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Merck

L5385

Sigma-Aldrich

α-Lactalbumin from bovine milk

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

Sinónimos:

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

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About This Item

Número de CAS:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.61
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origen biológico

bovine milk

Nivel de calidad

tpo

Type I

Ensayo

≥85% (PAGE)

Formulario

lyophilized powder

concentración

≥85 % protein

técnicas

cell culture | mammalian: suitable
electrophoresis: suitable

impurezas

calcium, tested

solubilidad

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

Nº de acceso UniProt

temp. de almacenamiento

−20°C

Información sobre el gen

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Descripción general

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]

Aplicación

α-Lactalbumin from bovine milk has been used as a supplement of basal medium for various cell cultures.[2][3] It has also been used as a marker for sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).[4]

Acciones bioquímicas o fisiológicas

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.[5] α-Lactalbumin also has a distinct zinc binding site that is thought to play a role in the binding of the lactose synthase complex. [6][7] 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.[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.

Calidad

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

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


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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.
Daniel Rusu et al.
The Journal of nutrition, 140(2), 382-391 (2009-12-25)
Innate immunity depends on the efficiency of neutrophils to be activated rapidly to restore homeostasis. It can benefit from priming agents that enhance neutrophil capacity to respond more efficiently to a subsequent stimulation. Among natural products, a bovine whey protein
XiaoLu Geng et al.
Soft matter, 15(24), 4787-4796 (2019-05-08)
Formation of nanotubes from partially hydrolysed α-lactalbumin (α-La) was investigated at five pH values, two concentrations of α-La and two calcium levels. Nanotubes were formed under almost all combinations of the investigated factors, and for the first time the formation
Dmitri Nikitin et al.
Computational and structural biotechnology journal, 20, 1366-1377 (2022-04-08)
Cardio- and cerebrovascular diseases are leading causes of death and disability, resulting in one of the highest socio-economic burdens of any disease type. The discovery of bacterial and human plasminogen activators and their use as thrombolytic drugs have revolutionized treatment
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

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