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L5385

Sigma-Aldrich

α-Lactalbumin from bovine milk

Type I, ≥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 I

Assay

≥85% (PAGE)

form

lyophilized powder

technique(s)

cell culture | mammalian: suitable
electrophoresis: suitable

solubility

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

UniProt accession no.

storage temp.

−20°C

Gene Information

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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.

Application

α-Lactalbumin from bovine milk has been used as a supplement of basal medium for various cell cultures. It has also been used as a marker for sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).

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 Α° 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

Calcium saturated. May have traces of ammonium sulfate 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)

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Identification of Mannose-Binding Protein from Milkfish (Chanos chanos F.) Serum
Argayosa AM, et al.
Journal of Mathematics, 6(3) (2019)
Yuekun Wu et al.
Food science & nutrition, 9(4), 2299-2307 (2021-04-13)
α-Dicarbonyl compounds (α-DCs) are a class of compounds generated during the thermal processing of food. Due to the high reactivity, α-DCs were endowed with the ability to react with food components thus lowering nutrition value and even leading to a
Effect of different exogenous fatty acids on the cytosolic triacylglycerol content in bovine mammary cells
Vargas-Bello-Perez E, et al.
Animal Nutrition, 5(2), 202-208 (2019)
M J Kronman et al.
The Journal of biological chemistry, 256(16), 8582-8587 (1981-08-25)
Removal of the tightly bound Ca2+ ion from bovine alpha-lactalbumin (Hiraoka et al. (1980) Biochem. Biophys. Res. Commun. 95, 1098-1104) produces a pronounced conformational change, as indicated by fluorescence and absorbance changes. These changes closely resemble the changes that occur
XiaoLu Geng et al.
Soft matter, 15(24), 4787-4796 (2019-05-08)
Formation of nanotubes from partially hydrolysed α-lactalbumin (α-La) was investigated at five pH values, two concentrations of α-La and two calcium levels. Nanotubes were formed under almost all combinations of the investigated factors, and for the first time the formation

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