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A1653

Sigma-Aldrich

Albumin from human serum

lyophilized powder, ≥96% (agarose gel electrophoresis)

Synonym(s):

HSA

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250 μG
CN¥4,489.38

CN¥4,489.38

Estimated to ship onMay 16, 2025Details

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250 μG
CN¥4,489.38

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

CN¥4,489.38

Estimated to ship onMay 16, 2025Details

Request a Bulk Order

biological source

human

Quality Level

300

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.

P02768

storage temp.

2-8°C

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This Item
A9511A4327A8301
Albumin from human serum lyophilized powder, ≥96% (agarose gel electrophoresis)

A1653

Albumin from human serum

Albumin from human serum lyophilized powder, ≥97% (agarose gel electrophoresis)

A9511

Albumin from human serum

Albumin from human serum lyophilized powder, essentially protease free, ≥96% (agarose gel electrophoresis)

A4327

Albumin from human serum

Albumin, glycated human lyophilized powder

A8301

Albumin, glycated human

assay

≥96% (agarose gel electrophoresis)

assay

≥97% (agarose gel electrophoresis)

assay

≥96% (agarose gel electrophoresis)

assay

90-100% protein basis (biuret)

biological source

human

biological source

human

biological source

human

biological source

human

technique(s)

ELISA: suitable, western blot: suitable, tissue culture: suitable

technique(s)

ELISA: suitable, tissue culture: suitable, western blot: suitable

technique(s)

tissue culture: suitable

technique(s)

cell culture | mammalian: suitable

Quality Level

300

Quality Level

300

Quality Level

200

Quality Level

200

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

impurities

HIV I and HIVII, HCV and HBsAg, tested negative

impurities

HIV I and HIVII, HCV and HBsAg, tested negative

impurities

HIV I and HIVII, HCV and HBsAg, tested negative

impurities

-

General description

Albumin (ALB) constitutes 25% of the proteins produced by the liver.[1] It is a protein of a single polypeptide chain with a thiol group.[2] The ALB gene is mapped to human 4q13.3.[3]

Application

Albumin from human serum has been used:
  • in cyclophilin isomerase assay[4]
  • as a component in blocking solution for immunogold quantification of amino acids and proteins in complex subcellular compartments[5]
  • in G-pseudotyped HIV (PHIV) assay mixture to study its effect on GSK364735 antiviral potency[6]

Albumin was used to test its effect on the in vitro bactericidal activity of cefditoren against penicillin-resistant Streptococcus pneumonia.[7]
It has been clinically used in serious and often life-threatening conditions, such as shock and blood loss due to trauma, burns, and surgery.[8]

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.[9] Pathological conditions like vasculitis, lymphangiectasia, glomerulonephritis, and hepatic sinusoidal hypertension might result in hypoalbuminemia.[1]
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.
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

Regulatory Information

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    0000440433
    0000440435

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    Serum proteins and the dysproteinemias
    Clinical biochemistry of domestic animals, 117-138 (1997)
    Fluid, electrolyte, and acid-base disturbances in liver disease
    Fluid, Electrolyte, and Acid-Base Disorders in Small Animal Practice, 456-456 (2011)
    János P Mészáros et al.
    Journal of inorganic biochemistry, 195, 91-100 (2019-04-01)
    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
    Abnormalities of plasma proteins
    Scientific Foundations of Biochemistry in Clinical Practice, 464-494 (1994)
    Angelo Zinellu et al.
    European journal of nutrition, 56(2), 785-791 (2015-12-15)
    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
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