A9511
Albumin from human serum
lyophilized powder, ≥97% (agarose gel electrophoresis)
Synonym(s):
HSA
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About This Item
CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
eCl@ss:
42010201
NACRES:
NA.25
Recommended Products
biological source
human
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.
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)
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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
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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
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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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