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A2810

Sigma-Aldrich

Adenosine 5′-diphosphate–Agarose

lyophilized powder

Synonym(s):

5′-ADP agarose

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About This Item

MDL number:
UNSPSC Code:
23151817
NACRES:
NA.56

form

lyophilized powder

extent of labeling

1-5 μmol per mL

matrix

cross-linked 4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

C-8

matrix spacer

9 atoms

storage temp.

−20°C

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Application

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.

Quantity

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

Physical form

Lyophilized powder stabilized with lactose

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Pawel Stocki et al.
The Journal of biological chemistry, 286(14), 12803-12811 (2011-01-11)
Tumor cells very often have elevated expression of HSP70, the anti-apoptotic properties of which contribute to overall tumor survival. Independent of its anti-apoptotic properties, HSP70 was also suggested to be involved in the antigen presentation process by chaperoning cytosolic peptides

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