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Merck

A9080

Sigma-Aldrich

Albumin solution human

30% in 0.85% sodium chloride, protease free

Synonym(s):

HSA

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.25

Pricing and availability is not currently available.

biological source

human

Quality Level

form

liquid

concentration

29.5-35.0% protein (biuret)
30% in 0.85% sodium chloride

technique(s)

ELISA: suitable
tissue culture: suitable
western blot: suitable

impurities

HIV I and HIVII, HCV and HBsAg, tested negative

UniProt accession no.

storage temp.

2-8°C

SMILES string

FC(F)(F)C(F)(F)C(F)(F)F

InChI

1S/C3F8/c4-1(5,2(6,7)8)3(9,10)11

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General description

Albumin is the most copious protein in blood plasma. Liver produces human albumin.[1] Human serum albumin undergoes three different post-translational modifications: oxidation, glycation, and S-nitrosylation. Modifications usually occur on the surface of the globular protein, and do not significantly affect conformation. However, modification strongly affects binding of fatty acids and drug molecules.
Human serum albumin undergoes three different post-translational modifications: oxidation, glycation, and S-nitrosylation. Modifications usually occur on the surface of the globular protein, and do not significantly affect conformation. However, modification strongly affects binding of fatty acids and drug molecules.

Other Notes

View more information on human serum albumin.

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Copper-binding properties of bovine serum albumin and its amino-terminal peptide fragment.
T Peters et al.
The Journal of biological chemistry, 242(7), 1574-1578 (1967-04-10)
A A Spector et al.
Journal of lipid research, 10(1), 56-67 (1969-01-01)
We have studied the binding of long-chain free fatty acids (FFA) to crystalline bovine serum albumin (BSA) that had been extracted with charcoal to remove endogenous fatty acids. The data were analyzed in terms of a model consisting of six
T. Scott and M. Eagleson
Concise encyclopedia of biochemistry, 19-20 (1988)
Harald Olsen et al.
BMC clinical pharmacology, 4, 4-4 (2004-03-30)
Albumin is the most abundant protein in blood plasma, and due to its ligand binding properties, serves as a circulating depot for endogenous and exogenous (e.g. drugs) compounds. Hence, the unbound drug is the pharmacologically active drug. Commercial human albumin

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