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Merck
모든 사진(1)

문서

H3917

Sigma-Aldrich

Heparinase I and III Blend from Flavobacterium heparinum

lyophilized powder, stabilized with ∼ 25% (w/w) bovine serum albumin, ≥200 unit/mg protein (enzyme + BSA)

동의어(들):

Heparinase I and Heparinase III blend

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About This Item

효소 위원회 번호:
UNSPSC 코드:
12352204
NACRES:
NA.54

생물학적 소스

bacterial (Flavobacterium heparinum)

Quality Level

결합

conjugate (Glucosaminoglycan)

형태

lyophilized powder

특이 활성도

≥200 units/mg protein

농도

≥200 unit/mg protein (enzyme + BSA)

배송 상태

dry ice

저장 온도

−20°C

일반 설명

Heparinase is an inducible, non-extracellular heparin-degrading enzyme. Three types of heparinises are produced by Flavobacterium heparinum and contains specific sequences of heparin.

애플리케이션

Heparinase I and III Blend from Flavobacterium heparinum has been used in:
  • the digestion of heparan sulfate from ovine vitreous
  • human embryonic kidney cells
  • glycosaminoglycans from arterial tissues
  • P0 retinae digestion

생화학적/생리학적 작용

Heparinase I and III plays vital role in various biological processes: modulate cell-growth factor interactions, cell-lipoprotein interactions, neovascularization. It cleaves highly sulphated polysaccharide chains in presence of 2-O-sulfated α-L-idopyranosyluronic acid and β-D-glucopyranosyluronic acid residues of polysaccharides.
Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate.

포장

Sold on the basis of Heparinase I units

단위 정의

One unit will form 0.1 micromole of unsaturated uronic acid per hour at 7.5 at 25 degrees C using Heparin, Sodium as substrate for heparinase I.

One unit will form 0.1 micromole of unsaturated uronic acid per hour at 7.5 at 25 degrees C using bovine kidney Heparan, Sulfate as substrate for heparinase III.

One unit will form 0.1 μmole of unsaturated uronic acid per hr at pH 7.5 at 25 °C. One International Unit (I.U.) is equivalent to approx. 600 Sigma units. Package sizes are sold in Sigma units.

기타 정보

Enzyme Commission Numbers: 4.2.2.7 Hep I and 4.2.2.8 Hep III

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


시험 성적서(COA)

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문서 라이브러리 방문

S Ernst et al.
Critical reviews in biochemistry and molecular biology, 30(5), 387-444 (1995-01-01)
Glycosaminoglycans (GAGs) play an intricate role in the extracellular matrix (ECM), not only as soluble components and polyelectrolytes, but also by specific interactions with growth factors and other transient components of the ECM. Modifications of GAG chains, such as isomerization
Farizeh Aalam et al.
PLoS pathogens, 16(10), e1008968-e1008968 (2020-10-20)
Despite 25 years of research, the basic virology of Kaposi Sarcoma Herpesviruses (KSHV) in B lymphocytes remains poorly understood. This study seeks to fill critical gaps in our understanding by characterizing the B lymphocyte lineage-specific tropism of KSHV. Here, we
P M Galliher et al.
Applied and environmental microbiology, 41(2), 360-365 (1981-02-01)
Heparinase production by Flavobacterium heparinum in complex protein digest medium, with heparin employed as the inducer, has been studied and improved. The maximum productivity of heparinase has been increased 156-fold over that achieved by previously published methods to 375 U/liter
D A Chappell et al.
The Journal of biological chemistry, 268(19), 14168-14175 (1993-07-05)
Bovine milk lipoprotein lipase (LPL) induced binding, uptake, and degradation of 125I-labeled normal human triglyceride-rich lipoproteins by cultured mutant fibroblasts lacking LDL receptors. The induction was dose-dependent and occurred whether LPL and 125I-lipoproteins were added to incubation media simultaneously or
Cassandra R Blanchette et al.
PLoS genetics, 13(1), e1006525-e1006525 (2017-01-10)
The regulation of cell migration is essential to animal development and physiology. Heparan sulfate proteoglycans shape the interactions of morphogens and guidance cues with their respective receptors to elicit appropriate cellular responses. Heparan sulfate proteoglycans consist of a protein core

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