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A6608

Sigma-Aldrich

Albumin human

recombinant, expressed in Saccharomyces cerevisiae, aqueous solution, 10% in aqueous buffer, ≥99% (agarose gel electrophoresis)

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Synonym(s):
rHSA
Empirical Formula (Hill Notation):
C2936H4624N786O889S41
CAS Number:
Molecular Weight:
66471.53
MDL number:
UNSPSC Code:
12352202
eCl@ss:
42010201
NACRES:
NA.25

biological source

human

Quality Level

recombinant

expressed in Saccharomyces cerevisiae

Assay

≥99% (agarose gel electrophoresis)

form

aqueous solution

mol wt

monomer ~67 kDa

concentration

10% in aqueous buffer

technique(s)

cell culture | mammalian: suitable

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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General description

Albumin constitutes 25% of the proteins produced by the liver and is a prominent protein found in the blood. It is a protein of a single polypeptide chain with a thiol group.

Application

Albumin human has been used:
  • to study its adsorption process on model mica surface at pH 3.5 using the atomic force microscopy (AFM) and in situ streaming potential measurements
  • to study its proteolytic activities under reducing conditions
  • in the medium for stem cell cultivation

This recombinant variant is recommended for use in absorption, distribution, metabolism, and excretion (ADME) pharmacological research; cell culture; drug delivery research; and cryopreservation of cells.

Biochem/physiol Actions

Albumin is a binding and transport protein that serves as a protein repository and a carrier for amino acids. Albumin binding dissolves the biomolecules in blood and ensures its effective transport. This also prevents the loss of substance through excretion. Pathological conditions like vasculitis, lymphangiectasia, glomerulonephritis, and hepatic sinusoidal hypertension might result in hypoalbuminemia. This product can be used in the pharmaceutical industry as a drug excipient and to coat medical devices.
Albumins are soluble monomeric proteins found in the body fluids and tissues of animals and in some plant seeds. Serum albumin functions as a carrier protein for steroids, fatty acids, and thyroid hormones. Serum albumins are also vital in regulating the colloidal osmotic pressures of blood.

Analysis Note

Endotoxin tested

Other Notes

View more information on human serum albumin.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

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Dmitry Kryndushkin et al.
Pharmaceutical research, 33(2), 526-539 (2015-10-27)
Ascorbic acid has been considered as a potential radical scavenging excipient for pharmaceutical formulations. However, under certain circumstances, ascorbic acid can generate reactive oxygen species via redox cycling. The objective of this study was to investigate ascorbic acid-induced oxidative carbonylation
Dmitry Kryndushkin et al.
Pharmaceutical research, 34(4), 765-779 (2017-02-06)
Protein carbonylation is an irreversible modification of Lys, Arg, Thr and Pro amino acids under conditions of oxidative stress. Previous studies have reported specific carbonylated residues in purified recombinant albumins, albeit with a lack of agreement between the studies. Currently
N A Pham et al.
Cytometry, 41(4), 245-251 (2000-11-21)
Increased mitochondrial generation of reactive oxygen intermediates (ROI) due to defective respiratory chain activity has been implicated in physiological processes such as apoptosis, in the pathogenesis of mitochondrial diseases, and as part of the normal aging process. Established methods addressing
Marta Kujda et al.
Colloids and surfaces. B, Biointerfaces, 127, 192-199 (2015-02-14)
Recombinant human serum albumin (rHSA) in monomeric state is widely used in pharmaceutical industry as a drug excipient and for preparing coatings for medical devices. In this work the adsorption process of rHSA on model mica surface at pH 3.5
Abnormalities of plasma proteins
Scientific Foundations of Biochemistry in Clinical Practice, 464-494 (1994)

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