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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

MDL number:
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

Signal Word

Warning

Hazard Statements

Hazard Classifications

Flam. Liq. 3

Storage Class Code

3 - Flammable liquids

WGK

WGK 3

Flash Point(F)

104.0 °F - closed cup

Flash Point(C)

40 °C - closed cup


Certificates of Analysis (COA)

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M Zhou et al.
Journal of molecular biology, 271(3), 362-373 (1997-08-22)
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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)
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
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

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