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A6784

Sigma-Aldrich

Albumin solution human

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

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Synonym(s):
HSA
CAS Number:
MDL number:
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)

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This Item
A8763A9080A9511
Albumin solution human 10% in 0.85% sodium chloride and 0.05% sodium azide, aseptically filled

Sigma-Aldrich

A6784

Albumin solution human

Albumin solution human 30% in 0.85% sodium chloride, protease free

Sigma-Aldrich

A9080

Albumin solution human

sterility

aseptically filled

sterility

-

sterility

-

sterility

-

form

liquid

form

lyophilized powder

form

liquid

form

lyophilized powder

concentration

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

concentration

-

concentration

29.5-35.0% protein (biuret), 30% in 0.85% sodium chloride

concentration

-

technique(s)

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

technique(s)

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

technique(s)

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

technique(s)

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

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

HIV I and HIVII, HCV and HBsAg, tested negative

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.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Customers Also Viewed

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
Juan C Segoviano-Ramirez et al.
Journal of diabetes research, 2020, 4827641-4827641 (2020-03-20)
Type 2 diabetes mellitus (DM2) is a disease that reports high morbidity and mortality rates worldwide. Between its complications, one of the most important is the development of plantar ulcers. The role of the polymorphonuclear cells (PMNs) is affected by

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