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Albumin, Human Serum, Recombinant, N-terminal Deletion (HSA)

Cat no: A1274-94

Albumin, Human Serum, Recombinant, N-terminal Deletion (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. Suitable 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\nDimers and Aggregates:\n(same/less than) 1% as determined by silver-stained SDS-PAGE gel analysis.\n\nApplications:\nSuitable for use in Formulation of Protein Therapeutics, Cryopreservation Vaccine formulation and manufacturing, Development of mammalian cell cultures, Infertility treatments, Coating for medical devices, Drug delivery in vivo diagnostics. Other applications not tested.\n\nStorage and Stability:\nMay be stored at 4 degrees C. For long-term storage, aliquot and store at 4 degrees C. Do not freeze. Aliquots are stable for at least 12 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

A1274-94

Size

100mg

Form

Supplied as a liquid. No additives.

Purity

(same/more than) 95% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified.

References

1. Physicochemical characterization of cross-linked human serum albumin dimer and its synthetic heme hybrid as an oxygen carrier. Komatsu T, Oguro Y, Takeoka S, Tsuchida E, Biochim Biophys Acta 2004 Nov 18;1675 1-3:21-31 2. Application of the 19F NMR technique to observe binding of the general anesthetic halothane to human serum albumin. Shikii K, Sakurai S, Seki H, Anal Sci 2004 Oct;20(10):1475-7 3. Dioxygenation of human serum albumin having a prosthetic heme group in a tailor-made heme pocket. Komatsu T, Ohmichi N, Curry S, J Am Chem Soc 2004 Nov 10;126(44):14304-5 4. Stabilizing mechanisms in commercial albumin preparations: octanoate and N-acetyl-L-tryptophanate protect human serum albumin against heat and oxidative stress. Anraku M, Tsurusaki Y, Maruyama T, Biochim Biophys Acta 2004 Oct 1;1702(1):9-17 5. Preparation and radiolabeling of human serum albumin (HSA)-coated magnetite nanoparticles for magnetically targeted therapy. Chunfu Z, Jinquan C, Yongxian W, Appl Radiat Isot 2004 Dec;61(6):1255-9 6. Interactions of human serum albumin with chlorogenic acid and ferulic acid. Kang J, Liu Y, Li S, Biochim Biophys Acta 2004 Sep 24;1674(2):205-14.

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