Accéder au contenu
MilliporeSigma
Toutes les photos(4)

Key Documents

L5385

Sigma-Aldrich

α-Lactalbumin from bovine milk

Type I, ≥85% (PAGE), lyophilized powder

Synonyme(s) :

Bos d 4, Lactose synthase B protein, alpha-lactalbumin

Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme


About This Item

Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.61

Source biologique

bovine milk

Type

Type I

Pureté

≥85% (PAGE)

Forme

lyophilized powder

Technique(s)

cell culture | mammalian: suitable
electrophoresis: suitable

Solubilité

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

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

Vous recherchez des produits similaires ? Visite Guide de comparaison des produits

Description générale

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).

Actions biochimiques/physiologiques

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.

Qualité

Calcium saturated. May have traces of ammonium sulfate and sodium phosphate

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

Déjà en possession de ce produit ?

Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Falk Bernsmann et al.
Journal of colloid and interface science, 344(1), 54-60 (2010-01-23)
We recently showed the possibility to build dopamine-melanin films of controlled thickness by successive immersions of a substrate in alkaline solutions of dopamine [F. Bernsmann, A. Ponche, C. Ringwald, J. Hemmerlé, J. Raya, B. Bechinger, J.-C. Voegel, P. Schaaf, V.
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)
Identification of Mannose-Binding Protein from Milkfish (Chanos chanos F.) Serum
Argayosa AM, et al.
Journal of Mathematics, 6(3) (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
Brandye M Smith et al.
Analytical chemistry, 74(14), 3386-3391 (2002-07-26)
Principal component regression (PCR) was applied to a spectral library of proteins in H2O solution acquired by single-pass attenuated total reflectance (ATR) Fourier transform infrared (FT-IR) spectroscopy. PCR was used to predict the secondary structure content, principally alpha-helical and the

Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..

Contacter notre Service technique