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A3559

Sigma-Aldrich

Albumin from mouse serum

lyophilized powder, essentially globulin free, ≥99% (agarose gel electrophoresis)

Synonym(s):

Mouse albumin

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.27

biological source

mouse

Assay

≥99% (agarose gel electrophoresis)

form

lyophilized powder

technique(s)

immunohistochemistry: suitable

UniProt accession no.

storage temp.

2-8°C

Gene Information

mouse ... ALB(11657)

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General description

Albumin, present in the blood, is the most abundant protein. Structurally, albumin comprises three homologous domains (DI, DII, and DIII) with 67% α-helices.

Application

Albumin from mouse serum has been used:
  • as a standard in the enzyme-linked immunosorbent assay (ELISA) with urine samples
  • in the preparation of isolevuglandin (IsoLG)-albumin adducts for immunohistochemical staining of human tissue samples
  • for comparative studies with thymic stromal lymphopoietin (TSLP) to test its effect on dermal thickness in mice

Biochem/physiol Actions

Albumin transports fatty acids, drugs, and hormones. Mouse serum albumin (MSA) binds to the neonatal Fc receptor (FcRn).

Preparation Note

Prepared from albumin (A3139).

Other Notes

Albumin from mouse serum is free of globulin. It is derived from Swiss Webster strain mouse serum by cold alcohol fractionation. There are no heating steps involved in the preparation of this product.
This Fraction V albumin can be used for making immune complexes with anti-albumin antibodies. Fatty acids will not interfere with the complex formation.

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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Jeannette Nilsen et al.
Scientific reports, 8(1), 14648-14648 (2018-10-04)
Albumin has a serum half-life of three weeks in humans and is utilized to extend the serum persistence of drugs that are genetically fused or conjugated directly to albumin or albumin-binding molecules. Responsible for the long half-life is FcRn that
Jung U Shin et al.
The Journal of investigative dermatology, 136(2), 507-515 (2016-01-30)
Recently, thymic stromal lymphopoietin (TSLP), which is well studied in allergic diseases, has been reported in fibrotic diseases, including idiopathic pulmonary fibrosis and atopic dermatitis fibrosis. However, the role of TSLP in keloid is obscure. In this study, we assessed
H P Yan et al.
Free radical biology & medicine, 106, 62-68 (2017-02-13)
The cellular production of free radicals or reactive oxygen species (ROS) can lead to protein, lipid or DNA modifications and tumor formation. The cellular lipids undergo structural changes through the actions of enzymes (e.g. cyclooxygenases) or free radicals to form
Lorena Perdices et al.
Free radical biology & medicine, 124, 550-557 (2018-07-15)
Retinitis pigmentosa (RP) comprises a group of inherited retinal degenerative conditions characterized by primary degeneration of the rod photoreceptors. Increased oxidative damage is observed in the retina, aqueous humor, and plasma of RP animal models and patients. The hepatic oxidative
M Morales et al.
Neuroscience, 152(1), 70-81 (2008-01-29)
The notion of functional interactions between the alpha7 nicotinic acetylcholine (alpha7 nACh) and the cannabinoid systems is emerging from recent in vitro and in vivo studies. Both the alpha7 nACh receptor and the cannabinoid receptor 1 (CB1) are highly expressed

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