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Key Documents

H0402

Sigma-Aldrich

Heparin−Agarose

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

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About This Item

Numéro MDL:
Code UNSPSC :
23151817
Nomenclature NACRES :
NA.56

Source biologique

heparin from Porcine intestinal mucosa

Forme

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

Matrice

4% beaded agarose

Activation de la matrice

epichlorohydrin

Fixation de matrice

terminal aldehyde by reductive amination to amine linker

Espaceur de matrice

7 atoms

Capacité

≥0.5 mg/mL binding capacity (thrombin)

Température de stockage

2-8°C

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Application

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.

Forme physique

1:1 suspension in a 20% ethanol solution

Notes préparatoires

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

Pictogrammes

Flame

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Flam. Liq. 3

Code de la classe de stockage

3 - Flammable liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

104.0 °F - closed cup

Point d'éclair (°C)

40 °C - closed cup


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Glycosaminoglycan binding assays.
A J Hoogewerf et al.
Methods in molecular biology (Clifton, N.J.), 138, 173-177 (2000-06-07)
M Zhou et al.
Journal of molecular biology, 271(3), 362-373 (1997-08-22)
Tn5 transposase (Tnp) binds to Tn5 and IS50 end inverted repeats, the outside end (OE) and the inside end (IE), to initiate transposition. We report the isolation of four Tnp mutants (YH41, TP47, EK54 and EV54) that increase the OE-mediated
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
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
Yongcheng Wang et al.
Molecular cell, 15(3), 343-353 (2004-08-12)
Amyloid beta-peptide, which forms neuronal and vascular amyloid deposits in Alzheimer's disease, is derived from an integral membrane protein precursor. The biological function of the precursor is currently unclear. Here we describe the X-ray structure of E2, the largest of

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