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A1653

Sigma-Aldrich

Albumin from human serum

lyophilized powder, ≥96% (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

biological source

human

Assay

≥96% (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 (ALB) constitutes 25% of the proteins produced by the liver. It is a protein of a single polypeptide chain with a thiol group. The ALB gene is mapped to human 4q13.3.

Application

Albumin from human serum has been used:
  • in cyclophilin isomerase assay
  • as a component in blocking solution for immunogold quantification of amino acids and proteins in complex subcellular compartments
  • in G-pseudotyped HIV (PHIV) assay mixture to study its effect on GSK364735 antiviral potency

Albumin was used to test its effect on the in vitro bactericidal activity of cefditoren against penicillin-resistant Streptococcus pneumonia.
It has been clinically used in serious and often life-threatening conditions, such as shock and blood loss due to trauma, burns, and surgery.

Biochem/physiol Actions

Albumin serves as a protein repository and functions as a binding and transport protein. Albumin binding dissolves the biomolecules in blood and ensures its effective transport. This prevents the loss of substance through excretion. Pathological conditions like vasculitis, lymphangiectasia, glomerulonephritis, and hepatic sinusoidal hypertension might result in hypoalbuminemia.
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.

Quality

Remainder mostly globulins

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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Half-sandwich organometallic complexes of curcumin are extensively investigated as anticancer compounds. Speciation studies were performed to explore the solution stability of curcumin complexes formed with [Rh(η5-C5Me5)(H2O)3]2+. Acetylacetone (Hacac), as the simplest β-diketone ligand bearing (O,O) donor set, was involved for
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The dietary flavonoids epicatechin (EC), epigallocatechin (EGC), epicatechin gallate (ECG) and epigallocatechin gallate (EGCG) have been shown to interact with circulating albumin for transport in blood to different body tissues. This interaction may modulate their bioavailability and effectiveness. Using affinity
Abnormalities of plasma proteins
Scientific Foundations of Biochemistry in Clinical Practice, 464-494 (1994)
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