A2810

Adenosin-5′-Diphosphat-Agarose

Name: Adenosin-5′-Diphosphat-Agarose
Brand: SIGMA
Price: 369 EUR

lyophilized powder

Synonym(e):

5′-ADP agarose

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5 ML

€ 369,00

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Über diesen Artikel

UNSPSC Code:

23151817

NACRES:

NA.56

MDL number:

MFCD00161947

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Unterstützung erhalten

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

Quality Level

200

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Dieser Artikel	A0144	G9768	01905
Sigma-Aldrich A2810 Adenosine 5′-diphosphate–Agarose	Sigma-Aldrich A0144 Adenosine 3′,5′-cyclic monophosphate–Agarose	Sigma-Aldrich G9768 Guanosine 5′-triphosphate–Agarose	Sigma-Aldrich 01905 Adenosine 5′-diphosphate
form lyophilized powder	form lyophilized powder	form aqueous glycerol suspension	form powder
Quality Level 200	Quality Level 200	Quality Level 200	Quality Level 200
extent of labeling 1-5 μmol per mL	extent of labeling ≥2 μmol per mL	extent of labeling 1-5 μmol per mL	extent of labeling -
matrix cross-linked 4% beaded agarose	matrix 4% beaded agarose	matrix cross-linked 4% beaded agarose	matrix -
matrix activation cyanogen bromide	matrix activation cyanogen bromide	matrix activation cyanogen bromide	matrix activation -
matrix attachment C-8	matrix attachment C-8	matrix attachment ribose hydroxyls	matrix attachment -

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.

Physical form

Lyophilisiertes Pulver stabilisiert mit Lactose

Preparation Note

Quellfaktor = 1 g ergibt 8-16 mL gepacktes Gel

Lagerklasse

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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In vitro reconstitution of heat shock protein-peptide complexes for generating peptide-specific vaccines against cancers and infectious diseases.

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

The second metal-binding site of 70 kDa heat-shock protein is essential for ADP binding, ATP hydrolysis and ATP synthesis.

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

Critical role of ADP interaction with P2Y12 receptor in the maintenance of alpha(IIb)beta3 activation: association with Rap1B activation.

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

ADP secretion and subsequent P2Y12 receptor signalling play a crucial role in thrombin-induced ERK2 activation in human platelets.

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

Purification of recombinant and endogenous HSP70s.

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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Adenosin-5′-Diphosphat-Agarose