\nSuitable for use in biochemical, excipient (an inert substance used as a diluent or vehicle for a drug), culture media and chromatographic applications. Eliminating blood borne pathogens, rHSA provides major regulatory advantages and batch to batch consistency in quality and performance. Highly purified and homogeneous rHSA is produced as a single allotype.\n\nStorage and Stability:\nMay be stored at 4 degrees C. For long-term storage, aliquot and store at 4 degrees C. Aliquots are stable for at least 6 months. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

A1327-22

Size

500mg

Form

Supplied as a sterile filtered and pasteurized liquid in PBS, 4mM sodium caprylate, 4mM acetyltrytophan.

Purity

(same/more than) 95% (SDS-PAGE). Endotoxin: (same/less than) 2EU/mg. Residual Yeast Content: None detected

References

US Biological application reference: Wu, Y.W. and Tsai, Y.H. (2008) Bioconjug Chem. 19:1822-1830. 1. Dockal, D.C., Ruker, ,C.F., Conformational transitions of three recombinant domains of human serum albumin depending on pH. J. Biol. Chem. 275: 3042-3050 (200. 2. Carter DC, Ho JX. Structure of Serum Albumin. Adv. Protein Chem. 1994;45:153-203. Review. 3. Peters T., Jr All About Albumin: Biochemistry, Genetics and Medical Applications Academic Press, Inc., Orlando, FL, 1995