L2506
β-Lactoglobulin from bovine milk
≥85% (PAGE), lyophilized powder
Synonym(s):
β-LG, Bos d 5, beta-LG
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About This Item
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biological source
bovine milk
Quality Level
Assay
≥85% (PAGE)
form
lyophilized powder
technique(s)
titration: suitable
UniProt accession no.
storage temp.
2-8°C
Gene Information
bovine ... LGB(280838)
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General description
β-Lactoglobulin plays a key role in immune response and modulates IgM levels and cell proliferation. β-Lactoglobulin from bovine is a model system for protein folding studies and denaturation kinetics. Polymorphisms in the β-lactoglobulin modulates bovine milk production and composition.
A member of the lipocalin family, βLg is a small protein of 162 amino acids with a molecular mass of ∼18,400 Da,. It has 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 BLG A and BLG B.
Application
β-Lactoglobulin from bovine milk has been used:
- for the generation of calibration curve for protein solubility index
- in acid-base titration
- as a standard for surface hydrophobicity analysis
β-Lactoglobulin was used in a cytologic assay for diagnosis of food hypersensitivity in patients with irritable bowel syndrome.
Quality
Contains β-lactoglobulins A and B which can be isolated chromatographically.
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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Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes
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Roles of electrostatic interaction and polymer structure in the binding of beta-lactoglobulin to anionic polyelectrolytes: measurement of binding constants by frontal analysis continuous capillary electrophoresis
Hattori T, et al.
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Polymorphism of Beta-Lactoglobulin Coding and 5?-Flanking Regions and Association with Milk Production Traits
Zakizadeh S, et al.
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