A1900
Albumin, Monomer bovine
Monomer ≥97 %
Synonym(s):
Albumin powder, Bovine albumins
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About This Item
CAS Number:
UNSPSC Code:
12352202
eCl@ss:
42010201
EC Number:
232-936-2
NACRES:
NA.26
MDL number:
Biological source:
bovine
Assay:
≥97% (PAGE)
Form:
lyophilized powder
Technique(s):
SDS-PAGE: suitable
biological source
bovine
Quality Level
assay
≥97% (PAGE)
form
lyophilized powder
composition
Monomer, ≥97%
technique(s)
SDS-PAGE: suitable
solubility
H2O: soluble 50 mg/mL
UniProt accession no.
storage temp.
2-8°C
Gene Information
bovine ... ALB(280717)
General description
The most abundant plasma protein in mammals is albumin. It is produced in the liver and transferred as a non-glycosylated protein into the plasma. This multifunctional protein can bind to ligands.
Application
Albumin, Monomer bovine has been used as a:
- molecular weight (MW) and polydispersion index (PDI) reference standard for the analysis of hyaluronic acid (HA)-based eye drops
- standard in multi-angle light scattering coupled with size exclusion chromatography (SEC-MALS) for calibration
- model protein to generate subvisible particles (SVPs) for flow imaging microscopy studies
The binding properties of albumin can be used for a wide range of clinical, pharmaceutical, and biochemical applications.
Biochem/physiol Actions
Albumin is the most important circulatory protein involved in the control of Ca2+ (and Mg2+) levels in mammals.
Preparation Note
Isolated from albumin (A4503) as described for mercaptalbumin in Janatova, J., et al., J. Biol. Chem., 243, 3612 (1968).
Storage Class
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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Piramon Hampitak et al.
ACS sensors, 5(11), 3520-3532 (2020-10-27)
We present a sensitive and low-cost immunoassay, based on a customized open-source quartz crystal microbalance coupled with graphene biointerface sensors (G-QCM), to quantify antibodies in undiluted patient serum. We demonstrate its efficacy for a specific antibody against the phospholipase A2
Joe A Kaczmarski et al.
Nature communications, 11(1), 5945-5945 (2020-11-25)
Several enzymes are known to have evolved from non-catalytic proteins such as solute-binding proteins (SBPs). Although attention has been focused on how a binding site can evolve to become catalytic, an equally important question is: how do the structural dynamics
Yu Isakari et al.
Biotechnology journal, 13(7), e1700738-e1700738 (2018-02-03)
Combining chemical reaction with separation offers several advantages. In this work possibility to induce spontaneous desorption of adsorbed macromolecules, once being PEGylated, through adjustment of the reagent composition is investigated. Bovine serum albumin (BSA) and activated oligonucleotide, 9T, are used
Surendra Dasari et al.
Journal of proteome research, 8(3), 1263-1270 (2009-01-29)
A robust peptide quantification method was developed where overlapping peptide isotopic distributions were fit with predicted peptide isotopic envelope mixture models (IEMMs). Application to two difficult quantitative problems was demonstrated. The first was the quantification of deamidation, where masses of
Manuel Maestre-Reyna et al.
IUBMB life, 73(2), 418-431 (2020-12-30)
Vibrio cholerae is the causative agent of the diarrheal disease cholera, for which biofilm communities are considered to be environmental reservoirs. In endemic regions, and after algal blooms, which may result from phosphate enrichment following agricultural runoff, the bacterium is
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