Merck
  • L5385
All Photos(4)

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
CAS Number:
MDL number:
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

Compare Similar Items

View Full Comparison

1 of 4

This Item
L4385L6385L6010
biological source

bovine milk

biological source

bovine milk

biological source

bovine milk

biological source

bovine milk

assay

≥85% (PAGE)

assay

-

assay

-

assay

≥85% (PAGE)

form

lyophilized powder

form

lyophilized powder

form

powder

form

lyophilized powder

technique(s)

cell culture | mammalian: suitable, electrophoresis: suitable

technique(s)

microbiological culture: suitable

technique(s)

electrophoresis: suitable

technique(s)

indirect ELISA: suitable

solubility

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

solubility

-

solubility

H2O: soluble 10 mg/mL

solubility

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

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

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

13 - Non 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

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

Enter Lot Number to search for Certificate of Origin (COO).

Product Information Sheet

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