Skip to Content
Merck
All Photos(4)

Documents

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

Sign Into View Organizational & Contract Pricing


About This Item

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

biological source

bovine milk

Quality Level

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

Looking for similar products? Visit Product Comparison Guide

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)

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Daniel Rusu et al.
The Journal of nutrition, 140(2), 382-391 (2009-12-25)
Innate immunity depends on the efficiency of neutrophils to be activated rapidly to restore homeostasis. It can benefit from priming agents that enhance neutrophil capacity to respond more efficiently to a subsequent stimulation. Among natural products, a bovine whey protein
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
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
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service