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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

Certificados de análisis (COA)

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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
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
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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