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Documentos Principais

L6010

Sigma-Aldrich

α-Lactalbumin from bovine milk

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

Sinônimo(s):

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

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About This Item

Número CAS:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.61

fonte biológica

bovine milk

Nível de qualidade

tipo

Type III

Ensaio

≥85% (PAGE)

Formulário

lyophilized powder

qualidade

calcium depleted

peso molecular

14,178 Da by calculation

concentração

≥85 % protein

técnica(s)

indirect ELISA: suitable

Impurezas

cation traces, tested

solubilidade

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

traços de cátion

Ca: ≤0.3 mol/mol

nº de adesão UniProt

temperatura de armazenamento

−20°C

Informações sobre genes

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Descrição geral

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

Aplicação

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

Ações bioquímicas/fisiológicas

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.
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.

Qualidade

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

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


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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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