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| Description | Obtustatin (CAS: 404882-00-4) is a short-chain disintegrin isolated from the venom of the viper Vipera lebetina obtusa, 31 amino acids with 4 disulfide bridges, sequence Cys-Lys-Cys-Thr-Cys-Gly-Thr-Cys-Gly-Thr-Glu-Tyr-Thr-Cys-Asn-Gln-Gly-Gly-Cys-Thr-Gly-Ser-Cys-Gly-Lys-Cys-Val-Cys, molecular formula C₁₈₄H₂₈₄N₅₂O₅₇S₈, MW 4393.06 Da. It is a potent, selective inhibitor of integrin α1β1 adhesion to collagen IV, inhibits angiogenesis, and is used in cancer-related research. |
| Structure type | 31-mer short-chain disintegrin (4 disulfide bridges) |
| Solubility | Soluble in water, PBS |
| Storage | Powder -20°C, dry, protected from light |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| Obtustatin (KTS-disintegrin) | Obtustatin; CTTGPCCRQCKLKPAGTTCWKTSLTSHYCTGKSCDCPLYPG; snake-venom short disintegrin; selective alpha1beta1 integrin antagonist; CAS 404882-00-4 | snake-venom disintegrin, KTS-motif non-RGD disintegrin, alpha1beta1 integrin antagonism, collagen receptor antagonism, cysteine-rich, 4 disulfide bonds, angiogenesis inhibition, tumor-vessel targeting, 41-mer mini-protein, reducing-agent sensitive | The shortest natural short disintegrin isolated from the venom of the viper Vipera lebetina obtusa (note: the established literature source is Vipera lebetina obtusa, NOT Crotalus adamanteus). Sequence CTTGPCCRQCKLKPAGTTCWKTSLTSHYCTGKSCDCPLYPG, 41 residues: Cys1-Thr2-Thr3-Gly4-Pro5-Cys6-Cys7-Arg8-Gln9-Cys10-Lys11-Leu12-Lys13-Pro14-Ala15-Gly16-Thr17-Thr18-Cys19-Trp20-Lys21-Thr22-Ser23-Leu24-Thr25-Ser26-His27-Tyr28-Cys29-Thr30-Gly31-Lys32-Ser33-Cys34-Asp35-Cys36-Pro37-Leu38-Tyr39-Pro40-Gly41. It contains 8 Cys forming 4 disulfide bonds with pairing (consistent across IUPHAR/BPS Guide to PHARMACOLOGY, MCE, TargetMol): Cys1-Cys10, Cys6-Cys29, Cys7-Cys34, Cys19-Cys36. Key feature: the active loop displays KTS (Lys-Thr-Ser) rather than the canonical RGD, making it a non-RGD KTS-disintegrin. C-terminus is a free acid. Net charge at pH ~7 is about +5 (Arg x1, Lys x4, His x1 positive; Asp x1 negative); all 8 cysteine thiols are engaged in disulfide bonds with no free thiol. Formula C184H284N52O57S8. | C184H284N52O57S8 | 4389.87 | 4393.08 | Free peptide (supplied as powder). Formula C184H284N52O57S8, exact mass ~4389.87 Da, average MW ~4393.08 Da, consistent with TargetMol catalog MW 4393.07; a triacetate salt form (~4573.21 Da) is an alternative supplier specification. | 41 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-OBTUST-01 | White to off-white powder (cysteine-rich mini-protein) | -20°C, dry, sealed, light-protected; the 4 disulfide bonds are required for the active conformation, so strictly avoid reducing agents (DTT / beta-mercaptoethanol / TCEP); aliquot and avoid repeated freeze-thaw | 2-8°C, dry and light-protected, for several weeks | Cysteine-rich with a Trp/His/Tyr hydrophobic face; water solubility is moderate. Reconstitute first with a small volume of sterile water or neutral buffer (pH 6.5-7.4); if needed, use a little DMSO or dilute acetic acid to aid dissolution before dilution to the working concentration. Aliquot solutions and store at -20°C, avoid repeated freeze-thaw. Never add DTT, beta-mercaptoethanol or any reducing agent, or the disulfides will break and the active conformation will be lost. | The disulfide-bonded conformation is stable in the solid; long-term at -20°C dry, light-protected, with desiccant; weigh quickly after opening and reseal immediately against moisture |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-OBTUST-01 | A 41-mer short disintegrin from Vipera lebetina obtusa venom, sequence CTTGPCCRQCKLKPAGTTCWKTSLTSHYCTGKSCDCPLYPG, 4 disulfide bonds (C1-C10/C6-C29/C7-C34/C19-C36), formula C184H284N52O57S8, MW ~4393.08; via its KTS (not RGD) active loop it selectively antagonizes the alpha1beta1 collagen-receptor integrin, serving as a potent angiogenesis inhibitor and tumor-vessel research tool; reducing-agent sensitive. | Obtustatin is the shortest natural short disintegrin purified from the venom of the viper Vipera lebetina obtusa, first characterized by Moreno-Murciano, Calvete and colleagues (J Biol Chem / Cancer Res 2003, 63:2020); it is only 41 residues. It shares a similar cysteine scaffold with classic RGD disintegrins (echistatin, eristostatin), but its active loop displays the KTS (Lys-Thr-Ser) triad rather than RGD, classifying it as a non-RGD KTS-disintegrin - the single most important distinction from most snake-venom disintegrins. Eight cysteines form four conserved disulfide bonds (Cys1-Cys10, Cys6-Cys29, Cys7-Cys34, Cys19-Cys36), folding the chain into a compact, rigid short-disintegrin fold that holds the KTS loop in a fixed receptor-recognition geometry. Functionally, obtustatin is among the most potent and selective antagonists of alpha1beta1 integrin (the collagen receptor) reported: it binds activated alpha1beta1 and competitively blocks adhesion of collagen (e.g. type IV) to endothelial alpha1beta1, thereby inhibiting endothelial-cell migration, capillary-like tube formation, and growth-factor- and tumor-induced angiogenesis in vivo. Unlike broad-spectrum RGD disintegrins (which hit alphaIIb beta3, alpha v beta3, alpha5beta1 and platelet aggregation simultaneously), obtustatin is highly selective for alpha1beta1 with essentially no action on alpha v beta3, alpha5beta1 or alphaIIb beta3, so it causes little platelet-aggregation inhibition or bleeding; this makes it a selective probe for studying the role of alpha1beta1 in angiogenesis, fibrosis and tumor vascularization. This product is supplied in the active disulfide-bonded conformation; storage and reconstitution must strictly avoid DTT, beta-mercaptoethanol and TCEP, which would break the disulfides, unfold the KTS loop and abolish activity. CAS 404882-00-4; sequence and disulfide pairing per IUPHAR/BPS Guide to PHARMACOLOGY, MedChemExpress, TargetMol catalogs and the primary literature. | snake-venom disintegrin, selective alpha1beta1 integrin antagonism, angiogenesis inhibition, tumor-angiogenesis research, collagen-receptor integrin studies, KTS-disintegrin, endothelial migration/tube formation, anti-angiogenic lead | alpha1beta1 integrin (collagen receptor, highly selective); competitively blocks type-IV collagen-endothelial alpha1beta1 adhesion; does not act on alpha v beta3 / alpha5beta1 / alphaIIb beta3 |
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