A1900
Albumin, Monomer bovine
Monomer ≥97 %
Synonym(s):
Albumin powder, Bovine albumins
Sign Into View Organizational & Contract Pricing
All Photos(3)
About This Item
CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
eCl@ss:
42010201
NACRES:
NA.26
Recommended Products
biological source
bovine
Quality Level
Assay
≥97% (PAGE)
form
lyophilized powder
composition
Monomer, ≥97%
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 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
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
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
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
Ming-Yuan Su et al.
Nature communications, 8(1), 1516-1516 (2017-11-16)
Peptidoglycan (PG) is a highly cross-linked, protective mesh-like sacculus that surrounds the bacterial cytoplasmic membrane. Expansion of PG is tightly coupled to growth of a bacterial cell and requires hydrolases to cleave the cross-links for insertion of nascent PG material.
Sarita Aryal et al.
Biomolecules, 10(9) (2020-08-30)
In Trichomonas vaginalis (T. vaginalis), cyclophilins play a vital role in dislodging Myb proteins from the membrane compartment and leading them to nuclear translocation. We previously reported that TvCyP1 cyclophilin from T. vaginalis forms a dimer and plays an essential
John P O'Donnell et al.
Methods in molecular biology (Clifton, N.J.), 2159, 93-113 (2020-06-13)
A common feature of dynamin-related proteins (DRPs) is their use of guanosine triphosphate (GTP) to control protein dynamics. In the case of the endoplasmic- reticulum- (ER)-resident membrane protein atlastin (ATL), GTP binding and hydrolysis result in membrane fusion of ER
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service