A3559
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
Produits recommandés
Source biologique
mouse
Niveau de qualité
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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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.
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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Les clients ont également consulté
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
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Journal of Orthopaedic Research : Official Publication of the Orthopaedic Research Society, 41, 1565-1581 (2023)
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
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
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