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Merck

A3559

Albumin from mouse serum

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

Sinónimos:

Mouse albumin

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Número CAS:
UNSPSC Code:
12352202
EC Number:
232-936-2
NACRES:
NA.27
MDL number:
eCl@ss:
32160409
Biological source:
mouse
Assay:
≥99% (agarose gel electrophoresis)
Form:
lyophilized powder
Technique(s):
immunohistochemistry: suitable
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biological source

mouse

Quality Level

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)

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.


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Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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Contenido relacionado

Product Information Sheet


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)