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L6010

Sigma-Aldrich

α-Lactalbumin from bovine milk

Type III, calcium depleted, ≥85% (PAGE), lyophilized powder

Synonyme(s) :

Bos d 4, Lactose synthase B protein, alpha-lactalbumin

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About This Item

Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.61

Source biologique

bovine milk

Type

Type III

Pureté

≥85% (PAGE)

Forme

lyophilized powder

Qualité

calcium depleted

Poids mol.

14,178 Da by calculation

Technique(s)

indirect ELISA: suitable

Solubilité

H2O: soluble 10 mg/mL, clear to slightly hazy, colorless to faintly yellow

Traces de cations

Ca: ≤0.3 mol/mol

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

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Description générale

may contain traces of (NH4)2SO4 and sodium phosphateL6010

Application

α-Lactalbumin from bovine milk has been used:
  • in indirect enzyme-linked immunosorbent assay (ELISA) and competitive ELISA methods
  • in binding of Hsp90 and HSJ1b analysis
  • to inhibit the lysozyme CAP-RAST assay

Actions biochimiques/physiologiques

α-Lactalbumin is the cheif protein in human milk. It consists of a single polypeptide chain with 8 cysteines which form disulfide bridges. α-Lactalbumin binds several metal ions, including calcium, which is thought to play a role in the regeneration of native α-lactalbumin from the reduced, denatured form. α-Lactalbumin also has a distinct zinc binding site that is thought to play a role in the binding of the lactose synthase complex.The mature protein consists of 123 amino acid residues (14 kD), and it has a three-dimensional structure with 1.7 Angstrom resolution, demonstrating four α-helices and a triple stranded antiparallel β-sheet.
Alters the substrate specificity of galactosyltransferase to increase the rate of lactose formation; the complex of galactosyltransferase and α-lactalbumin is called lactose synthase. Site-directed mutagenesis of Asp87 or Asp88 to Ala completely abolishes the strong calcium binding affinity and reduces the stimulation of lactose synthase to <3.5% of the maximal rate.

Qualité

May contain traces of (NH4)2SO4 and sodium phosphate.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

B Fang et al.
Journal of dairy science, 99(8), 5991-6004 (2016-05-30)
An α-lactalbumin-oleic acid (α-LA-OA) complex has exhibited selective antitumor activity in animal models and clinical trials. Although apoptosis and autophagy are activated and the functions of several organelles are disrupted in response to α-LA-OA, the detailed antitumor mechanism remains unclear.
B M Fu et al.
The American journal of physiology, 274(6 Pt 2), H2062-H2073 (1998-06-25)
We previously proposed a two-pathway model for solute and water transport across vascular endothelium (Fu, B. M., R. Tsay, F. E. Curry, and S. Weinbaum. J. Biomech. Eng. 116: 502-513, 1994) that hypothesized the existence of a continuous slit 2
Melanie Jannaway et al.
Frontiers in physiology, 12, 687563-687563 (2021-10-09)
Lymphatic vascular permeability prevents lymph leakage that is associated with lymphedema, lymphatic malformations, obesity, and inflammation. However, the molecular control of lymphatic permeability remains poorly understood. Recent studies have suggested that adherens junctions and vesicle transport may be involved in
T Schnaider et al.
Life sciences, 67(12), 1455-1465 (2000-09-13)
The 90 kDa heat shock protein (Hsp90) is a major cytoplasmic molecular chaperone associating with numerous other proteins. Both genetic and in vitro refolding experiments using reticulocyte lysate have suggested a functional interaction of Hsp90 with yeast human homologues of
Effect of conjugation of cow milk whey protein with polyethylene glycol on changes in their immunoreactive and allergic properties
Wroblewska B and Jedrychowski L
Food and agricultural immunology, 14(2), 155-162 (2002)

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