L6010

Sigma-Aldrich

α-Lactalbumin from bovine milk

Type III, calcium depleted, ≥85% (PAGE), lyophilized powder

CAS Number:
MDL number:
NACRES:
NA.61

Quality Level

biological source

bovine milk

type

Type III

assay

≥85% (PAGE)

form

lyophilized powder

quality

calcium depleted

mol wt

14,178 Da by calculation

application(s)

indirect ELISA: suitable

solubility

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

cation traces

Ca: ≤0.3 mol/mol (may contain traces of (NH4)2SO4 and sodium phosphateL6010)

UniProt accession no.

storage temp.

−20°C

Gene Information

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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:
  • in indirect enzyme-linked immunosorbent assay (ELISA) and competitive ELISA methods
  • in binding of Hsp90 and HSJ1b analysis
  • to inhibit the lysozyme CAP-RAST assay

Packaging

100, 500 mg in poly bottle
1 g in poly bottle

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 Angstrom 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

May contain traces of (NH4)2SO4 and sodium phosphate.

storage_class_code

11 - Combustible Solids

WGK Germany

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

Certificate of Origin

B M Fu et al.
The American journal of physiology, 274(6 Pt 2), H2062-H2073 (1998-06-25)
We previously proposed a two-pathway model for solute and water transport across vascular endothelium (Fu, B. M., R. Tsay, F. E. Curry, and S. Weinbaum. J. Biomech. Eng. 116: 502-513, 1994) that hypothesized the existence of a continuous slit 2...
Shang Shen et al.
Experimental physiology, 95(2), 369-379 (2009-11-03)
To investigate whether vascular endothelial growth factor (VEGF) enhances cancer cell adhesion to normal microvessels, we used in vivo video microscopy to measure adhesion rates of MDA-MB-435s human breast cancer cells and ErbB2-transformed mouse mammary carcinomas in the postcapillary venules...
Bingmei M Fu et al.
American journal of physiology. Heart and circulatory physiology, 284(6), H2124-H2135 (2003-02-01)
To investigate the ultrastructural mechanisms of acute microvessel hyperpermeability by vascular endothelial growth factor (VEGF), we combined a mathematical model (J Biomech Eng 116: 502-513, 1994) with experimental data of the effect of VEGF on microvessel hydraulic conductivity (L(p)) and...
Renata Muca et al.
Journal of chromatography. A, 1492, 79-88 (2017-03-13)
Adsorption behavior of unstable proteins, i.e., bovine serum albumin and α-lactalbumin, has been studied on a hydrophobic interaction chromatography medium under mass overloading conditions at different kosmotropic salt concentrations in the mobile phase. A mechanistic model has been formulated and...
Jannik Nedergaard Pedersen et al.
Protein science : a publication of the Protein Society, 27(2), 451-462 (2017-11-03)
Proteins and lipids can form complexes called liprotides, in which the partially denatured protein forms a shell encasing a lipid core. This effectively stabilizes a lipid micelle in an aqueous solvent and suggests that liprotides may provide a suitable vessel...

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