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由来生物
Echis carinatus
アッセイ
≥90% (HPLC)
フォーム
powder
テクニック
flow cytometry: suitable
inhibition assay: suitable
保管温度
−20°C
Amino Acid Sequence
Glu-Cys-Glu-Ser-Gly-Pro-Cys-Cys-Arg-Asn-Cys-Lys-Phe-Leu-Lys-Glu-Gly-Thr-Ile-Cys-Lys-Arg-Ala-Arg-Gly-Asp-Asp-Met-Asp-Asp-Tyr-Cys-Asn-Gly-Lys-Thr-Cys-Asp-Cys-Pro-Arg-Asn-Pro-His-Lys-Gly-Pro-Ala-Thr
詳細
Echistatin is a single chain 49 amino acid residue protein, which prevents the aggregation of platelets. It has an isoelectric point (pI) of 8.3 and a molecular weight of 5400. This peptide is present in the venom of Echis carinatus, which is a saw-scaled viper. It contains the arginine-glycine-aspartic (RGD) acid sequence, which is present in proteins that bind to glycoprotein IIb/IIIa complex. It shares the proline-arginine-asparagine-proline sequence with the Aα chain of human fibrinogen. This protein is a member of disintegrin family, which prevents cell adhesion. With regards to molecular weight, echistatins are the smallest member of disintegrin family, and contains four isoforms called, α1, α2, β and γ.
アプリケーション
Echistatin has been used:
- as an inhibitor of integrin function to study the role of microfibril-associated glycoprotein-1 (Magp1) in the morphogenesis of vascular structures
- for the preparation of microbubbles targeted to αvβ3 integrins in tumor angiogenesis imaging
- as a conjugate to αvβ3 in flow cytometric binding studies
生物化学的／生理学的作用
Disintegrin類は、マムシ毒から分離されたintegrin β1およびβ3インヒビタ-タンパク質の新規ファミリ-です。低分子量でシステイン残基に富むペプチドであり、Arg-Gly-Asp(RGD)配列を含みます。Integrinの機能に対する最も強力なインヒビタ-として知られています。Disintegrinは、メラノ-マ細胞や線維芽細胞とフィブロネクチンとの接着のような細胞外マトリックスへの細胞接着を阻害するほか、血小板凝集も強力に阻害します。
ディスインテグリンファミリ-メンバ-、インテグリンβ1およびβ3の新規阻害タンパク質、およびインテグリン機能の最も強力なインヒビタ-です。
Echistatin is a disintegrin, which prevents the aggregation of platelets. They interact with and prevent the binding of fibrinogen to their receptors on the membrane of platelets. It also inhibits platelet aggregation mediated by epinephrine, thrombin, collagen, or platelet-activating factor. Studies in isolated osteoclasts show that this peptide inhibits bone resorption by osteoclasts, most probably by damaging adhesion structures.
保管分類コード
11 - Combustible Solids
WGK
WGK 3
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
E2138-50UG:
E2138PROC:
E2138-.1MG:
E2138-BULK:
E2138-VAR:
E2138-PPG:
E2138-PH:
M Gawaz et al.
Circulation, 96(6), 1809-1818 (1997-10-10)
Platelet interaction with endothelium plays an important role in the pathophysiology of coronary microcirculation. We assessed the role of the vitronectin receptor (integrin alpha(v)beta3) in platelet/endothelium adhesion. We investigated the effect on platelet/endothelium adhesion of plasma obtained from patients with
M Sato et al.
The Journal of cell biology, 111(4), 1713-1723 (1990-10-01)
The venom protein, s-echistatin, originally derived from the saw-scaled viper Echis carinatus, was found to be a potent inhibitor of bone resorption by isolated osteoclasts. This Arg24-Gly25-Asp26-(RGD)-containing protein inhibited the excavation of bone slices by rat osteoclasts (IC50 = 0.1
L C Chuang et al.
Biochemical and biophysical research communications, 220(2), 246-254 (1996-03-18)
An echistatin analogue, designated as des(46-49)-[Ala8,37]-echistatin gamma, was synthesized chemically by solid-phase peptide synthesis. The analogue was made by replacing Cys8 and Cys37 residues with two alanines and the deletion of C-terminal peptide 46-49 of echistatin gamma, resulting in an
Z R Gan et al.
The Journal of biological chemistry, 263(36), 19827-19832 (1988-12-25)
A 49-residue protein, echistatin, which inhibits platelet aggregation, was purified from the venom of the saw-scaled viper Echis carinatus. The purification procedure included gel filtration on Sephadex G-50, cation-exchange chromatography on Mono S, and C18 reverse-phase high pressure liquid chromatography.
Functional and computational studies of the ligand-associated metal binding site of beta3 integrins.
Marta Murcia et al.
Proteins, 71(4), 1779-1791 (2008-01-05)
A combination of experimental and computational approaches was used to provide a structural context for the role of the beta3 integrin subunit ligand-associated metal binding site (LIMBS) in the binding of physiological ligands to beta3 integrins. Specifically, we have carried
ライフサイエンス、有機合成、材料科学、クロマトグラフィー、分析など、あらゆる分野の研究に経験のあるメンバーがおります。.
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