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Merck

A9080

Albumin solution human

30% in 0.85% sodium chloride, protease free

Sinónimos:

HSA

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About This Item

Número CAS:
70024-90-7
UNSPSC Code:
12352202
NACRES:
NA.25
MDL number:
MFCD00081418

Nombre del producto

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

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

InChI key

QYSGYZVSCZSLHT-UHFFFAOYSA-N

biological source

human

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.

P02768

storage temp.

2-8°C

Quality Level

200

Gene Information

human ... ALB(213)

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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.

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.

Clase de almacenamiento

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificados de análisis (COA)

Lot/Batch Number
0000349249
0000349249
0000366702
0000366702
SLCQ1853

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Visite la Librería de documentos

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)
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)
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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