추천 제품
생물학적 소스
heparin from Porcine intestinal mucosa
Quality Level
양식
(1:1 suspension in a 20% ethanol solution)
Matrix
4% beaded agarose
기질 활성
epichlorohydrin
기질 부착
terminal aldehyde by reductive amination to amine linker
기질 스페이서
7 atoms
용량
≥0.5 mg/mL binding capacity (thrombin)
저장 온도
2-8°C
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애플리케이션
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.
물리적 형태
1:1 suspension in a 20% ethanol solution
제조 메모
Prepared by end-point attachment for high-efficiency fractionation of antithrombin III and other specific binding proteins
신호어
Warning
유해 및 위험 성명서
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
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
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
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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