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A9511

Sigma-Aldrich

Albumin from human serum

lyophilized powder, ≥97% (agarose gel electrophoresis)

Synonym(s):

HSA

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About This Item

CAS Number:
70024-90-7
EC Number:
274-272-6
MDL number:
MFCD00081418
UNSPSC Code:
12352202
eCl@ss:
42010201
NACRES:
NA.25

biological source

human

Quality Level

300

Assay

≥97% (agarose gel electrophoresis)

form

lyophilized powder

mol wt

monomer calculated mol wt 66478 Da

technique(s)

ELISA: suitable
tissue culture: suitable
western blot: suitable

impurities

HIV I and HIVII, HCV and HBsAg, tested negative

solubility

H2O: soluble 50 mg/mL

UniProt accession no.

P02768

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 is the most copious protein in blood plasma. Liver produces human albumin.
Human albumin possess a molecular weight of 67 kDa.

Application

Albumin from human serum has been used:
  • to standardize the column for molecular-exclusion chromatography
  • to prepare the tobacco mosaic virus (TMV)-poly ethylene glycol (PEG8)-serum albumin (SA) particles
  • to analyze its modifications after oxidation using a Fenton system

Albumin-bound fluorescence was used in serum of patients with chronic renal failure.

Biochem/physiol Actions

Albumin turnover is seen in infants with iron deficiency anemia. Serum albumin is a reliable prognostic indicator in liver disease. Oxidative modification of albumin is seen in advanced liver disease.
Serum albumin functions as a carrier protein for steroids, fatty acids, and thyroid hormones, and is vital in regulating the colloidal osmotic pressures of blood. Albumin is also seen to bind to exogenous substances, particularly drugs (e.g., ibuprofen, warfarin), and strongly influence their pharmacokinetics. Oxidative stress leading to changes in the redox state of albumin has widely varied effects on its physiological function.

Preparation Note

Prepared using method IV of Cohn, E.J., et al., J. Am. Chem. Soc., 69, 1753 (1947).

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

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Effects of Fenton Reaction on Human Serum Albumin: An In Vitro Study
Khosravifarsani M, et al.
Electron Physician, 8(9), 2970-2970 (2016)
Serum albumin camouflage of plant virus based nanoparticles prevents their antibody recognition and enhances pharmacokinetics
Pitek A, et al.
Biomaterials, 89(7-8), 89-97 (2016)
Elham Behzadi et al.
International journal of nanomedicine, 14, 257-270 (2019-01-16)
Recently, nanomaterials have moved into biological and medicinal implementations like cancer therapy. Therefore, before clinical trials, their binding to plasma proteins like human serum albumin (HSA) and their cytotoxic effects against normal and cancer cell lines should be addressed. Herein
H A Schwertner et al.
Clinical chemistry, 26(5), 649-652 (1980-04-01)
A band that is strongly fluorescent and migrates electrophoretically with serum albumin is commonly found in electrophoretograms of sera from patients with chronic renal failure. We sought to determine whether the fluorescence originates from binding of certain still-unidentified metabolites or
Daniele Sanna et al.
Inorganic chemistry, 49(1), 174-187 (2009-12-02)
The possible biotransformations in the blood serum of four representative insulin-enhancing vanadium compounds, [VO(6-mepic)(2)], cis-[VO(pic)(2)(H(2)O)], [VO(acac)(2)], and [VO(dhp)(2)], where 6-mepic, pic, acac, and dhp indicate the deprotonated forms of 6-methylpicolinic and picolinic acids, acetylacetone, and 1,2-dimethyl-3-hydroxy-4(1H)-pyridinone, were examined. In particular
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