An optimal Cdk2 peptide substrate
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Product Categories

Product Type

Biochemicals
Peptides

Research Area

Cell Biology
Cell Cycle
Cell Signaling

Application

Enzyme Activity

Cdk2 Peptide Substrate (trifluoroacetate salt)

Item No. 44656

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
L-histidyl-L-histidyl-L-alanyl-L-seryl-L-prolyl-L-arginyl-L-lysine, trifluoroacetate salt
Synonyms
  • Cyclin-dependent Kinase 2 Peptide Substrate
  • His-His-Ala-Ser-Pro-Arg-Lys-OH
Molecular Formula
C35H57N15O9 • XCF3COOH
Formula Weight
831.9
Purity
≥90%
Formulation (Request formulation change)
A solid
Peptide Sequence
HHASPRK-OH
Solubility(Learn about Variance in Solubility)
PBS (7.2 pH): Soluble: ≥ 10 mg/ml
SMILES
N[C@@H](CC1=CN=CN1)C(N[C@@H](CC2=CN=CN2)C(N[C@@H](C)C(N[C@@H](CO)C(N3[C@@H](CCC3)C(N[C@@H](CCCNC(N)=N)C(N[C@H](C(O)=O)CCCCN)=O)=O)=O)=O)=O)=O.O=C(O)C(F)(F)F
InChi Code
InChI=1S/C35H57N15O9.C2HF3O2/c1-19(45-31(55)25(13-21-15-41-18-44-21)48-29(53)22(37)12-20-14-40-17-43-20)28(52)49-26(16-51)33(57)50-11-5-8-27(50)32(56)46-23(7-4-10-42-35(38)39)30(54)47-24(34(58)59)6-2-3-9-36;3-2(4,5)1(6)7/h14-15,17-19,22-27,51H,2-13,16,36-37H2,1H3,(H,40,43)(H,41,44)(H,45,55)(H,46,56)(H,47,54)(H,48,53)(H,49,52)(H,58,59)(H4,38,39,42);(H,6,7)/t19-,22-,23-,24-,25-,26-,27-;/m0./s1
InChi Key
XPYANGMZUXKVJO-FWYIDSEUSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    5 mg

    $32

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    10 mg

    $58

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    25 mg

    $112

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    Product Description

    Cdk2 peptide substrate is an optimal peptide substrate of Cdk2.1 It binds across the Cdk2 catalytic site when in complex with Cdk2 phosphorylated at T160 and cyclin A3. Cdk2 peptide substrate has been used in enzyme assays for Cdk2 activity.2,3

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Brown, N.R., Noble, M.E., Endicott, J.A., et al. The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nat. Cell. Biol. 1(7), 438-443 (1999).

    2. Anscombe, E., Meschini, E., Mora-Vidal, R., et al. Identification and characterization of an irreversible inhibitor of CDK2. Chem. Biol. 22(9), 1159-1164 (2015).

    3. Song, K., Liu, X., Huang, W., et al. Improved method for the identification and validation of allosteric sites. J. Chem. Inf. Model 57(9), 2358-2363 (2017).