A2810
Adenosine 5′-diphosphate–Agarose
lyophilized powder
Sinônimo(s):
5′-ADP agarose
Faça loginpara ver os preços organizacionais e de contrato
Selecione um tamanho
5 ML
R$ 2.411,00
R$ 2.411,00
Previsão de entrega em28 de maio de 2025
Selecione um tamanho
Alterar visualização
5 ML
R$ 2.411,00
About This Item
R$ 2.411,00
Previsão de entrega em28 de maio de 2025
Produtos recomendados
Formulário
lyophilized powder
Extensão da rotulagem
1-5 μmol per mL
Matriz
cross-linked 4% beaded agarose
ativação da matriz
cyanogen bromide
ligação da matriz
C-8
espaçador de matriz
9 atoms
temperatura de armazenamento
−20°C
Procurando produtos similares? Visita Guia de comparação de produtos
Aplicação
Adenosine 5′-diphosphate has been used in the research of platelet integrin α(IIb)β3, which is crucial for platelet aggregation. It has been determined that the interaction between Adenosine 5′-diphosphate and the receptor P2Y12 is needed for the maintenance of integrin α(IIb)β3 activation. Adenosine 5′-diphosphate agarose (5′-ADP agarose) has been used in purification of heat schock proteins.
Quantidade
Swelling factor = 1 gram yields 8-16 mL packed gel
forma física
Lyophilized powder stabilized with lactose
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
Escolha uma das versões mais recentes:
Já possui este produto?
Encontre a documentação dos produtos que você adquiriu recentemente na biblioteca de documentos.
Os clientes também visualizaram
Xueji Wu et al.
The Biochemical journal, 378(Pt 3), 793-799 (2003-12-11)
The chaperone activity of Hsp70 (70 kDa heat-shock protein) in protein folding and its conformational switch, including oligomeric and monomeric interconversion, are regulated by the hydrolysis of ATP and the ATP-ADP exchange cycle. The crystal structure of human ATPase domain
Zihai Li
Methods (San Diego, Calif.), 32(1), 25-28 (2003-11-20)
Known commonly as molecular chaperones for proteins, heat shock proteins (HSPs) have also been found to chaperone small molecular weight cellular peptides. HSP-peptide complexes can prime T cell immunity specific against the peptides bound to HSPs, but not against HSPs
Knut Fälker et al.
Thrombosis and haemostasis, 92(1), 114-123 (2004-06-24)
Stimulating human platelets with thrombin induces the activation of the extracellular signal-regulated kinase 2 (ERK2). We demonstrate that this effect is highly dependent on ADP secretion and P2Y12 receptor signalling. AR-C69931MX (10 microM), a specific antagonist of the Gi-coupled P2Y12
Antoine Ménoret
Methods (San Diego, Calif.), 32(1), 7-12 (2003-11-20)
Heat shock proteins (HSPs) are powerful immunogens against the antigenic peptides they chaperone. The antigenic peptides are MHC I-binding peptides and their elongated precursors derived from tumor antigens, viral antigens, minor histocompatibility antigens, or model antigens. HSP-peptide complexes can immunize
T Kamae et al.
Journal of thrombosis and haemostasis : JTH, 4(6), 1379-1387 (2006-05-19)
Platelet integrin alpha(IIb)beta3 plays a crucial role in platelet aggregation, and the affinity of alpha(IIb)beta3 for fibrinogen is dynamically regulated. Employing modified ligand-binding assays, we analyzed the mechanism by which alpha(IIb)beta3 maintains its high-affinity state. Washed platelets adjusted to 50
Active Filters
Nossa equipe de cientistas tem experiência em todas as áreas de pesquisa, incluindo Life Sciences, ciência de materiais, síntese química, cromatografia, química analítica e muitas outras.
Entre em contato com a assistência técnica
