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About This Item
Form:
powder
Assay:
≥90% (PAGE)
Biological source:
bovine milk
Mol wt:
18,363 Da by calculation
biological source
bovine milk
Quality Level
assay
≥90% (PAGE)
form
powder
mol wt
18,363 Da by calculation
technique(s)
HPLC: suitable
UniProt accession no.
storage temp.
2-8°C
Gene Information
bovine ... LGB(280838)
General description
A member of the lipocalin family, βLg is a small protein of 162 amino acids with a molecular mass of ∼18,400 Da, featuring an eight-stranded β-barrel (strands A-H) succeeded by a three-turn a-helix and a final β-strand (strand I) that forms part of the dimerization interface.
Milk from dairy cows contains the protein β-lactoglobulin (BLG). It naturally occurs in a number of genetic variants, and the most prevalent bovine variants are known as BLG A and BLG B.
Application
β-Lactoglobulin A from bovine milk has been used:
- as a calibrant for the calibration of the TriWave device
- as a standard in the detection and quantification of β-lactoglobulin in bovine milk by reverse-phase high performance liquid chromatography (HPLC)
- in the purification and molecular weight measurement of protease samples
β-Lactoglobulin was used in the identification of the genetic variants of κ-casein in milk by isoelectric focusing electrophoresis.
Biochem/physiol Actions
β-Lactoglobulin (β-lg) possesses heat-set gelation properties. It also exhibits antiviral, anticarcinogenic and hypocholesterolemic effects. β-lg can bind to retinol and long-chain fatty acids. It may participate in the absorption and metabolism of fatty acids.
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Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
低风险生物材料
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Bioactive milk proteins, peptides and lipids and other functional components derived from milk and bovine colostrum
Functional Foods, 471-511 (2011)
K M Oliveira et al.
European journal of biochemistry, 268(2), 477-483 (2001-02-13)
The crystal structures of beta-lactoglobulin genetic variants A and B have been determined in the orthorhombic space group C222(1) (lattice Y) by X-ray diffraction at 2.0 A and 1.95 A resolution, respectively. The structural comparison shows that both variants exhibit
An Acid Protease Produced by Monilinia fructigena in vitro and in Infected Apple Fruits, and its Possible Role in Pathogenesis
Hislop EC, et al.
Microbiology, 128(4), 799-807 (1982)
Global Trade Item Number
| SKU | GTIN |
|---|---|
| L7880-100MG | 04061833263570 |
| L7880-10MG | 04061833965740 |
| L7880-250MG | 04061833965757 |
| L7880-25MG | 04061833965764 |