L6385
α-Lactalbumin from bovine milk
For use as a marker in SDS-PAGE
Synonym(s):
alpha-lactalbumin
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biological source
bovine milk
Quality Level
form
powder
mol wt
~14.2 kDa
packaging
vial of 5 mg
concentration
>5 mg per vial protein (biuret)
technique(s)
electrophoresis: suitable
solubility
H2O: soluble 10 mg/mL
UniProt accession no.
storage temp.
2-8°C
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1 of 4
This Item | L4385 | L5385 | L6010 |
|---|---|---|---|
| biological source bovine milk | biological source bovine milk | biological source bovine milk | biological source bovine milk |
| technique(s) electrophoresis: suitable | technique(s) microbiological culture: suitable | technique(s) cell culture | mammalian: suitable, electrophoresis: suitable | technique(s) indirect ELISA: suitable |
| Quality Level 200 | Quality Level 200 | Quality Level 300 | Quality Level 300 |
| form powder | form lyophilized powder | form lyophilized powder | form lyophilized powder |
| Gene Information cow ... LALBA(281894) | Gene Information cow ... LALBA(281894) | Gene Information cow ... LALBA(281894) | Gene Information cow ... LALBA(281894) |
| storage temp. 2-8°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
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.[1]
Application
α-Lactalbumin from bovine milk is suitable for use:
- as an electrophoresis marker, with a molar mass of approximately 14,200Da[2][3][4]
- in a study to investigate selective binding of proteins on charged surface iron oxide nanoparticles via reverse charge parity model[5]
Biochem/physiol Actions
α-Lactalbumin 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.[7] α-Lactalbumin also has a distinct zinc binding site that is thought to play a role in the binding of the lactose synthase complex. [8][9] 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 a-helices and a triple stranded antiparallel β-sheet.[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. 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.
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