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Merck

L7269

α-Lactalbumin from human milk

≥95% (SDS-PAGE), lyophilized powder

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Número CAS:
UNSPSC Code:
12352202
NACRES:
NA.61
MDL number:
Biological source:
human milk
Assay:
≥95% (SDS-PAGE)
Form:
lyophilized powder
Technique(s):
cell migration: suitable
Concentration:
>75 % protein (UV)
Servicio técnico
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biological source

human milk

Quality Segment

assay

≥95% (SDS-PAGE)

form

lyophilized powder

mol wt

14,070 Da by calculation

concentration

>75 % protein (UV)

technique(s)

cell migration: suitable

solubility

H2O: soluble 10 mg/mL(lit.)

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... LALBA(3906)

General description

α-Lactalbumin (α-LA) is a small, acidic, whey protein that constitutes about 22% of the total proteins in human milk. It is produced by the epithelial cells of the mammary gland. α-LA is made up of two domains, a large α-helical domain, and a small β-sheet domain.

Application

α-Lactalbumin (α-LA) has been used as a standard

  • to study the partitioning behavior of different monomeric proteins with exposure to amino acids on the protein surface
  • to study the interaction between α-LA and cathepsin D
  • to study the ability of breast milk fractions to enhance the transepithelial flux of extrinsic iron in colon carcinoma cell line

Biochem/physiol Actions

α-Lactalbumin (α-LA) forms a complex with lactose synthase within the mammary gland and plays a role in milk production and regulates milk volume. It acts as an essential source for bioactive peptides and essential amino acids such as lysine, tryptophan, branched-chain amino acids, and sulfur-containing amino acids that play a role in an infant′s nutrition. In addition, α-LA has a wide range of applications including a supplement to foster gastrointestinal health and modulate sleep and depression. α-LA also shows therapeutic effects against sarcopenia, seizures, mood disorders, and cancer. It has a Ca2+ binding site that binds with Na+, K+, Mg2+, and Mn2+ and many Zn2+ binding sites.
Alters the substrate specificity of galactosyltransferase to increase the rate of lactose formation; the complex of galactosyltransferase and α-lactalbumin is called lactose synthase.
Alters the substrate specificity of galactosyltransferase to increase the rate of lactose formation; the complex of galactosyltransferase and α-lactalbumin is called lactose synthase. Complexes of α-lactalbumin with oleic acid show drastically different activities than α-lactalbumin alone, being strongly cytotoxic to tumor cells. The complex is referred to as HAMLET (human alpha-lactalbumin made lethal to tumor cells).


Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable



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