Identification | Back Directory | [Name]
MALANTIDE | [CAS]
86555-35-3 | [Synonyms]
MALANTIDE RTKRSGSVYEPLKI RTLRSGSVYEPLKI Malantide, ≥97% (HPLC) Malantide, Protein Kinase Substrate MALANTIDE SYNTHETIC >97% CAMP-DEPENDENT PROTEI arg-thr-lys-arg-ser-gly-ser-val-tyr-*glu-pro-leu- ARG-THR-LYS-ARG-SER-GLY-SER-VAL-TYR-GLU- PRO-LEU-LY HIGH-AFFINITY CAMP DEPENDENT PROTEIN KINASE SUBSTRATE ARG-THR-LYS-ARG-SER-GLY-SER-VAL-TYR-GLU-PRO-LEU-LYS-ILE H-ARG-THR-LYS-ARG-SER-GLY-SER-VAL-TYR-GLU-PRO-LEU-LYS-ILE-OH High-Affinity cAMP Dependent Protein Kinase Substrate, Malantide L-Isoleucine,L-arginyl-L-threonyl-L-lysyl-L-arginyl-L-serylglycyl-L-seryl-L-valyl-L-tyrosyl-L-a-glutamyl-L-prolyl-L-leucyl-L-lysyl- L-Isoleucine, L-arginyl-L-threonyl-L-lysyl-L-arginyl-L-serylglycyl-L-seryl-L-valyl-L-tyrosyl-L-α-glutamyl-L-prolyl-L-leucyl-L-lysyl- L-Arginyl-L-threonyl-L-lysyl-L-arginyl-L-serylglycyl-L-seryl-L-valyl-L-tyrosyl-L-alpha-glutamyl-L-prolyl-L-leucyl-L-lysyl-L-isoleucine | [Molecular Formula]
C72H124N22O21 | [MDL Number]
MFCD00144718 | [MOL File]
86555-35-3.mol | [Molecular Weight]
1633.92 |
Chemical Properties | Back Directory | [density ]
1.46±0.1 g/cm3(Predicted) | [storage temp. ]
−20°C
| [solubility ]
H2O: 1 mg/mL
| [form ]
powder
| [pka]
3.38±0.10(Predicted) | [color ]
white
| [Sequence]
Arg-Thr-Lys-Arg-Ser-Gly-Ser-Val-Tyr-Glu-Pro-Leu-Lys-Ile |
Hazard Information | Back Directory | [Uses]
Malantide is a synthetic dodecapeptide derived from the site phosphorylated by cAMP-dependent protein kinase (PKA) on the β-subunit of phosphorylase kinase. Malantide is a highly specific substrate for PKA with a Km of 15 μM and shows protein inhibitor (PKI) inhibition >90% substrate phosphorylation in various rat tissue extracts[1]. Malantide is also an efficient substrate for PKC with a Km of 16 μM[2]. | [References]
[1] Murray KJ, et al. Use of a synthetic dodecapeptide (malantide) to measure the cyclic AMP-dependent protein kinase activity ratio in a variety of tissues. Biochem J. 1990 May 1;267(3):703-8. DOI:10.1042/bj2670703 [2] Z H Zhao, et al. Characterization of a New Substrate for Protein Kinase C: Assay by Continuous Fluorometric Monitoring and High Performance Liquid Chromatography. Biochem Biophys Res Commun. 1991 May 15;176(3):1454-61. DOI:10.1016/0006-291x(91)90450-l |
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