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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
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)
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
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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