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Merck

A2810

Sigma-Aldrich

Adenosine 5′-diphosphate–Agarose

lyophilized powder

别名:

5′-ADP agarose

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About This Item

MDL號碼:
分類程式碼代碼:
23151817
NACRES:
NA.56

形狀

lyophilized powder

標籤範圍

1-5 μmol per mL

基質

cross-linked 4% beaded agarose

基質活化

cyanogen bromide

基質結合

C-8

基質墊片

9 atoms

儲存溫度

−20°C

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相关类别

應用

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.

數量

Swelling factor = 1 gram yields 8-16 mL packed gel

外觀

用乳糖稳定化的冻干粉

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


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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
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
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
Purification and characterization of acetate kinase from <I>Clostridium thermocellum</I>.
Lin, W.R., et al.
Tetrahedron, 54(52), 15915-15925 (1998)
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

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