L2506
β-Lactoglobulin from bovine milk
≥85% (PAGE), lyophilized powder
Sinonimo/i:
β-LG, Bos d 5, beta-LG
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1 G
CHF 184.00
5 G
CHF 807.00
CHF 184.00
Spedizione prevista il14 aprile 2025
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Cambia visualizzazione
1 G
CHF 184.00
5 G
CHF 807.00
About This Item
CHF 184.00
Spedizione prevista il14 aprile 2025
Prodotti consigliati
Origine biologica
bovine milk
Livello qualitativo
Saggio
≥85% (PAGE)
Stato
lyophilized powder
tecniche
titration: suitable
N° accesso UniProt
Temperatura di conservazione
2-8°C
Informazioni sul gene
bovine ... LGB(280838)
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Descrizione generale
β-Lactoglobulin plays a key role in immune response and modulates IgM levels and cell proliferation.[1] β-Lactoglobulin from bovine is a model system for protein folding studies and denaturation kinetics.[2] Polymorphisms in the β-lactoglobulin modulates bovine milk production and composition.[3]
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.[4]
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.[5]
Applicazioni
β-Lactoglobulin from bovine milk has been used:
- for the generation of calibration curve for protein solubility index[6]
- in acid-base titration[7]
- as a standard for surface hydrophobicity analysis[8]
β-Lactoglobulin was used in a cytologic assay for diagnosis of food hypersensitivity in patients with irritable bowel syndrome.[9]
Qualità
Contains β-lactoglobulins A and B which can be isolated chromatographically.
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
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I clienti hanno visto anche
Reversible unfolding of bovine beta-lactoglobulin mutants without a free thiol group
Yagi M, et al.
Test, 278(47), 47009-47015 (2003)
Effect of dynamic high pressure on whey protein aggregation: A comparison with the effect of continuous short-time thermal treatments
Gracia-Julia A, et al.
Food Hydrocolloids, 22(6), 1014-1032 (2008)
Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes
Alizadeh-Pasdar N and Li-Chan ECY
Journal of Agricultural and Food Chemistry, 48(2), 328-334 (2000)
Polymorphism of Beta-Lactoglobulin Coding and 5?-Flanking Regions and Association with Milk Production Traits
Zakizadeh S, et al.
Biotechnology, Biotechnological Equipment, 26(1), 2716-2721 (2012)
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.
Langmuir, 16(25), 9738-9743 (2000)
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