A caspase-2, caspase-3, and caspase-7 inhibitor
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Alternative(s)
27426Z-VDVAD-pNA (trifluoroacetate salt)
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Ac-VDVAD-CHO (trifluoroacetate salt)

Item No. 27136

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
N-acetyl-L-valyl-L-α-aspartyl-L-valyl-N-[(1S)-2-carboxy-1-formylethyl]-L-alaninamide, trifluoroacetate salt
Synonyms
  • Ac-Val-Asp-Val-Ala-Asp-CHO
Molecular Formula
C23H37N5O10 • XCF3COOH
Formula Weight
543.6
Purity
≥95%
Formulation (Request formulation change)
A solid
Solubility(Learn about Variance in Solubility)
Water: 1 mg/ml
SMILES
OC(C[C@H](NC([C@H](C)NC([C@@H](NC([C@H](CC(O)=O)NC([C@@H](NC(C)=O)C(C)C)=O)=O)C(C)C)=O)=O)C=O)=O.FC(F)(C(O)=O)F
InChi Code
InChI=1S/C23H37N5O10.C2HF3O2/c1-10(2)18(25-13(6)30)23(38)27-15(8-17(33)34)21(36)28-19(11(3)4)22(37)24-12(5)20(35)26-14(9-29)7-16(31)32;3-2(4,5)1(6)7/h9-12,14-15,18-19H,7-8H2,1-6H3,(H,24,37)(H,25,30)(H,26,35)(H,27,38)(H,28,36)(H,31,32)(H,33,34);(H,6,7)/t12-,14-,15-,18-,19-;/m0./s1
InChi Key
CROWZHDWIJEKAB-NVOIZEPQSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    1 mg

    $107

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    5 mg

    $266

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    Product Description

    Ac-VDVAD-CHO is an inhibitor of caspase-2, -3, and -7 (Kis = 3.5, 1, and 7.5 nM, respectively).1 It inhibits caspase-2 and -3 in cell-based assays with IC50 values of 1,334 and 346 nM, respectively.2 Ac-VDVAD-CHO (3 μM) inhibits increases in alkaline phosphatase and caspase-2 and -3 activity induced by human recombinant bone morphogenic protein 4 (BMP4) in MC3T3-E1 murine bone marrow stromal cells.3 It also inhibits BMP4-induced cell cycle arrest at the G0/G1 phase in MC3T3-E1 cells.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Talanian, R.V., Quinlan, C., Trautz, S., et al. Substrate specificities of caspase family proteases. The Journal of Biological Chemisty 272(15), 9677-9682 (1997).

    2. Maillard, M.C., Brookfield, F.A., Courtney, S.M., et al. Exploiting differences in caspase-2 and -3 S2 subsites for selectivity: Structure-based design, solid-phase synthesis and in vitro activity of novel substrate-based caspase-2 inhibitors. Bioorg. Med. Chem. 19(19), 5833-5851 (2011).

    3. Mogi, M., and Togari, A. Activation of caspases is required for osteoblastic differentiation. The Journal of Biological Chemisty 278(48), 47477-47482 (2003).