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Echistatin (TFA)

Echistatin TFA, the smallest active RGD protein belonging to the family of disintegrins that are derived from snake venoms, is a potent inhibitor of platelet aggregation. Echistatin is a potent inhibitor of bone resorption in culture. Echistatin is a potent antagonist of αIIbβ3, αvβ3 and α5β1[1][2][3][4].

Product Specifications

UNSPSC

12352209

Target

Integrin

Type

Peptides

Related Pathways

Cytoskeleton

Applications

Metabolism-protein/nucleotide metabolism

Field of Research

Metabolic Disease; Inflammation/Immunology

Assay Protocol

https://www.medchemexpress.com/echistatin-tfa.html

Purity

99.32

Solubility

H2O : 50 mg/mL (ultrasonic)

Smiles

O=C(O)C(F)(F)F.O=C(N[C@@H](CSSC[C@@H](C(N[C@@H](CCCCN)C(N[C@@H](CC1=CC=CC=C1)C(N[C@@H](CC(C)C)C(N[C@@H](CCCCN)C(N[C@@H](CCC(O)=O)C(NCC(N[C@@H]([C@H](O)C)C(N[C@@H]([C@@H](C)CC)C(N[C@@H](CSSC[C@@H](C(N2[C@@H](CCC2)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CC(N)=O)C(N3[C@@H](CCC3)C(N[C@@H](CC4=CNC=N4)C(N[C@@H](CCCCN)C(NCC(N5[C@@H](CCC5)C(N[C@@H](C)C(N[C@@H]([C@H](O)C)C(O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)NC6=O)C(N[C@@H](CCCCN)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](C)C(N[C@@H](CCCNC(N)=N)C(NCC(N[C@@H](CC(O)=O)C(N[C@@H](CC(O)=O)C(N[C@@H](CCSC)C(N[C@@H](CC(O)=O)C(N[C@@H](CC(O)=O)C(N[C@H]7CC8=CC=C(C=C8)O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)NC9=O)C(N[C@@H](CCC(O)=O)C(N[C@@H](CO)C(NCC(N%10[C@@H](CCC%10)C(N[C@@H](CSSC[C@@H](C(N[C@@H](CC(N)=O)C(NCC(N[C@@H](CCCCN)C(N[C@H]%11[C@H](O)C)=O)=O)=O)=O)NC7=O)C(N[C@@H](CSSC[C@@H](C(N[C@H]6CC(O)=O)=O)NC%11=O)C(N[C@@H](CCCNC(N)=N)C(N[C@H]9CC(N)=O)=O)=O)=O)=O)=O)=O)=O)=O)[C@H](CCC(O)=O)N.[x]

Molecular Formula

C217H341N71O74S9.xC2HF3O2

Molecular Weight

5417.00 (free acid)

References & Citations

[1]J Musial, et al. Inhibition of platelet adhesion to surfaces of extracorporeal circuits by disintegrins. RGD-containing peptides from viper venoms. Circulation. 1990 Jul;82 (1) :261-73.|[2]M Sato, et al. Echistatin is a potent inhibitor of bone resorption in culture. J Cell Biol. 1990 Oct;111 (4) :1713-23.|[3]C C Kumar, et al. Biochemical characterization of the binding of echistatin to integrin alphavbeta3 receptor. J Pharmacol Exp Ther. 1997 Nov;283 (2) :843-53.|[4]I Wierzbicka-Patynowski, et al. Structural requirements of echistatin for the recognition of alpha (v) beta (3) and alpha (5) beta (1) integrins. J Biol Chem. 1999 Dec 31;274 (53) :37809-14.

Shipping Conditions

Blue Ice

Storage Conditions

-80°C, 2 years; -20°C, 1 year (Powder, sealed storage, away from moisture)

Scientific Category

Peptides

Clinical Information

No Development Reported

Isoform

α5β1; αIIbβ3; αvβ3

Available Sizes

Curated Selection

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