β-Lactoglobulin 

β-Lactoglobulin, a major whey protein, is a small globular protein from the lipocalin family. β-Lactoglobulin is an important source of the essential and branched-chain amino acids (leucine, isoleucine, and valine). β-Lactoglobulin shows antioxidant properties, because it contains two disulfide bonds and one free thiol group. β-Lactoglobulin is a ligand transport agent. β-Lactoglobulin is one of the major allergens in milk and can be utilized in the research for developing safe hypoallergenic dairy products^[1][2][3][4].

Heat treatment of bovine milk antigen bovine β-Lactoglobulin generates ligands for RAGE, Gal-3, CD-36 and SR-AI as a result of structural changes and glycation. Glycated BLG is less sensitive to digestion and maintains its binding to RAGE and Gal-3. Post-digestion retained immunogenicity of glycated BLG may be mediated via RAGE as a signaling pathway, and via Gal-3 facilitating internalization^[1].
β-Lactoglobulin possesses antioxidant properties, because it contains two disulfide bonds (Cys-66 to Cys-160, Cys-106 to Cys-119) and one free thiol group (Cys-121)^[2].
Structurally, β-Lactoglobulin has unique features, i.e. a rigid β-barrel core surrounded by one long and several short α-helices with two disulfide (SS) bonds and one free cysteinyl thiol (SH) buried in the core. There are two variants of β-Lactoglobulin (BLG). Variant A (BLGA) has Asp64 and Val118 in place of Gly64 and Ala118 of another variant, B (BLGB). These variants are in equilibrium with a hetero- or homo-dimer under physiological conditions^[3].
β-Lactoglobulin is the building block of amyloid fibrils and has a variety of applications, including stabilizing gels or emulsions^[4].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

9045-23-2

Solid

White to off-white

[b-Lactoglobulin]

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Teodorowicz M, et al. Enhanced Uptake of Processed Bovine β-Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity. Mol Nutr Food Res. 2021;65(8):e2000834.  [Content Brief]

  [2]. Gołębiowski A, et al. Isolation and Self-Association Studies of Beta-Lactoglobulin. Int J Mol Sci. 2020;21(24):9711. Published 2020 Dec 19.  [Content Brief]

  [3]. Iwaoka M, et al. Oxidative folding pathways of bovine milk β-lactoglobulin with odd cysteine residues. FEBS Open Bio. 2019;9(8):1379-1391.  [Content Brief]

  [4]. Uttinger MJ, et al. Measurement of length distribution of beta-lactoglobulin fibrils by multiwavelength analytical ultracentrifugation. Eur Biophys J. 2020;49(8):745-760.  [Content Brief]