Skip to Content
Merck
All Photos(1)

Key Documents

A6784

Sigma-Aldrich

Albumin solution human

10% in 0.85% sodium chloride and 0.05% sodium azide, aseptically filled

Synonym(s):

HSA

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.25

biological source

human

Quality Level

sterility

aseptically filled

form

liquid

concentration

10% in 0.85% sodium chloride and 0.05% sodium azide
9.5-11.4% protein (biuret)

technique(s)

ELISA: suitable
tissue culture: suitable
western blot: suitable

impurities

HIV I and HIVII, HCV and HBsAg, tested negative

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)

Looking for similar products? Visit Product Comparison Guide

General description

Human serum albumin (HSA) is a monomeric, globular, and α-helical protein that constitutes a major part of human blood plasma proteins. This single-chain polypeptide protein contains 585 amino acid residues and 17 internal disulfide bridges and one free cysteine.
Human serum albumin undergoes three different post-translational modifications: oxidation, glycation, and S-nitrosylation. Modifications usually occur on the surface of the globular protein, and do not significantly affect conformation. However, modification strongly affects binding of fatty acids and drug molecules.

Application

Albumin solution human has been used as a supplement in RPMI 1640 media during polymorphonuclear cell (PMN) incubation. It has also been used as a culture media for the differentiation and maturation of monocyte-derived dendritic cells.

Biochem/physiol Actions

Human serum albumin (HSA) plays a vital role in the regulation of the colloidal osmotic pressure of blood. It also aids in the maintenance of metal ion homeostasis, including the transport and storage of transition metals. The high binding capacity of HSA with a wide range of ions and molecules makes it an effective molecular cargo and nano vehicle used in biophysical, clinical, and industrial fields. Human and bovine albumins contain 16% nitrogen and are often used as standards in protein calibration studies. It is used as a blocking agent in Western blots or enzyme-linked immunosorbent assay (ELISA) applications. Globulin-free albumins are suitable for use in applications where no other proteins should be present (e.g., electrophoresis).

Features and Benefits

  • Easily crystallized and contain an excess of acidic amino acids.
  • Serum and plasma albumin is carbohydrate-free and comprises 55-62% of the protein present
  • Due to its high charge to mass ratio albumin binds water, Ca2+, Na+, K+, fatty acids, bilirubin, hormones, and drugs.
  • The free hydrophobic region of fatty acid-free albumins helps to solubilize lipids in tissue culture

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

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Samah Al-Harthi et al.
Journal of inorganic biochemistry, 198, 110716-110716 (2019-06-04)
Human serum albumin (HSA) is a monomeric, globular, multi-carrier and the most abundant protein in the blood. HSA displays multiple ligand binding sites with extraordinary binding capacity for a wide range of ions and molecules. For decades, HSA's ability to

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service