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A3559

Sigma-Aldrich

Albumin from mouse serum

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

Synonyme(s) :

Mouse albumin

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About This Item

Numéro CAS:
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.27

Source biologique

mouse

Pureté

≥99% (agarose gel electrophoresis)

Forme

lyophilized powder

Technique(s)

immunohistochemistry: suitable

Numéro d'accès UniProt

Température de stockage

2-8°C

Informations sur le gène

mouse ... ALB(11657)

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Catégories apparentées

Description générale

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

Actions biochimiques/physiologiques

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

Notes préparatoires

Prepared from albumin (A3139).

Autres remarques

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.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

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
Steven A Jacobs et al.
Protein engineering, design & selection : PEDS, 28(10), 385-393 (2015-08-16)
A number of classes of proteins have been engineered for high stability using consensus sequence design methods. Here we describe the engineering of a novel albumin binding domain (ABD) three-helix bundle protein. The resulting engineered ABD molecule, called ABDCon, is
Optimizing the synthesis of interleukin-12-loaded PLGA nanospheres (rmIL-12ns) via ultrasonication for treatment of metastatic osteosarcoma.
Lacinski, et al.
Journal of Orthopaedic Research : Official Publication of the Orthopaedic Research Society, 41, 1565-1581 (2023)
Tamara K Nowling et al.
PloS one, 15(3), e0230499-e0230499 (2020-03-19)
Glycosphingolipids (GSLs) hexosylceramides and lactosylceramides are elevated in lupus mice and human patients with nephritis. Whereas other renal diseases characterized by increased GSL levels are thought to be a result of upregulated GSL synthesis, our results suggest elevated hexosylceramides and
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

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