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L6010

Sigma-Aldrich

α-Lactalbumin from bovine milk

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

Synonym(s):

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

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine milk

type

Type III

Assay

≥85% (PAGE)

form

lyophilized powder

quality

calcium depleted

mol wt

14,178 Da by calculation

technique(s)

indirect ELISA: suitable

solubility

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

cation traces

Ca: ≤0.3 mol/mol

UniProt accession no.

storage temp.

−20°C

Gene Information

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General description

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

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. 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.

Quality

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Ozgür Tarhan et al.
The Journal of dairy research, 81(1), 98-106 (2013-12-20)
Alpha-lactalbumin (α-la) is one of the major proteins in whey. When partially hydrolysed with Bacillus licheniformis protease, it produces nanotubular structures in the presence of calcium ions by a self-assembly process. This study presents investigation of α-la protein structure during
Prevalence of lysozyme sensitization in an egg-allergic population
Fremont S, et al.
Allergy, 52(2), 224-228 (1997)
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
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.

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