Product Name: Syntide-2 [PLARTLSVAGLPGKK]
Sequence One Letter Code: PLARTLSVAGLPGKK
Sequence Three Letter Code: H-Pro-Leu-Ala-Arg-Thr-Leu-Ser-Val-Ala-Gly-Leu-Pro-Gly-Lys-Lys-OH
Cas No: 108334-68-5
Chemical Formula:C68H122N20O18
Molecular Weight: 1507.9
Purity: 95%
Form: Lyophilized
Storage Conditions: - 20 °C
Research Area: Cancer Disease Research
SMILES: C[C@H]([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)O)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H]2CCCN2)O
IUPAC: (2S)-6-amino-2-[[(2S)-6-amino-2-[[2-[[(2S)-1-[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-5-(diaminomethylideneamino)-2-[[(2S)-2-[[(2S)-4-methyl-2-[[(2S)-pyrrolidine-2-carbonyl]amino]pentanoyl]amino]propanoyl]amino]pentanoyl]amino]-3-hydroxybutanoyl]amino]-4-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]-3-methylbutanoyl]amino]propanoyl]amino]acetyl]amino]-4-methylpentanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]hexanoyl]amino]hexanoic acid
INCHIKEY: NKBRRWBNPNUBDD-TYKVATLISA-N
INCHI:
InChI=1S/C68H122N20O18/c1-35(2)29-46(83-57(95)42-21-16-26-73-42)60(98)77-40(10)56(94)81-44(22-17-27-74-68(71)72)59(97)87-54(41(11)90)65(103)84-47(30-36(3)4)61(99)85-49(34-89)62(100)86-53(38(7)8)64(102)78-39(9)55(93)75-32-52(92)80-48(31-37(5)6)66(104)88-28-18-23-50(88)63(101)76-33-51(91)79-43(19-12-14-24-69)58(96)82-45(67(105)106)20-13-15-25-70/h35-50,53-54,73,89-90H,12-34,69-70H2,1-11H3,(H,75,93)(H,76,101)(H,77,98)(H,78,102)(H,79,91)(H,80,92)(H,81,94)(H,82,96)(H,83,95)(H,84,103)(H,85,99)(H,86,100)(H,87,97)(H,105,106)(H4,71,72,74)/t39-,40-,41+,42-,43-,44-,45-,46-,47-,48-,49-,50-,53-,54-/m0/s1
Conjugation: Unconjugated
Code Nacres: NA.26
Application: Syntide-2 [PLARTLSVAGLPGKK] is a synthetic peptide substrate extensively used for selective assessment of serine/threonine kinase activity. The sequence is efficiently phosphorylated by Ca²⁺/calmodulin-dependent protein kinase II (CaMK II) and protein kinase C (PKC), while exhibiting minimal cross-reactivity with other kinases. It is a poor substrate for phosphorylase kinase and is not effectively phosphorylated by myosin light chain kinase, enabling comparative specificity studies. Derived from a motif homologous to phosphorylation site 2 of glycogen synthase, Syntide-2 supports quantitative kinetic analysis, including Vmax/Km comparisons across kinase families. The peptide is widely applied in enzymology, intracellular signaling research, and kinase inhibitor screening platforms. Its defined phosphorylation profile makes it particularly useful for dissecting CaMK II– and PKC-dependent pathways in biochemical and cell-based assay systems.
Current Research: Syntide-2 [PLARTLSVAGLPGKK] is a synthetic peptide substrate widely used for selective evaluation of serine/threonine kinase activity in biochemical and cell-based assays. The sequence is efficiently phosphorylated by Ca²⁺/calmodulin-dependent protein kinase II (CaMK II) and protein kinase C (PKC), while demonstrating limited reactivity with several other kinases. This defined phosphorylation profile makes Syntide-2 a reliable tool for comparative kinase specificity studies, kinetic analysis, and inhibitor screening applications. Structural Basis and Kinase Recognition Syntide-2 is derived from a sequence motif homologous to phosphorylation site 2 of glycogen synthase, a well-characterized serine/threonine kinase target. The peptide contains a threonine residue within a favorable recognition context for CaMK II and PKC, including basic residues that support kinase docking and substrate positioning. CaMK II preferentially phosphorylates substrates containing basic amino acids proximal to the phosphorylation site, particularly within sequences influenced by Ca²⁺/calmodulin binding. PKC recognizes serine or threonine residues flanked by basic residues in similar contexts. The sequence of Syntide-2 satisfies these structural requirements, resulting in efficient phosphorylation by both kinase families. Importantly, Syntide-2 exhibits minimal phosphorylation by phosphorylase kinase and is not effectively phosphorylated by myosin light chain kinase (MLCK), supporting its utility in distinguishing kinase activity across related enzyme systems. Applications in CaMK II Research CaMK II is a multifunctional kinase central to calcium-dependent signaling in neuronal, cardiac, and skeletal muscle systems. It regulates synaptic plasticity, memory formation, excitation–contraction coupling, and gene expression. Syntide-2 is extensively used to measure CaMK II catalytic activity under defined Ca²⁺/calmodulin conditions. Applications include: Determination of CaMK II kinetic parameters (K_m and V_max) Assessment of autophosphorylation-dependent activation states Comparative analysis of CaMK II isoforms Evaluation of calcium signaling modulators Because CaMK II activity is tightly regulated by intracellular calcium flux, Syntide-2 provides a reproducible substrate for controlled enzymatic assays. Applications in PKC Signaling Studies Protein kinase C is a family of serine/threonine kinases activated by diacylglycerol (DAG), phospholipids, and, in some isoforms, Ca²⁺. PKC regulates diverse cellular processes including proliferation, apoptosis, migration, and receptor signaling. Syntide-2 supports quantitative evaluation of PKC activity across conventional and novel isoforms. In inhibitor development workflows, the peptide is used to determine IC₅₀ values and to characterize selectivity profiles of candidate PKC inhibitors. Enzyme Kinetics and Comparative Specificity Syntide-2 is particularly useful for kinetic comparisons across kinase families. Because it exhibits high catalytic efficiency (V_max/K_m) with CaMK II and PKC while remaining a poor substrate for certain other kinases, it provides a platform for: Cross-kinase specificity assessment Enzyme competition studies Structure–activity relationship (SAR) analysis Profiling of kinase-selective inhibitors The short and defined sequence reduces confounding effects of secondary or tertiary structure present in full-length protein substrates, improving assay reproducibility. Experimental Compatibility Syntide-2 is compatible with multiple detection platforms, including: Radiometric assays using [γ-³²P] ATP incorporation Fluorescence-based phosphorylation assays HPLC and mass spectrometry detection Coupled luminescent kinase assays Its consistent phosphorylation profile supports both purified enzyme assays and cell lysate-based kinase measurements. Research Impact By providing a selective and well-characterized substrate for CaMK II and PKC, Syntide-2 enables detailed investigation of calcium-dependent and DAG-dependent signaling pathways. It supports mechanistic enzymology studies, pharmacological inhibitor screening, and comparative kinase profiling in research areas ranging from neurobiology and cardiovascular physiology to cancer signaling. Overall, Syntide-2 [PLARTLSVAGLPGKK] serves as a versatile and reliable substrate for dissecting serine/threonine kinase activity and advancing understanding of intracellular phosphorylation networks.
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