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A9080

Sigma-Aldrich

Albumin solution human

30% in 0.85% sodium chloride, protease free

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Synonym(s):
HSA
CAS Number:
MDL number:
NACRES:
NA.25

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

InChI

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

InChI key

QYSGYZVSCZSLHT-UHFFFAOYSA-N

Gene Information

human ... ALB(213)

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This Item
A8763A5843B8894
Albumin solution human 30% in 0.85% sodium chloride, protease free

Sigma-Aldrich

A9080

Albumin solution human

form

liquid

form

lyophilized powder

form

lyophilized powder

form

solution

concentration

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

concentration

-

concentration

-

concentration

20 mg/mL in H2O

technique(s)

ELISA: suitable, tissue culture: suitable, western blot: suitable

technique(s)

ELISA: suitable, tissue culture: suitable, western blot: suitable

technique(s)

-

technique(s)

FISH: suitable

impurities

HIV I and HIVII, HCV and HBsAg, tested negative

impurities

HIV I and HIVII, HCV and HBsAg, tested negative

impurities

HIV I and HIVII, HCV and HBsAg, tested negative, ≤1.0 EU/mg endotoxin

impurities

HIV I and HIVII, HCV and HBsAg, tested negative

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

General description

Albumin is the most copious protein in blood plasma. Liver produces human albumin. 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.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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rAlbumin human United States Pharmacopeia (USP) Reference Standard

USP

1012595

rAlbumin human

Protein Standard analytical standard, 80 mg/mL (HSA and gamma-globulins)

Supelco

P8119

Protein Standard

Albumin human recombinant, expressed in Pichia pastoris, lyophilized powder, ≥90% (agarose gel electrophoresis)

Sigma-Aldrich

A7736

Albumin human

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)
Víctor Collado-Díaz et al.
Frontiers in pharmacology, 12, 613449-613449 (2021-04-20)
The cardiovascular toxicity of Abacavir is related to its purinergic structure. Purinergic P2X7-receptors (P2X7R), characterized by activation by high concentrations of ATP and with high plasticity, seem implicated. We appraise the nature of the interplay between Abacavir and P2X7R in
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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