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Merck
CN

H0402

Heparin−Agarose

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

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About This Item

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

Quality Level

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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

signalword

Warning

hcodes

Hazard Classifications

Flam. Liq. 3

Storage Class

3 - Flammable liquids

wgk

WGK 3

flash_point_f

104.0 °F - closed cup

flash_point_c

40 °C - closed cup

Regulatory Information

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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)
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
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

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