Echistatin
Based on 1 Customer Validation
Echistatin is a naturally derived RGD-containing snake venom peptide. Echistatin exhibits an IC50 of 0.6 nM against mouse αvβ3 integrin, and acts as an antagonist against αvβ3, αIIbβ3, α5β1 integrins, pp125FAK and paxillin. Echistatin reduces the phosphorylation of pp125FAK and paxillin, inhibits the autophosphorylation and kinase activity of pp125FAK, and weakens its binding to pp60src and paxillin. Echistatin disrupts the actin cytoskeleton and focal adhesions, induces melanoma cell detachment from fibronectin, and regulates cell adhesion and motility. Echistatin inhibits osteoclast maturation and migration, bone resorption, platelet aggregation, bone loss, as well as adhesion and metastasis of Lewis lung cancer cells; it also increases the number of osteoclasts and bone coverage area in mice with secondary hyperparathyroidism. Echistatin can be used in research related to melanoma, lung cancer and secondary hyperparathyroidism.
For research use only. We do not sell to patients.
- Purity: 91.33%
- CAS No.: 154303-05-6
- Formula: C217H341N71O74S9
- Molecular Weight:5417.00
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Storage:
Sealed storage, away from moisture.
Powder -80°C, 2 years , -20°C, 1 year* In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture)
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
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Biological Activity
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Chemical Information
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Solvent & Solubility
- Purity & Documentation
- References
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Help & FAQs
Biological Activity
|
αvβ3 |
α5β1 |
αIIbβ3 |
Echistatin (100 μg/mL; 15 min-3 h) reduces the phosphorylation level of pp125FAK Tyr397 in fibronectin-adherent B16-BL6 mouse melanoma cells; decreases the binding level of pp125FAK to paxillin in a time-dependent manner; and inhibits the autophosphorylation of pp125FAK, the phosphorylation of paxillin, and the binding level of pp125FAK to pp60src[1].
Echistatin (100 μg/mL; 30 min) induces detachment of fibronectin-adherent B16-BL6 mouse melanoma cells and causes loss of pp125FAK and paxillin from focal adhesions[1].
Echistatin (10 nCi/tube; 1 h) binds specifically to αvβ3 integrin in membrane fractions enriched from mouse osteoclast-like cells, with an IC50 of 0.6 nM, and this binding is selectively blocked by anti-αvβ3 integrin antibody[2].
Echistatin (100 nM; 7 days, days 0-4, days 4-7) potently inhibits the formation of TRAP-positive multinucleated osteoclast-like cells in a mouse MB1.8 cell-bone marrow co-culture system, with an IC50 of 0.7 nM[2].
Echistatin (10-11 to 10-8 M; 15 h) inhibits M-CSF-induced fusion of mouse mononuclear pre-fusion osteoclasts with an IC50 of 0.6 nM, and inhibits M-CSF-induced migration of mouse mononuclear pre-fusion osteoclasts with an IC50 of 1.0 nM[2].
Echistatin enables the quantitative detection of Echistatin levels in biological samples via competitive receptor binding assays, in which Echistatin extracts from HEK 293 cells overexpressing αvβ3 integrin displace radiolabeled Echistatin[3].
Echistatin (0.1-20 μg/mL; 10 min-6 days) is a reversible, non-cytotoxic inhibitor that suppresses the adhesion of Lewis lung carcinoma (3LL) cells to immobilized fibronectin and laminin in vitro[4].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
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Cell Line:fibronectin-adherent B16-BL6 mouse melanoma cells
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Concentration:100 μg/mL
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Incubation Time:15 min, 30 min, 1 h
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Result:Caused a 69% decrease in Tyr397-phosphorylated pp125FAK levels compared to untreated control cells after 15 min.
Reduced Tyr397 phosphorylation by 39% after 1 h, with a less pronounced decrease observed at 30 min compared to 15 min.
Confirmed equal protein loading across all samples via reprobing with anti-pp125FAK antibody.
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Cell Line:fibronectin-adherent B16-BL6 mouse melanoma cells
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Concentration:100 μg/mL
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Incubation Time:15 min, 30 min, 1 h, 3 h
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Result:Caused a 42% decrease in paxillin phosphorylation after 15 min.
Reduced paxillin phosphorylation by 63% after 1 h.
Reduced paxillin phosphorylation by 68% after 3 h.
Confirmed equal protein loading via reprobing with anti-paxillin antibody.
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Cell Line:fibronectin-adherent B16-BL6 mouse melanoma cells
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Concentration:100 μg/mL
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Incubation Time:30 min
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Result:Induced progressive cell detachment from the fibronectin substratum, cell rounding, and the disappearance of both pp125FAK and paxillin from focal adhesions.
Observed pp125FAK and paxillin colocalized in focal adhesion structures with additional diffuse cytoplasmic and perinuclear staining in untreated cells.
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Cell Line:murine osteoblastic MB1.8 cells, BALB/c mouse bone marrow cells
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Concentration:100 nM
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Incubation Time:7 days (0-7d), for the first 4 days (0-4d), or for the last 3 days (4-7d)
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Result:Completely inhibited formation of TRAP-positive multinucleated cells when present for the full 7-day period or only days 4-7.
Had no effect on formation of TRAP-positive multinucleated cells when added only days 0-4.
Inhibited formation of TRAP-positive multinucleated cells in a dose-dependent and RGD-dependent manner, with an IC50 of 0.7 nM.
Did not inhibit formation of TRAP-positive mononuclear cells.
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Cell Line:95% pure murine mononuclear prefusion osteoclasts (pOCs)
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Concentration:10-11, 10-10, 10-9, 10-8 M
10 nM -
Incubation Time:15 h
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Result:Inhibited M-CSF-induced pOC fusion in a dose-dependent, RGD-dependent manner, with an IC50 of 0.6 nM.
Had no inhibitory effect on spontaneous fusion of pOCs at high plating densities.
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Cell Line:95% pure murine mononuclear prefusion osteoclasts (pOCs)
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Concentration:10-11, 10-10, 10-9, 10-8, 10-7 M
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Incubation Time:20 min preincubation; 15 h migration incubation
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Result:Inhibited M-CSF-induced pOC migration in a dose-dependent, RGD-dependent manner, with an IC50 of 1.0 nM.
Echistatin (6-30 µg/kg/min; subcutaneous injection; continuous infusion; 6 h) inhibits the acute calcemic response to exogenous PTH in parathyroidectomized mice[3].
Echistatin (20 μg；intramuscular injection; co-injected once together with tumor cells) co-administrated with 2.5 × 105 3LL cells via intramuscular injection suppresses tumor growth and metastasis of Lewis lung carcinoma in male C57BL/6NCrlBR mice[4].
Echistatin (1 μg/g; intraperitoneal injection; once every 72 hours; 4 doses total) inhibits Lewis lung cancer tumor growth and metastasis formation in male C57BL/6NCrlBR mice[4].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
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Animal Model:BALB/C (male, 9 weeks old, ~20 g, secondary hyperparathyroidism induced by low calcium diet)[3]
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Dosage:30 µg/kg/min
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Administration:s.c.; continuous infusion; 3 days
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Result:Preserved trabecular bone microarchitecture (BV/TV, thickness, number, spacing) close to normal levels and blocked bone loss in low-calorie mice, elevated femoral ash weight moderately, and restrained excessive osteoid accumulation.
Upregulated osteoclast surface and count relative to model mice without altering osteoclast polarity or average nuclei number.
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Animal Model:BALB/C (male, 9 weeks old, ~20 g, thyroparathyroidectomized with exogenous PTH infusion)[3]
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Dosage:30 µg/kg/min; 6 µg/kg/min
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Administration:s.c.; continuous infusion; 6 hours
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Result:Completely blocked the PTH-induced increase in serum calcium at the 30 µg/kg/min dose.
Achieved mean serum echistatin levels of 152.2 nM at the 30 µg/kg/min dose and 77.8 nM at the 6 µg/kg/min dose at euthanasia.
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Animal Model:C57BL/6NCrlBR (1-month-old male, 20-22 g, intramuscular injection of 2.5 × 105 viable 3LL cells)[4]
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Dosage:20 μg
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Administration:i.m.; single co-injection with tumor cells
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Result:Reduced tumor weight by 10%.
Inhibited lung metastasis formation by 20%.
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Animal Model:C57BL/6NCrlBR (1-month-old male, 20-22 g, intramuscular injection of 5 × 105 viable 3LL cells)[4]
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Dosage:1 μg/g body weight; total 80 μg/mouse
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Administration:i.p.; every 72 hours; 4 total doses
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Result:Inhibited tumor growth by 15%.
Inhibited lung metastasis formation by 41%.
Chemical Information
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CAS No. 154303-05-6
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Appearance Solid
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Molecular Weight 5417.00
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Formula C217H341N71O74S9
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Color White to off-white
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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 (Disulfide bridge:Cys2-Cys11;Cys7-Cys32;Cys8-Cys37;Cys20-Cys39)
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Sequence Shortening
ECESGPCCRNCKFLKEGTICKRARGDDMDDYCNGKTCDCPRNPHKGPAT (Disulfide bridge:Cys2-Cys11;Cys7-Cys32;Cys8-Cys37;Cys20-Cys39)
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Structure Classification
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Initial Source
snake Echis carinatus
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Shipping
Room temperature in continental US; may vary elsewhere.
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Storage
Sealed storage, away from moisture
Powder -80°C 2 years -20°C 1 year * In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture)
Solvent & Solubility
H2O
Peptide Solubility and Storage Guidelines:
1. Calculate the length of the peptide.
2. Calculate the overall charge of the entire peptide according to the following table:
| Contents | Assign value | |
|---|---|---|
| Acidic amino acid | Asp (D), Glu (E), and the C-terminal -COOH. | -1 |
| Basic amino acid | Arg (R), Lys (K), His (H), and the N-terminal -NH2 | +1 |
| Neutral amino acid | Gly (G), Ala (A), Leu (L), Ile (I), Val (V), Cys (C), Met (M), Thr (T), Ser (S), Phe (F), Tyr (Y), Trp (W), Pro (P), Asn (N), Gln (Q) | 0 |
3. Recommended solution:
| Overall charge of peptide | Details |
|---|---|
| Negative (<0) |
1. Try to dissolve the peptide in water first. 2. If water fails, add NH4OH (<50 μL). 3. If the peptide still does not dissolve, add DMSO (50-100 μL) to solubilize the peptide. |
| Positive (>0) |
1. Try to dissolve the peptide in water first. 2. If water fails, try dissolving the peptide in a 10%-30% acetic acid solution. 3. If the peptide still does not dissolve, try dissolving the peptide in a small amount of DMSO. |
| Zero (=0) |
1. Try to dissolve the peptide in organic solvent (acetonitrile, methanol, etc.) first. 2. For very hydrophobic peptides, try dissolving the peptide in a small amount of DMSO, and then dilute the solution with water to the desired concentration. |
Purity & Documentation
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Data Sheet (277 KB)
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SDS (393 KB)
- English - EN (393 KB)
- Français - FR (393 KB)
- Deutsch - DE (393 KB)
- Norwegian - NO (393 KB)
- Español - ES (393 KB)
- Swedish - SV (393 KB)
- Italian - IT (393 KB)
- Korean - KR (393 KB)
- Portuguese - PT (393 KB)
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Handling Instructions (2659 KB)
References
[1]. Della Morte R, et al. Echistatin inhibits pp125FAK autophosphorylation, paxillin phosphorylation and pp125FAK-paxillin interaction in fibronectin-adherent melanoma cells. European journal of biochemistry. 2000 Aug;267(16):5047-54. [Content Brief]
[2]. Nakamura I, et al. Echistatin inhibits the migration of murine prefusion osteoclasts and the formation of multinucleated osteoclast-like cells. Endocrinology. 1998 Dec;139(12):5182-93. [Content Brief]
[3]. Masarachia P, et al. Histomorphometric evidence for echistatin inhibition of bone resorption in mice with secondary hyperparathyroidism. Endocrinology. 1998 Mar;139(3):1401-10. [Content Brief]
[4]. Spalleticernia D, et al. Echistatin inhibits Lewis lung carcinoma cell-matrix adhesion in vitro and experimental metastasis in vivo. International journal of oncology. 1997 Oct;11(4):757-63. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
Echistatin Related Classifications
HY-P1189 Related Classifications
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