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L4385

Sigma-Aldrich

α-Lactalbumin from bovine milk

Marker for non-denaturing PAGE

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About This Item

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

Source biologique

bovine milk

Niveau de qualité

Forme

lyophilized powder

Poids mol.

~14.2 kDa

Technique(s)

microbiological culture: suitable

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

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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 was used in the isolation and analysis of restriction endonuclease digestive patterns of chromosomal DNA from Mycobacterium paratuberculosis and other Mycobacterium species. It was also used in a study to test if the neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins.

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.

Reconstitution

0.9-1.4 mg/mL after reconstitution with 1 mL of water

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


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Consulter la Bibliothèque de documents

Michael Helwig et al.
The Journal of biological chemistry, 288(2), 1114-1124 (2012-11-23)
Neurodegenerative diseases such as Alzheimer (AD) and Parkinson (PD) are characterized by abnormal aggregation of misfolded β-sheet-rich proteins, including amyloid-β (Aβ)-derived peptides and tau in AD and α-synuclein in PD. Correct folding and assembly of these proteins are controlled by
Comparison of the amino acid sequence of bovine alpha-lactalbumin and hens egg white lysozyme.
K Brew et al.
The Journal of biological chemistry, 242(16), 3747-3749 (1967-08-25)
Gladys Bichang'a et al.
Journal of chemical ecology, 44(11), 1030-1039 (2018-08-08)
Foraging parasitoids use chemical signals in host recognition and selection processes. Although, the volatiles play a relevant role in the localization by parasitoids of their hosts feeding on plants, the host identification process for acceptance occurs mainly during contact between
Why people become psychiatric nurses.
P Jackson
Nursing, 4(10), 32-34 (1990-05-10)
D B Veprintsev et al.
FEBS letters, 412(3), 625-628 (1997-08-04)
The thermal denaturation of bovine and human apo-alpha-lactalbumins at neutral pH has been studied by intrinsic protein fluorescence, circular dichroism (CD), and differential scanning microcalorimetry (DSC) methods. Apo-alpha-lactalbumin possesses a thermal transition with a midpoint about 25-30 degrees C under

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