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L5385 Sigma

α-Lactalbumin from bovine milk

Type I, ≥85% (PAGE), lyophilized powder



Related Categories Molecular Biology, Protein Sequencing, Protein Structural Analysis, Proteomics, Standards for Protein Sequencing More...
type   Type I
assay   ≥85% (PAGE)
form   lyophilized powder
solubility   H2O: soluble10 mg/mL, clear, colorless to faintly yellow
storage temp.   −20°C
Gene Information   cow ... LALBA(281894)



1 g in poly bottle

25, 100, 500 mg in poly bottle


Calcium saturated. May have traces of ammonium sulfate and sodium phosphate

Biochem/physiol Actions

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.

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 Α° resolution, demonstrating four α-helices and a triple stranded antiparallel β-sheet.

General description

α-Lactalbumin is a small, globular, whey protein that has been found in all milk studied to date. It is a metalloprotein of approximately 14 kDa produced in the mammary glands.

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Safety Information

NONH for all modes of transport
WGK Germany 


Certificate of Analysis

Certificate of Origin

Protocols & Articles
Peer-Reviewed Papers


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