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Merck
CN

H0402

Sigma-Aldrich

Heparin−Agarose

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

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About This Item

MDL编号:
UNSPSC代码:
23151817
NACRES:
NA.56

生物来源

heparin from Porcine intestinal mucosa

质量水平

表单

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

基质

4% beaded agarose

基质活化

epichlorohydrin

基质附着

terminal aldehyde by reductive amination to amine linker

基质隔离区

7 atoms

容量

≥0.5 mg/mL binding capacity (thrombin)

储存温度

2-8°C

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应用

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.

外形

1:1 suspension in a 20% ethanol solution

制备说明

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

象形图

Flame

警示用语:

Warning

危险声明

危险分类

Flam. Liq. 3

储存分类代码

3 - Flammable liquids

WGK

WGK 3

闪点(°F)

104.0 °F - closed cup

闪点(°C)

40 °C - closed cup

法规信息

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分析证书(COA)

Lot/Batch Number

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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
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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