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L7269

Sigma-Aldrich

α-Lactalbumin from human milk

≥95% (SDS-PAGE), lyophilized powder

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5 MG
CHF 394.00
25 MG
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Spedizione prevista il01 giugno 2025



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5 MG
CHF 394.00
25 MG
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About This Item

Numero CAS:
Numero MDL:
Codice UNSPSC:
12352202
NACRES:
NA.61

CHF 394.00


Spedizione prevista il01 giugno 2025


Origine biologica

human milk

Saggio

≥95% (SDS-PAGE)

Stato

lyophilized powder

PM

14,070 Da by calculation

Concentrazione

>75 % protein (UV)

tecniche

cell migration: suitable

Solubilità

H2O: soluble 10 mg/mL(lit.)

N° accesso UniProt

Temperatura di conservazione

−20°C

Informazioni sul gene

human ... LALBA(3906)

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Descrizione generale

α-Lactalbumin (α-LA) is a small, acidic,[1] whey protein that constitutes about 22% of the total proteins in human milk.[2] 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.[1]

Applicazioni

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[3]
  • to study the interaction between α-LA and cathepsin D[4]
  • to study the ability of breast milk fractions to enhance the transepithelial flux of extrinsic iron in colon carcinoma cell line

Azioni biochim/fisiol

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.[2] It has a Ca2+ binding site that binds with Na+, K+, Mg2+, and Mn2+ and many Zn2+ binding sites.[1]
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).

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Breast Milk Fractions Solubilize Fe(III) and Enhance Iron Flux across Caco-2 Cells
Robert E. S.
The Journal of Nutrition, 449?455-449?455 (2003)
HAMLET effect on cell death and mitochondrial respiration in colorectal cancer cell lines with KRAS/BRAF mutations.
??ilinskas, et al.
Journal of Cancer Research and Clinical Oncology (2023)
Applications for ?-lactalbumin in human nutrition
Donald K L, et al.
Nutrition Research Reviews, 76(6), 444?460-444?460 (2018)
The surface exposed amino acid residues of monomeric proteins determine the partitioning in aqueous two-phase systems
Kristina B, et al.
Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology, 253-268 (2002)
Junai Gan et al.
Molecular nutrition & food research, 63(18), e1900259-e1900259 (2019-07-05)
The use of human milk products is increasing for high-risk infants. Human milk contains endogenous enzymes that comprise a dynamic proteolytic system, yet biological properties of these enzymes and their activities in response to variations including pH within infants are

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