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H0402

Sigma-Aldrich

Heparin−Agarose

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

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About This Item

MDL number:
MFCD00163876
UNSPSC Code:
23151817
NACRES:
NA.56

biological source

heparin from Porcine intestinal mucosa

form

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

matrix

4% beaded agarose

matrix activation

epichlorohydrin

matrix attachment

terminal aldehyde by reductive amination to amine linker

matrix spacer

7 atoms

capacity

≥0.5 mg/mL binding capacity (thrombin)

storage temp.

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.

Physical form

1:1 suspension in a 20% ethanol solution

Preparation Note

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

pictograms

Flame
GHS02

signalword

Warning

hcodes

H226

Hazard Classifications

Flam. Liq. 3

Storage Class

3 - Flammable liquids

wgk_germany

WGK 3

flash_point_f

104.0 °F - closed cup

flash_point_c

40 °C - closed cup

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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
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
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
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