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A2514

Sigma-Aldrich

Albumin from goat

≥96% (agarose gel electrophoresis)

Synonym(s):

Albumin powder, Goat albumin

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.21

biological source

goat

Quality Level

assay

≥96% (agarose gel electrophoresis)

form

powder

storage temp.

2-8°C

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General description

Albumin is a globular protein. Serum albumin is a member of the multigene protein family. Human serum albumin (HSA) consists of three homologous domains (I-III) that form a heart-shaped structure. Each domain is a result of two subdomains called A and B. Bovine serum albumin (BSA) has a structure that is very similar to HSA as it has a heart-shaped structure that has three homologous domains (I-III) and each domain has three sub-domains.

Application

Albumin from goat has been used to verify the specificity of radioimmunoassay (RIA)-780 and 805.

Biochem/physiol Actions

Albumin is a highly soluble, multifunctional and major circulating plasma protein. It plays a role in physiological and pharmacological areas. Albumin participates in the transport of metals, cholesterol, hormones, bile pigments, drugs, and fatty acids. It regulates osmotic pressure and distributes fluids between various compartments. In addition, plasma albumin exhibits anti-oxidant effects to minimize oxidative stress. Albumin attributes to the major portion of total serum antioxidant properties.

Preparation Note

Fraction V Powder

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Bovine Serum Albumin lyophilized powder, ≥96% (agarose gel electrophoresis)

Sigma-Aldrich

A2153

Bovine Serum Albumin

Bovine Serum Albumin lyophilized powder, crystallized, ≥98.0% (GE)

Sigma-Aldrich

05470

Bovine Serum Albumin

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Abdullah Hussain et al.
Immunology, 128(2), 236-244 (2009-09-11)
Anti-proteinase 3 antibodies are implicated in the pathogenesis of small vessel vasculitis. These are primarily immunoglobulin G (IgG), with different subclasses predominating at different stages of disease. However, little is known of their respective roles in pathogenesis. We have previously
Nikolay N Brandt et al.
Journal of biomedical optics, 20(5), 051015-051015 (2014-12-06)
The analysis of the structure-function relationship is extremely important in the study of proteins. The importance of function-related motions of large parts or subglobules of protein molecules stimulates the spectroscopic study in the low-frequency (terahertz) domain. However, only tentative assignments
Claus G Madsen et al.
European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V, 92, 1-7 (2015-02-11)
This study describes how protein release from polymer matrices correlate with simple measurements on the intrinsic viscosity of the polymer solutions used for casting the matrices and calculations of the solubility parameters of polymers and solvents used. Matrices of poly(dl-lactide-co-glycolide)
Gayathri Kanika et al.
Journal of biochemical and molecular toxicology, 29(8), 349-359 (2015-03-17)
Several reports indicated that histone deacetylases (HDACs) play a crucial role in inflammation and fibrogenesis. Sodium butyrate (SB) is a short-chain fatty acid having HDAC inhibition potential. The present study aimed to evaluate the protective effect of SB against L-arginine

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