Passa al contenuto
Merck
Tutte le immagini(3)

Key Documents

Altri documenti

L6010

Sigma-Aldrich

α-Lactalbumin from bovine milk

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

Sinonimo/i:

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

Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali
Tutte le immagini(3)

About This Item

Numero CAS:
9051-29-0
Numero MDL:
MFCD00162025
Codice UNSPSC:
12352202
NACRES:
NA.61

Origine biologica

bovine milk

Tipo

Type III

Saggio

≥85% (PAGE)

Forma fisica

lyophilized powder

Qualità

calcium depleted

PM

14,178 Da by calculation

tecniche

indirect ELISA: suitable

Solubilità

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

Cationi in tracce

Ca: ≤0.3 mol/mol

N° accesso UniProt

P00711

Temperatura di conservazione

−20°C

Informazioni sul gene

cow ... LALBA(281894)

Cerchi prodotti simili? Visita Guida al confronto tra prodotti

Descrizione generale

may contain traces of (NH4)2SO4 and sodium phosphateL6010

Applicazioni

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

Azioni biochim/fisiol

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.

Qualità

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

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

Certificati d'analisi (COA)

Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.

Possiedi già questo prodotto?

I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.

Visita l’Archivio dei documenti

B Fang et al.
Journal of dairy science, 99(8), 5991-6004 (2016-05-30)
An α-lactalbumin-oleic acid (α-LA-OA) complex has exhibited selective antitumor activity in animal models and clinical trials. Although apoptosis and autophagy are activated and the functions of several organelles are disrupted in response to α-LA-OA, the detailed antitumor mechanism remains unclear.
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
Melanie Jannaway et al.
Frontiers in physiology, 12, 687563-687563 (2021-10-09)
Lymphatic vascular permeability prevents lymph leakage that is associated with lymphedema, lymphatic malformations, obesity, and inflammation. However, the molecular control of lymphatic permeability remains poorly understood. Recent studies have suggested that adherens junctions and vesicle transport may be involved in
T Schnaider et al.
Life sciences, 67(12), 1455-1465 (2000-09-13)
The 90 kDa heat shock protein (Hsp90) is a major cytoplasmic molecular chaperone associating with numerous other proteins. Both genetic and in vitro refolding experiments using reticulocyte lysate have suggested a functional interaction of Hsp90 with yeast human homologues of
Effect of conjugation of cow milk whey protein with polyethylene glycol on changes in their immunoreactive and allergic properties
Wroblewska B and Jedrychowski L
Food and agricultural immunology, 14(2), 155-162 (2002)
Visualizza tutti i documenti correlati

Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..

Contatta l'Assistenza Tecnica.