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Peptide Phosphorylation

Cellular phosphorylation is a modification that can change the activity, binding properties, or cellular localization of proteins or enzymes. It is also an important regulatory process that plays a critical role in many disease pathologies, including inflammation, cancer, neurological and metabolic disorders. Enzymes that phosphorylate proteins at specific amino acid residues (e.g., tyrosine, serine, and threonine) are called kinases. Enzymes that remove a phosphate group by hydrolysis are termed phosphatases. Because phosphorylation is central to most signal transduction pathways, phosphorylated peptides (i.e., phosphopeptides) are used for the analysis of protein kinases and phosphatases in may cellular assays.

phosphorylated custom peptide synthesis

CPC Scientific can synthesize phosphopeptides with specific residues (i.e., pSer, pTyr, pThr) phosphorylated in virtually any combination. While many of our phosphopeptides are synthesized as custom requests, we stock many common phosphorylated peptides as catalog items.

PHOSPHORYLATED CATALOG PEPTIDES
(SIGN-006) GS2, Glycogen Synthase Peptide-2Learn More »

H-Tyr-Arg-Arg-Ala-Ala-Val-Pro-Pro-Ser-Pro-Ser-Leu-Ser-Arg-His-Ser-Ser-Pro-His-Gln-pSer-Glu-Asp-Glu-Glu-Glu-OH

(PPEP-002) 2 CDC25C, CHK1 and CHK2 Substrate, phosphorylatedLearn More »

H-Lys-Lys-Lys-Val-Ser-Arg-Ser-Gly-Leu-Tyr-Arg-pSer-Pro-Ser-Met-Pro-Glu-Asn-Leu-Asn-Arg-Pro-Arg-NH2

(PPEP-001) [pS345]-Chk1Learn More »

H-Gln-Gly-Ile-Ser-Phe-pSer-Gln-Pro-Thr-Cys-OH

(HIST-078) AKT/PKB/Rac-Protein Kinase Substrate [ARKRERTY-pS-FGHHA], PhosphorylatedLearn More »

H-Ala-Arg-Lys-Arg-Glu-Arg-Thr-Tyr-pSer-Phe-Gly-His-His-Ala-OH

(HIST-056) [pSer28]-Histone H3 (21-44)Learn More »

H-Ala-Thr-Lys-Ala-Ala-Arg-Lys-pSer-Ala-Pro-Ser-Thr-Gly-Gly-Val-Lys-Lys-Pro-His-Arg-Tyr-Arg-Pro-Gly-OH

(HIST-009) [pSer42]-Histone H1 (29-59), Tetrahymena thermophilaLearn More »

H-Lys-Asp-Thr-Lys-Pro-Thr-Pro-Thr-Lys-Gly-Lys-Ala-Ala-pSer-Ala-Ser-Thr-Thr-Pro-Val-Lys-Lys-Asp-Val-Thr-Pro-Val-Lys-Ala-Asp-Thr-OH

(HIST-023) [pSer10]-Histone H3 (1-15); H3pS10Learn More »

H-Ala-Arg-Thr-Lys-Gln-Thr-Ala-Arg-Lys-pSer-Thr-Gly-Gly-Lys-Ala-OH

(HIST-080) CDK5 Substrate [PK-pT-PKKAKKL], PhosphorylatedLearn More »

H-Pro-Lys-pThr-Pro-Lys-Lys-Ala-Lys-Lys-Leu-OH

mono-dispersed PEGlyated Custom Peptides

Cyclo(-Asp-Glu-Tyr(PO4H2)-Leu-Asp-Pro-D-Phe-Lys-).
Leone, Marilisa, et al. "Design and NMR Studies of Cyclic Peptides Targeting the N-Terminal Domain of the Protein Tyrosine Phosphatase YopH." Chemical Biology & Drug Design 77.1 (2011): 12-19.

Phosphorylated Custom Peptide Citations

"The peptides TH-(1-43) (MPTPDATTPQAKGFRRAVSELDAKQAEAIMSPRFIGRRQSLIE) and THp-(1-43) (MPTPDATTPQAKGFRRAVS(PO3)2-ELDAKQAEAIMSPRFIGRRQSLIE) were synthesized by CPC Scientific (San Jose, CA) at approximately 90% purity, as seen by mass spectroscopy, and used without further purification."

1. Skjevik, Åge Aleksander, et al. "The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes." Journal of Molecular Biology 426.1 (2014): 150-168.Learn More »

"Two peptides of the polyserine tract of AmVg and NvVg were synthesized by CPC Scientific (Sunnyvale, CA, USA) for NMR analysis. The synthesis was performed after isotope-labeling expression attempts in Escherichia coli were deemed unsuitable for the project because of the very low final yield. Synthesis of serine repeats is hampered by the steric conflicts caused by the chemical group used to protect the side-chains from chemical modification during synthesis. In order to make synthesis of serine repeats feasible and aid assignment, one serine residue was mutated into a residue of similar properties in each peptide. The peptides had the following sequences: AmVg (residues 358–392): EKLKQDILNLRTDISTS(Sp)SS(15I)SSSEENDFWQPKPT AmVg (residues 336–385): R(15V)SKT(15A)MNSNQI(15V)SDNS(15L)(15S)STEEK(15L)KQDI(15L)N(15L)RTDI(15S)S(15S)(Sp)S(15A)IS (15S)(15S)EEND. NvVg (residues 351–385): EHKHSDESTSE(Sp)FES(15I)ADNNDDSYFQRKPKLTEAP NvVg (residues 335–372): RPNK(15L)N(15L)QRRHDHKS(15G)EHKHSDE(15S)S(15S)E(Sp)FE(15A)I(15A)DNNDD."

2. Havukainen, Heli, et al. "A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation." The Journal of Experimental Biology 215.11 (2012): 1837-1846.Learn More »

"The peptides TH-(1-43), i.e. MPTPDATTPQAKGFRRAVSELDAKQAEAIMSPRFIGRRQSLIE, and its Ser19-phosphorylated counterpart THp-(1-43), i.e. MPTPDATTPQAKGFRRAVS(PO3)ELDAKQAEAIMSPRFIGRRQSLIE, were synthesized by CPC Scientific (San Jose, CA, USA) at approx. 90% purity, as seen by mass spectroscopy."

3. Bustad, Helene J., et al. "The peripheral binding of 14-3-3γ to membranes involves isoform-specific histidine residues." PloS One 7.11 (2012): e49671.Learn More »

"Cyclo-DEYDDPfK; Cyclo-DE(pY)LDPfK; Cyclo-DE(FCOOH)LDPfK (FCOOH= phenylalanine with a carboxyl group at the para position) were purchased either from the MCW facility of the Wisconsin Medical College or from CPC Scientific (San José, CA, USA)"

4. Leone, Marilisa, et al. "Design and NMR Studies of Cyclic Peptides Targeting the N-Terminal Domain of the Protein Tyrosine Phosphatase YopH." Chemical Biology & Drug Design 77.1 (2011): 12-19.Learn More »

"PRMT5pT634 (Biotin-SAIHNPTGRSYpTIGL-COOH, where pT represents phosphothreonine), PGHS2 (Biotin-SGSGVLIKRRSTEL-COOH),PGHS2pT602 (Biotin-SGSGVLIKRRSpTEL-COOH), IRK1 (Biotin-SGSGPRPLRRESEI-COOH), IRK1pS425 (BiotinSGSGPRPLRREpSEI-COOH, where pS represents phosphoserine), ERBB4 (Biotin-GTVLPPPPYRHRNTVV-COOH), and ERBB4pT1306 (Biotin-GTVLPPPPYRHRNpTVV-COOH)) and by CPC Scientific, Inc. (E6 (HPV16) (Biotin-RSSRTRRETQLCOOH) and E6 (HPV16)pT156 (Biotin-RSSRTRREpTQLCOOH))."

5. Espejo, Alexsandra B., et al. "PRMT5 C-terminal Phosphorylation Modulates a 14-3-3/PDZ Interaction Switch." Journal of Biological Chemistry 292.6 (2017): 2255-2265.Learn More »

"Phosphopeptide LPISASHpSpSKTR was synthesized by CPC Scientific (San Jose, CA, USA). Both peptides were diluted to a concentration of 20 μM in 49/49/2 (vol/vol/vol) methanol/water/ammonium hydroxide solution."

6. Crizer, David M., Yu Xia, and Scott A. McLuckey. "Transition metal complex cations as reagents for gas-phase transformation of multiply deprotonated polypeptides." Journal of the American Society for Mass Spectrometry 20.9 (2009): 1718-1722.Learn More »

"The peptides P20A (Ac-AAASGINAEWPLWPGEAGWGRLEGRRTYEAEI-NH 2 ) andbiotin-P20A (biotin-PEG4-AAASGINAEWPLWPGEAGWGRLEGRRTYEAEI-NH2 ) were synthesized by CPC Scientific."

7. Fu, Shushu, et al. "P20A inhibits HIV-1 fusion through its electrostatic interaction with the distal region of the gp41 fusion core." Microbes and Infection 17.9 (2015): 665-670.Learn More »