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Merck

L6010

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:
9051-29-0
UNSPSC Code:
12352202
NACRES:
NA.61
MDL number:
MFCD00162025

Nom du produit

α-Lactalbumin from bovine milk, Type III, calcium depleted, ≥85% (PAGE), lyophilized powder

biological source

bovine milk

type

Type III

assay

≥85% (PAGE)

form

lyophilized powder

quality

calcium depleted

mol wt

14,178 Da by calculation

concentration

≥85 % protein

technique(s)

indirect ELISA: suitable

impurities

cation traces, tested

solubility

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

cation traces

Ca: ≤0.3 mol/mol

UniProt accession no.

P00711

storage temp.

−20°C

Quality Level

300

Gene Information

cow ... LALBA(281894)

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Catégories apparentées

Analysis Note

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

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

Biochem/physiol Actions

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.

General description

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

Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificats d'analyse (COA)

Lot/Batch Number
0000382362
0000352692
0000352687
0000352688
0000350737

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Consulter la Bibliothèque de documents

Prevalence of lysozyme sensitization in an egg-allergic population
Fremont S, et al.
Allergy, 52(2), 224-228 (1997)
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
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.
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)
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
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Product Information Sheet - L6010

Product Information Sheet

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