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Documenti fondamentali

H0402

Sigma-Aldrich

Heparin−Agarose

(1:1 suspension in a 20% ethanol solution)

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About This Item

Numero MDL:
Codice UNSPSC:
23151817
NACRES:
NA.56

Origine biologica

heparin from Porcine intestinal mucosa

Livello qualitativo

Stato

(1:1 suspension in a 20% ethanol solution)

Matrice

4% beaded agarose

Attivazione matrice

epichlorohydrin

Gruppi immobilizzati alla matrice

terminal aldehyde by reductive amination to amine linker

Braccio spaziatore

7 atoms

Capacità

≥0.5 mg/mL binding capacity (thrombin)

Temperatura di conservazione

2-8°C

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Applicazioni

Heparin agarose is developed from porcine intestinal mucosa and is used in affinity chromatography. Heparin agarose has been used in studies to provide information on human monocytic ehrlichiosis, tumor necrosis and the effects of coagulation from Vipera snake venom.

Stato fisico

1:1 suspension in a 20% ethanol solution

Nota sulla preparazione

Prepared by end-point attachment for high-efficiency fractionation of antithrombin III and other specific binding proteins

Pittogrammi

Flame

Avvertenze

Warning

Indicazioni di pericolo

Classi di pericolo

Flam. Liq. 3

Codice della classe di stoccaggio

3 - Flammable liquids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

104.0 °F - closed cup

Punto d’infiammabilità (°C)

40 °C - closed cup


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Kenji Kashiwagi et al.
Biomaterials, 30(6), 1166-1175 (2008-11-22)
Efficient immobilization of biomacromolecules on material surfaces is a key to development in areas of regenerative medicine and tissue engineering. However, strong and irreversible immobilization of cytokines on surfaces often diminishes their biological functionality. A destructive hydrophobic interaction between the
W H Yu et al.
The Journal of biological chemistry, 275(6), 4183-4191 (2000-02-08)
Many matrix metalloproteinases (MMPs) are tightly bound to tissues; matrilysin (MMP-7), although the smallest of the MMPs, is one of the most tightly bound. The most likely docking molecules for MMP-7 are heparan sulfate proteoglycans on or around epithelial cells
Glycosaminoglycan binding assays.
A J Hoogewerf et al.
Methods in molecular biology (Clifton, N.J.), 138, 173-177 (2000-06-07)
B A Kluszynski et al.
The Journal of biological chemistry, 272(21), 13541-13547 (1997-05-23)
We have studied the ability of histidine-rich glycoprotein (HRG) to neutralize the anticoagulant activity of heparin in plasma and in a purified component clotting assay. Addition of HRG to plasma or to the purified component assay did not neutralize the
Miriam Corredor et al.
Biophysical journal, 110(6), 1291-1303 (2016-03-31)
Semaphorin3A (Sema3A) is a vertebrate-secreted protein that was initially characterized as a repulsive-guidance cue. Semaphorins have crucial roles in several diseases; therefore, the development of Sema3A inhibitors is of therapeutic interest. Sema3A interacts with glycosaminoglycans (GAGs), presumably through its C-terminal

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