pep2-SVKE

pep2-SVKE is inactive control peptide analog of pep2-SVKI, and an inhibitor peptide that corresponds the C-terminus of the GluA2 AMPA receptor subunit.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R0835

CAS No:1315378-76-7

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cGMP Peptide
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M.F/Formula
C59H89N13O20
M.W/Mr.
1300.43
Sequence
YNVYGIESVKE
Labeling Target
AMPA receptor
Appearance
White lyophilised solid
Purity
>98 %
Activity
Inhibitor

pep2-SVKE is a synthetic peptide compound designed to facilitate advanced research in the fields of molecular biology, biochemistry, and peptide-based functional studies. As a sequence-defined peptide, it serves as a valuable tool for investigating specific protein-protein interactions, signaling pathways, and structural motifs relevant to cellular processes. The defined amino acid sequence of pep2-SVKE enables precise modulation and interrogation of biological systems, making it an asset for researchers exploring the mechanistic underpinnings of peptide-mediated events. Its utility extends to a range of experimental contexts where synthetic peptides are required for probing biochemical phenomena or for use as reference materials in analytical and assay development.

Peptide-protein interaction studies: In the context of molecular interaction research, pep2-SVKE can be used to elucidate the binding dynamics between peptides and their target proteins. By serving as a model ligand or interaction motif, it enables detailed characterization of affinity, specificity, and kinetic parameters in binding assays such as surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), or co-immunoprecipitation. Such studies provide critical insight into the molecular determinants of recognition and signaling, supporting the development of novel modulators or inhibitors for research applications.

Signal transduction pathway analysis: Synthetic peptides like pep2-SVKE are frequently employed to dissect cellular signaling pathways, particularly when investigating the role of short linear motifs in post-translational modification or protein recruitment. Researchers can introduce this peptide into cell-based or in vitro systems to mimic, compete with, or inhibit endogenous interactions, thereby clarifying the contribution of specific sequence motifs to downstream signaling events. This approach is instrumental in mapping pathway architecture and identifying potential regulatory nodes within complex biological networks.

Peptide mapping and epitope characterization: The defined structure of pep2-SVKE makes it suitable for use in peptide mapping experiments, where it can function as a reference or probe to localize functional domains within larger protein sequences. In immunological studies, it may be utilized to identify and characterize linear epitopes recognized by antibodies, facilitating the development of peptide-specific detection reagents or the refinement of immunoassays. Such applications are essential for advancing both basic research and the creation of diagnostic tools.

Analytical method development: As a well-characterized synthetic peptide, pep2-SVKE is valuable in the optimization and validation of analytical techniques, including high-performance liquid chromatography (HPLC), mass spectrometry (MS), and capillary electrophoresis. Its defined sequence and physicochemical properties allow it to serve as a calibration standard, internal control, or system suitability marker, ensuring the accuracy and reproducibility of peptide quantification and identification in complex biological samples.

Peptide synthesis and process optimization: The use of pep2-SVKE extends to the evaluation and refinement of solid-phase peptide synthesis (SPPS) protocols. Its synthesis can be employed as a benchmark for assessing coupling efficiency, deprotection strategies, and purification workflows. By monitoring the yield and purity of this model peptide, researchers can optimize synthetic methodologies, troubleshoot process bottlenecks, and improve scalability for the production of other custom peptides. This contributes to enhanced reproducibility and efficiency in peptide chemistry laboratories.

Solubility
-20 °C
InChI
InChI=1S/C59H89N13O20/c1-7-31(6)49(58(90)65-38(19-21-45(78)79)53(85)69-42(28-73)55(87)72-47(29(2)3)56(88)64-37(10-8-9-23-60)52(84)66-39(59(91)92)20-22-46(80)81)70-44(77)27-63-51(83)40(25-33-13-17-35(75)18-14-33)68-57(89)48(30(4)5)71-54(86)41(26-43(62)76)67-50(82)36(61)24-32-11-15-34(74)16-12-32/h11-18,29-31,36-42,47-49,73-75H,7-10,19-28,60-61H2,1-6H3,(H2,62,76)(H,63,83)(H,64,88)(H,65,90)(H,66,84)(H,67,82)(H,68,89)(H,69,85)(H,70,77)(H,71,86)(H,72,87)(H,78,79)(H,80,81)(H,91,92)/t31-,36-,37-,38-,39-,40-,41-,42-,47-,48-,49-/m0/s1
InChI Key
AHURAWWDQDDHNP-OIKDQGPWSA-N
Isomeric SMILES
CC[C@H](C)[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC(=O)CNC(=O)[C@H](CC1=CC=C(C=C1)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CC2=CC=C(C=C2)O)N

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