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Key Documents

A2810

Sigma-Aldrich

Adenosin-5′-Diphosphat-Agarose

lyophilized powder

Synonym(e):

5′-ADP agarose

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About This Item

MDL-Nummer:
MFCD00161947
UNSPSC-Code:
23151817
NACRES:
NA.56

Form

lyophilized powder

Qualitätsniveau

200

Kennzeichnungsgrad

1-5 μmol per mL

Matrix

cross-linked 4% beaded agarose

Matrixaktivierung

cyanogen bromide

Matrixanbindung

C-8

Matrix-Spacer

9 atoms

Lagertemp.

−20°C

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Anwendung

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.

Menge

Quellfaktor = 1 g ergibt 8-16 mL gepacktes Gel

Physikalische Form

Lyophilisiertes Pulver stabilisiert mit Lactose

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

Analysenzertifikate (COA)

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Adenosin-5′-diphosphat Dinatriumsalz ≥90%

Sigma-Aldrich

01897

Adenosin-5′-diphosphat Dinatriumsalz

Sigma-Aldrich

Sigma-Aldrich

P4832

Poly-L-Lysin -Lösung

Mangan(II)-chlorid Tetrahydrat ReagentPlus®, ≥99%

Sigma-Aldrich

M3634

Mangan(II)-chlorid Tetrahydrat

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
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
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
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
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