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L7252

Sigma-Aldrich

Lactalbumin

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500 G
CHF 57.90
2.5 KG
CHF 167.00

CHF 57.90


Spedizione prevista il17 aprile 2025


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Cambia visualizzazione
500 G
CHF 57.90
2.5 KG
CHF 167.00

About This Item

Numero CAS:
Numero CE:
Numero MDL:
Codice UNSPSC:
12352202
NACRES:
NA.61

CHF 57.90


Spedizione prevista il17 aprile 2025


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Origine biologica

bovine

Livello qualitativo

Stato

powder

tecniche

cell culture | insect: suitable

N° accesso UniProt

Temperatura di conservazione

2-8°C

Informazioni sul gene

bovine ... LALBA(281894)

Descrizione generale

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]

Applicazioni

α-Lactalbumin was used in a cytologic assay for diagnosis of food hypersensitivity in patients with irritable bowel syndrome.[2]
Lactalbumin has also been used in rearing anopheline mosquitoes.[3]

Azioni biochim/fisiol

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.[4] α-Lactalbumin also has a distinct zinc binding site that is thought to play a role in the binding of the lactose synthase complex. [5][6] The mature protein consists of 123 amino acid residues (14 kDa), and it has a three-dimensional structure with 1.7 Angstrom resolution, demonstrating four a-helices and a triple stranded antiparallel β-sheet.[1]

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)


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Petter Storm et al.
PloS one, 8(3), e58578-e58578 (2013-03-19)
Ion channels and ion fluxes control many aspects of tissue homeostasis. During oncogenic transformation, critical ion channel functions may be perturbed but conserved tumor specific ion fluxes remain to be defined. Here we used the tumoricidal protein-lipid complex HAMLET as
Y-B Zhang et al.
Cell death & disease, 4, e550-e550 (2013-03-23)
HAMLET is a complex of oleic acids and decalcified α-lactalbumin that was discovered to selectively kill tumor cells both in vitro and in vivo. Autophagy is an important cellular process involved in drug-induced cell death of glioma cells. We treated
C S James Ho et al.
PloS one, 7(12), e53051-e53051 (2013-01-10)
HAMLET (Human Alpha-lactalbumin Made LEthal to Tumor cells) is the first member in a new family of protein-lipid complexes with broad tumoricidal activity. Elucidating the molecular structure and the domains crucial for HAMLET formation is fundamental for understanding its tumoricidal
Yoshiko Moriyama et al.
Langmuir : the ACS journal of surfaces and colloids, 28(47), 16268-16273 (2012-11-01)
The thermal stability of two homologous proteins, lysozyme and α-lactalbumin, was examined by circular dichroism. The present study clearly showed two different aspects between the homologous proteins: (1) the original helices of lysozyme and α-lactalbumin were unchanged at heat treatments
Takashi Nakamura et al.
The Journal of biological chemistry, 288(20), 14408-14416 (2013-04-13)
Although HAMLET (human α-lactalbumin made lethal to tumor cells), a complex formed by human α-lactalbumin and oleic acid, has a unique apoptotic activity for the selective killing of tumor cells, the molecular mechanisms of expression of the HAMLET activity are

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