GYPGKF-NH2, Agonist of PAR4, CAS No.rp174187, Agonist of PAR4

CAS: rp174187 Cat. No.: rp174187

GRADE & PURITY Moligand™

Specifications

Product Name

GYPGKF-NH2, Agonist of PAR4, CAS No.rp174187

Grau

Moligand™

Especificações e pureza

Moligand™

Tipo de ação

AGONIST

Mecanismo de ação

Agonist of PAR4

CAS

rp174187

Tipo de molécula

Peptide

Product Line

Produtos biológicos

Armazenamento e envio

Condições de armazenamento de armazenamento

Room temperature

Alvos associados (humanos)

F2RL3 Tchem Proteinase-activated receptor 4 (0 Activities)

Discover Target: F2RL3

Activity Type	Activity Value -log(M)	Mechanism of Action	Activity Reference	Publications (PubMed IDs)

Informação genética

• Reference:
  • 1. Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration., The Journal of biological chemistry, Steegborn, C C and 7 more authors.
  • 2. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences., Proceedings of the National Academy of Sciences of the United States of America, Strausberg, Robert L RL and 83 more authors.
  • 3. Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine gamma-lyase (CTH)., Human genetics, Wang, Jian J and Hegele, Robert A RA.
  • 4. Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase., Biochemical and biophysical research communications, Lu, Y Y, O'Dowd, B F BF, Orrego, H H and Israel, Y Y.
  • 5. Single nucleotide polymorphism in CTH associated with variation in plasma homocysteine concentration., Clinical genetics, Wang, J J, Huff, A M AM, Spence, J D JD and Hegele, R A RA.
  • 6. Cystathionine gamma-lyase overexpression inhibits cell proliferation via a H2S-dependent modulation of ERK1/2 phosphorylation and p21Cip/WAK-1., The Journal of biological chemistry, Yang, Guangdong G, Cao, Kun K, Wu, Lingyun L and Wang, Rui R.
  • 7. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)., Genome research, Gerhard, Daniela S DS and 115 more authors.
  • 8. Towards a proteome-scale map of the human protein-protein interaction network., Nature, Rual, Jean-François JF and 37 more authors.
  • 9. The DNA sequence and biological annotation of human chromosome 1., Nature, Gregory, S G SG and 178 more authors.
  • 10. Polymorphisms in one-carbon metabolism and trans-sulfuration pathway genes and susceptibility to bladder cancer., International journal of cancer, Moore, Lee E LE and 14 more authors. more
  • 11. Toward a confocal subcellular atlas of the human proteome., Molecular & cellular proteomics : MCP, Barbe, Laurent L and 10 more authors.
  • 12. Kinetic properties of polymorphic variants and pathogenic mutants in human cystathionine gamma-lyase., Biochemistry, Zhu, Weidong W, Lin, Alexander A and Banerjee, Ruma R.
  • 13. Pathway-based evaluation of 380 candidate genes and lung cancer susceptibility suggests the importance of the cell cycle pathway., Carcinogenesis, Hosgood, H Dean HD and 12 more authors.
  • 14. Relationship between cystathionine gamma-lyase gene polymorphism and essential hypertension in Northern Chinese Han population., Chinese medical journal, Li, Yun Y and 8 more authors.
  • 15. Active cystathionine beta-synthase can be expressed in heme-free systems in the presence of metal-substituted porphyrins or a chemical chaperone., The Journal of biological chemistry, Majtan, Tomas T, Singh, Laishram R LR, Wang, Liqun L, Kruger, Warren D WD and Kraus, Jan P JP.
  • 16. MALDI-TOF MS genotyping of polymorphisms related to 1-carbon metabolism using common and mass-modified terminators., Clinical chemistry, Meyer, Klaus K, Fredriksen, Ase A and Ueland, Per Magne PM.
  • 17. Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S., The Journal of biological chemistry, Sun, Qingxiang Q and 10 more authors.
  • 18. Oral facial clefts and gene polymorphisms in metabolism of folate/one-carbon and vitamin A: a pathway-wide association study., Genetic epidemiology, Boyles, Abee L AL and 16 more authors.
  • 19. Large-scale proteomics and phosphoproteomics of urinary exosomes., Journal of the American Society of Nephrology : JASN, Gonzales, Patricia A PA and 7 more authors.
  • 20. An association study of 45 folate-related genes in spina bifida: Involvement of cubilin (CUBN) and tRNA aspartic acid methyltransferase 1 (TRDMT1)., Birth defects research. Part A, Clinical and molecular teratology, Franke, Barbara B and 7 more authors.
  • 21. Polymorphisms in innate immunity genes and lung cancer risk in Xuanwei, China., Environmental and molecular mutagenesis, Shen, Min M and 12 more authors.
  • 22. H2S biogenesis by human cystathionine gamma-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia., The Journal of biological chemistry, Chiku, Taurai T and 5 more authors.
  • 23. Variations in folate pathway genes are associated with unexplained female infertility., Fertility and sterility, Altmäe, Signe S and 7 more authors.
  • 24. Bile-acid-activated farnesoid X receptor regulates hydrogen sulfide production and hepatic microcirculation., World journal of gastroenterology, Renga, Barbara B, Mencarelli, Andrea A, Migliorati, Marco M, Distrutti, Eleonora E and Fiorucci, Stefano S.
  • 25. Cystathionine gamma-lyase: Clinical, metabolic, genetic, and structural studies., Molecular genetics and metabolism, Kraus, Jan P JP and 14 more authors.
  • 26. Relative contributions of cystathionine beta-synthase and gamma-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions., The Journal of biological chemistry, Singh, Sangita S, Padovani, Dominique D, Leslie, Rachel A RA, Chiku, Taurai T and Banerjee, Ruma R.
  • 27. PTEN identified as important risk factor of chronic obstructive pulmonary disease., Respiratory medicine, Hosgood, H Dean HD, Menashe, Idan I, He, Xingzhou X, Chanock, Stephen S and Lan, Qing Q.
  • 28. Genetic susceptibility to distinct bladder cancer subphenotypes., European urology, Guey, Lin T LT and 18 more authors.
  • 29. Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip., American journal of human genetics, Talmud, Philippa J PJ and 38 more authors.
  • 30. Integrative predictive model of coronary artery calcification in atherosclerosis., Circulation, McGeachie, Michael M and 13 more authors.
  • 31. Cystathionine beta-synthase 844Ins68 polymorphism is not associated with the levels of homocysteine and cysteine in an Indian population., Biomarkers : biochemical indicators of exposure, response, and susceptibility to chemicals, Kumar, Jitender J, Garg, Gaurav G, Karthikeyan, Ganesan G and Sengupta, Shantanu S.
  • 32. The expression and activity of cystathionine-γ-lyase and 3-mercaptopyruvate sulfurtransferase in human neoplastic cell lines., Amino acids, Jurkowska, Halina H, Placha, Wojciech W, Nagahara, Noriuki N and Wróbel, Maria M.
  • 33. Ancient origin of the CTH alelle carrying the c.200C>T (p.T67I) variant in patients with cystathioninuria., Clinical genetics, Espinós, C C and 8 more authors.
  • 34. Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study., Diabetes care, Bailey, Swneke D SD and 11 more authors.
  • 35. Maternal genes and facial clefts in offspring: a comprehensive search for genetic associations in two population-based cleft studies from Scandinavia., PloS one, Jugessur, Astanand A and 12 more authors.
  • 36. [Expression of cystathionine-γ-lyase/hydrogen sulfide pathway in CVB3-induced myocarditis in mice]., Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics, Hua, Wang W and 6 more authors.
  • 37. Folate-metabolizing gene variants and pregnancy outcome of IVF., Reproductive biomedicine online, Laanpere, M M and 5 more authors.
  • 38. Specificity protein-1 as a critical regulator of human cystathionine gamma-lyase in smooth muscle cells., The Journal of biological chemistry, Yang, Guangdong G, Pei, Yanxi Y, Teng, Huajian H, Cao, Qiuhui Q and Wang, Rui R.
  • 39. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium., Briefings in bioinformatics, Gaudet, Pascale P, Livstone, Michael S MS, Lewis, Suzanna E SE and Thomas, Paul D PD.
  • 40. Expression of cystathionine β-synthase and cystathionine γ-lyase in human pregnant myometrium and their roles in the control of uterine contractility., PloS one, You, Xing-Ji XJ and 8 more authors.
  • 41. MicroRNA-21 represses human cystathionine gamma-lyase expression by targeting at specificity protein-1 in smooth muscle cells., Journal of cellular physiology, Yang, Guangdong G, Pei, Yanxi Y, Cao, Qiuhui Q and Wang, Rui R.
  • 42. H2S-Induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response., Science signaling, Krishnan, Navasona N, Fu, Cexiong C, Pappin, Darryl J DJ and Tonks, Nicholas K NK.
  • 43. Characterization of hydrogen sulfide and its synthases, cystathionine β-synthase and cystathionine γ-lyase, in human prostatic tissue and cells., Urology, Guo, Hui H and 5 more authors.
  • 44. Sp1 is involved in regulation of cystathionine γ-lyase gene expression and biological function by PI3K/Akt pathway in human hepatocellular carcinoma cell lines., Cellular signalling, Yin, Peng P and 12 more authors.
  • 45. H₂S protects against pressure overload-induced heart failure via upregulation of endothelial nitric oxide synthase., Circulation, Kondo, Kazuhisa K and 14 more authors.
  • 46. Reduced cystathionine γ-lyase and increased miR-21 expression are associated with increased vascular resistance in growth-restricted pregnancies: hydrogen sulfide as a placental vasodilator., The American journal of pathology, Cindrova-Davies, Tereza T and 5 more authors.
  • 47. Dysregulation of hydrogen sulfide producing enzyme cystathionine γ-lyase contributes to maternal hypertension and placental abnormalities in preeclampsia., Circulation, Wang, Keqing K and 14 more authors.
  • 48. Regulation of cystathionine γ-lyase in mammalian cells by hypoxia., Biochemical genetics, Wang, Maoxian M, Guo, Zhanyun Z and Wang, Shilong S.
  • 49. A genome-wide association study of chemotherapy-induced alopecia in breast cancer patients., Breast cancer research : BCR, Chung, Suyoun S and 6 more authors.
  • 50. [Cystathionine γ-lyase]., Postepy higieny i medycyny doswiadczalnej (Online), Jurkowska, Halina H, Kaczor-Kamińska, Marta M, Bronowicka-Adamska, Patrycja P and Wróbel, Maria M.
  • 51. Decreased cystathionine-γ-lyase (CSE) activity in livers of type 1 diabetic rats and peripheral blood mononuclear cells (PBMC) of type 1 diabetic patients., The Journal of biological chemistry, Manna, Prasenjit P, Gungor, Neslihan N, McVie, Robert R and Jain, Sushil K SK.
  • 52. Hydrogen sulfide (H2S)/cystathionine γ-lyase (CSE) pathway contributes to the proliferation of hepatoma cells., Mutation research, Pan, Yan Y and 5 more authors.
  • 53. The cystathionine γ-lyase/hydrogen sulfide system maintains cellular glutathione status., The Biochemical journal, Lee, Zheng-Wei ZW, Low, Yi-Lian YL, Huang, Shufen S, Wang, Tianxiao T and Deng, Lih-Wen LW.
  • 54. The binding site for the transcription factor, NF-κB, on the cystathionine γ-lyase promoter is critical for LPS-induced cystathionine γ-lyase expression., International journal of molecular medicine, Wang, Maoxian M, Guo, Zhanyun Z and Wang, Shilong S.
  • 55. Regulation of cystathionine gamma-lyase/H₂S system and its pathological implication., Frontiers in bioscience (Landmark edition), Zhao, Kexin K, Li, Hongzhu H, Li, Shuangshuang S and Yang, Guangdong G.
  • 56. Dysregulation of hydrogen sulphide metabolism impairs oviductal transport of embryos., Nature communications, Ning, Nannan N and 5 more authors.
  • 57. Wnt/β-catenin signaling induces the transcription of cystathionine-γ-lyase, a stimulator of tumor in colon cancer., Cellular signalling, Fan, Kun K and 7 more authors.
  • 58. miRNA-30 family inhibition protects against cardiac ischemic injury by regulating cystathionine-γ-lyase expression., Antioxidants & redox signaling, Shen, Yaqi Y and 7 more authors.
  • 59. Role of the cystathionine γ lyase/hydrogen sulfide pathway in human melanoma progression., Pigment cell & melanoma research, Panza, Elisabetta E and 11 more authors.
  • 60. A proteome-scale map of the human interactome network., Cell, Rolland, Thomas T and 69 more authors.
  • 61. Neurodegeneration in Huntington's disease involves loss of cystathionine γ-lyase., Cell cycle (Georgetown, Tex.), Paul, Bindu D BD and Snyder, Solomon H SH.
  • 62. The importance of MTHFR, MTR, MTRR and CSE expression levels in Caucasian women with preeclampsia., European journal of obstetrics, gynecology, and reproductive biology, Seremak-Mrozikiewicz, Agnieszka A and 6 more authors.
  • 63. The importance of rs1021737 and rs482843 polymorphisms of cystathionine gamma-lyase in the etiology of preeclampsia in the Caucasian population., Ginekologia polska, Mrozikiewicz, Przemysław M PM and 8 more authors.
  • 64. Cystathionine γ-lyase, a H2S-generating enzyme, is a GPBAR1-regulated gene and contributes to vasodilation caused by secondary bile acids., American journal of physiology. Heart and circulatory physiology, Renga, Barbara B and 9 more authors.
  • 65. Correlation between the cystathionine-γ-lyase (CES) and the severity of peptic ulcer disease., African health sciences, Chen, Xiong X, Wan, Ying-Chun YC, Guo, Tao T, Xu, Can-Xia CX and Wang, Fen F.
  • 66. MPST but not CSE is the primary regulator of hydrogen sulfide production and function in the coronary artery., American journal of physiology. Heart and circulatory physiology, Kuo, Maggie M MM and 10 more authors.
  • 67. Transcriptional Regulation of Cystathionine-γ-Lyase in Endothelial Cells by NADPH Oxidase 4-Dependent Signaling., The Journal of biological chemistry, Mistry, Rajesh K RK and 8 more authors.
  • 68. LPS Up-Regulates Cystathionine γ -Lyase Gene Expression in Primary Human Macrophages via NF-κB/ERK Pathway., Inflammation & allergy drug targets, Badiei, Alireza A, Gieseg, Steven S, Davies, Sian S, Izani Othman, Mohd M and Bhatia, Madhav M.
  • 69. Radiation Exposure Promotes Hepatocarcinoma Cell Invasion through Epithelial Mesenchymal Transition Mediated by H2S/CSE Pathway., Radiation research, Pan, Yan Y, Zhou, Cuiping C, Yuan, Dexiao D, Zhang, Jianghong J and Shao, Chunlin C.
  • 70. Cystathionine γ-lyase(CSE)/hydrogen sulfide system is regulated by miR-216a and influences cholesterol efflux in macrophages via the PI3K/AKT/ABCA1 pathway., Biochemical and biophysical research communications, Gong, Duo D and 15 more authors.
  • 71. MicroRNA-186 promotes macrophage lipid accumulation and secretion of pro-inflammatory cytokines by targeting cystathionine γ-lyase in THP-1 macrophages., Atherosclerosis, Yao, Yan Y and 9 more authors.
  • 72. Cystathionine γ-lyase is expressed in human atherosclerotic plaque microvessels and is involved in micro-angiogenesis., Scientific reports, van den Born, J C JC and 5 more authors.
  • 73. Dichotomous effects of isomeric secondary amines containing an aromatic nitrile and nitro group on human aortic smooth muscle cells via inhibition of cystathionine-γ-lyase., Biochimie, Ji, Yajing Y and 6 more authors.
  • 74. Distinctive expression pattern of cystathionine-β-synthase and cystathionine-γ-lyase identifies mesenchymal stromal cells transition to mineralizing osteoblasts., Journal of cellular physiology, Gambari, Laura L and 6 more authors.
  • 75. Age-Dependent Allergic Asthma Development and Cystathionine Gamma-Lyase Deficiency., Antioxidants & redox signaling, Wang, Peipei P and 6 more authors.
  • 76. Augmented H2S production via cystathionine-beta-synthase upregulation plays a role in pregnancy-associated uterine vasodilation., Biology of reproduction, Sheibani, Lili L and 7 more authors.
  • 77. Total sulfane sulfur bioavailability reflects ethnic and gender disparities in cardiovascular disease., Redox biology, Rajpal, Saurabh S and 12 more authors.
  • 78. Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides., Gene, Maruyama, K K and Sugano, S S.

Application Protocols

No tested application list is provided for this item. The following general protocols can guide first‑use in common assay types; optimize per your system.

1. Stock solution preparation

• Bring vial to room temperature in a desiccated environment. Briefly centrifuge to collect material. Dissolve in water or buffer to 1–10 mM. If insoluble, pre‑wet with DMSO (5–20% v/v of final volume), then dilute with buffer. Filter sterilize if needed (0.22 µm, low‑binding).

2. Binding assay by fluorescence anisotropy (literature‑style)

• Label a fraction of the peptide (e.g., N‑terminal fluorophore via NHS chemistry) and keep this product as the unlabeled competitor. Titrate protein against a fixed labeled‑peptide concentration at 20–25°C. Record anisotropy changes; determine KD by fitting to a one‑site model. Include controls with this unlabeled peptide to confirm specificity.

3. Enzyme profiling with LC‑MS readout

• Incubate peptide (10–200 µM) with enzyme/preparation in appropriate buffer (e.g., 50 mM HEPES, pH 7.5, 100 mM NaCl) at 25–37°C. Quench at timepoints with acidified acetonitrile. Analyze by LC‑MS to detect intact peptide and fragments.

4. Cell treatment (exploratory, in vitro only)

• Prepare sterile aqueous stocks. Verify compatibility with serum and DMSO limits. Start at low micromolar concentrations, monitor cytotoxicity independently. No claims of bioactivity are made.

Note: These are general templates. Validate conditions and concentrations for your specific target and readout.

Biological Roles

No specific biological target or endogenous role is assigned to GYPGKF‑NH2 in the Product Data. The following are general considerations for this peptide composition.

• Structural motifs:
  • The Y–P motif can favor a β‑turn or induce local rigidity due to proline’s conformational constraints (literature observation). This can influence binding epitopes in PPIs.
  • Aromatic residues (Tyr, Phe) contribute to π–π and cation–π interactions; Lys provides a positive charge for electrostatic contacts with acidic surfaces.
• Spectroscopic utility:
  • Tyrosine enables intrinsic UV absorbance near 275–280 nm and weak fluorescence (literature), which can be leveraged for concentration determination and binding studies without extrinsic labels.
• Enzymology context (general):
  • Short peptides are frequently used as surrogate substrates or inhibitors to profile peptidase or recognition domain specificity. The C‑terminal amide mimics an internal peptide bond environment.
• Physicochemical behavior in biology:
  • The presence of Lys (basic) and two aromatics yields amphipathic character; overall behavior (cellular uptake, aggregation) is sequence‑ and environment‑dependent.

Important: The product is designated for research use only and is not intended for diagnostic, therapeutic, or clinical use. Any biological effects must be established empirically in the user’s system; no claims of activity, potency, or target selectivity are made here.

Buffer Applications

This item is a peptide ligand, not a buffering reagent. It is not typically used to establish or maintain pH in biochemical systems.

Practical notes related to buffers (user guidance):

• Stock preparation: Dissolve initially in water or a compatible buffer (e.g., PBS, HEPES). If solubility is limited, pre‑wet with a small volume of DMSO, then dilute into buffer with gentle mixing.
• pH considerations: Begin near neutral to mildly acidic pH to protect tyrosine from oxidation; adjust pH only after complete dissolution. Avoid strong bases for initial solubilization.
• Ionic strength: Moderate salt (e.g., 100–150 mM NaCl) can suppress non‑specific adsorption in binding assays.
• Filtration: For sterile applications, use 0.22 µm low‑protein‑binding filters.

If you require a buffering system for experiments involving this peptide, consider standard biological buffers (e.g., phosphate pH 6–8, HEPES pH 6.8–8.2, citrate pH 3–6). Recipes and exact pH ranges should be selected based on the biology of the assay components.

Green Alternatives

As a peptide analyte/ligand, the “greenness” considerations center on solvent choices for dissolution, assay media, and purification rather than replacement of the molecule itself.

Greener choices and trade‑offs (general guidance):

• Water-based dissolution
  • Pros: Non‑toxic, inexpensive, minimal environmental impact; suitable buffers (PBS, HEPES) provide physiological ionic strength.
  • Cons: May be limited by hydrophobic residues (Tyr, Phe) that reduce aqueous solubility; may require pH adjustment.
• Minimal DMSO co‑solvent
  • Pros: Excellent solubilizing power for challenging sequences; compatible with many assays at ≤0.5–1% v/v.
  • Cons: DMSO is a dipolar aprotic with environmental persistence concerns; can interfere with some biochemical assays.
• Ethanol as an alternative co‑solvent
  • Pros: Biobased availability, readily biodegradable.
  • Cons: Often a poorer peptide solvent than DMSO/DMF; may denature proteins in downstream assays at low percentages.

Comparison snapshot (literature-based):

• Water/buffer: First-line choice for this sequence due to lysine and C‑terminal amide; attempt dissolution with mild acidification before resorting to organics.
• DMSO vs DMF: DMSO is generally preferred for biological assays; DMF is effective but less favored for bioassays due to toxicity/handling.

Operational green tips:

• Prepare concentrated stocks to minimize solvent volume; use glass vials to reduce plastic waste.
• Avoid repeated freeze–thaw by aliquoting to prevent degradation and waste.
• Use aqueous mobile phases with volatile modifiers for LC‑MS (e.g., water/acetonitrile with formic acid) to reduce halogenated solvent use where possible.

Pharmaceutical Uses

No pharmacopeial status, excipient role, or manufacturing use is provided for this item. It is supplied strictly for research use only.

Context and boundaries:

• Not for human or veterinary use. Do not use in clinical diagnostics, therapeutic formulations, or as an API/excipient in drug products.
• Formulation notes for research: In preclinical research settings, peptides like GYPGKF‑NH2 may be formulated into simple aqueous buffers for in vitro testing, or complexed with carriers for delivery studies. Such uses are strictly non‑clinical and require user validation of sterility, endotoxin levels, and stability; none of these parameters are specified for this item.
• Regulatory: No claims of GMP manufacture or compliance with pharmacopeial monographs (USP/EP/JP) are made. For any translational work, independent qualification and vendor audits are necessary.

Please refer to the CoA/Spec Sheet for any available details on purity, counterion, water content, and recommended handling that may influence research formulation decisions.

Physical Properties

Item-specific numerical specifications are not provided in the Product Data for this peptide.

• Appearance: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
• Melting point, boiling point, density, refractive index: Not applicable/Not specified for peptides; refer to CoA/Spec Sheet.
• Solubility (general guidance, literature/practice):
  • Likely soluble in aqueous media due to the lysine side chain and C‑terminal amide; initial dissolution in water, PBS, or dilute acids (e.g., 0.1% TFA or 10–50 mM HCl) often helps. If hydrophobic contributions (Tyr/Phe) impede solubility, co‑solubilize with small amounts of DMSO or DMF before dilution into buffer.
  • Avoid high pH during initial dissolution to prevent tyrosine oxidation; neutralize after full dissolution if needed.
• pKa considerations (literature):
  • Lys ε‑NH3+ pKa ~10.5; Tyr phenol pKa ~10; N‑terminus pKa ~8–9. The peptide’s overall ionization depends on medium ionic strength and temperature.
• LogP: Peptides are generally not described by logP; amphipathic character arises from mixed hydrophobic (F, Y) and basic (K) residues.
• Hygroscopicity: Small peptides can be hygroscopic and moisture‑sensitive depending on counterions and residual solvents (literature observation). Minimize atmospheric exposure.

Note: For authoritative physical specifications (water content, counterion, residual solvents, exact solubility), consult the product’s CoA/Spec Sheet.

Quality and Grades

• Grade: Moligand™. This designation indicates inclusion in Aladdin’s discovery/screening ligand portfolio, intended for research screening, target identification, and SAR exploration. It emphasizes consistency, handling convenience, and suitability for library use rather than pharmacopoeial compliance.

What this means in practice:

• Identity and purity: Supplied as a defined peptide sequence (GYPGKF‑NH2). Specific purity metrics, counterion identity, and analytical methods (HPLC area %, MS, NMR, water/solvent content) are Not specified for this item; refer to CoA/Spec Sheet.
• Low‑adsorption packaging: Library components are typically packaged to minimize peptide adsorption and moisture uptake; actual container/closure details are Not specified for this item.
• Stabilization: No stabilizer information is provided. If present, stabilizers or counterions will be listed on the CoA; otherwise, assume neat peptide.
• Trace specifications: Metal content, residual solvents, and bioburden/endotoxin limits are Not specified for this item; refer to CoA/Spec Sheet.

Fit for purpose:

• Analytical/assay suitability: Moligand™ items are suitable for biochemical screening (binding assays, enzymology, phenotypic assays), chemical biology, and method development. For regulated applications, additional qualification is required.

Documentation:

• CoA/Spec Sheet: Obtain lot‑specific HPLC/MS characterization, net peptide content, counterion, and recommended dissolution conditions from the CoA.
• SDS: Provides safety classification and handling details.

Note: For research use only.

Reaction and Applications

This product is a synthetic peptide tool compound rather than a synthetic reagent. Its primary uses are in biochemical and chemical biology workflows.

Research/application domains (general):

• Target screening and binding assays: As a defined sequence (GYPGKF‑NH2), it can be used to probe peptide–protein interactions, recognition motifs, or substrate preferences in enzyme or PPI assays.
• SAR and positional scanning: The sequence provides a basis for alanine scans, D‑isomer substitutions, or terminal modifications to map activity hot spots.
• Biophysical characterization: Evaluate interaction thermodynamics via ITC, MST, SPR, or fluorescence anisotropy (Tyr fluorescence/absorbance can assist in concentration determination and binding readouts).
• Cellular/biochemical assays: When cell‑permeability is required, conjugation to carriers (e.g., CPPs) or labeling (biotin/fluorophores) may be pursued; this item can serve as the unlabeled reference.
• Analytical standards: Use as an LC‑MS retention/mass reference in method development; the Tyr and Phe residues provide UV absorbance at 214/280 nm (literature property of aromatic residues).

Not typical applications:

• It is not commonly used as a reagent in bond-forming organic reactions (e.g., cross‑couplings, Grignards). See Synthetic Utility for limited derivatization strategies.

Practical notes:

• Work under inert atmosphere is generally unnecessary; however, limit exposure to oxidants/air for extended periods to protect tyrosine from oxidation (literature caution).
• For quantitative studies, determine exact peptide content (by amino acid analysis or UV at 280 nm using Tyr ε, literature) and correct for counterion/water content per CoA.

Reaction Conditions

This product is not intended as a reagent for classical organic reactions. Nevertheless, typical conditions relevant to peptide handling and derivatization are summarized for general guidance (literature/practice):

• N‑terminal acylation/labeling: Dissolve peptide in aqueous buffer (pH 7.5–8.5) with minimal organic co‑solvent; react with NHS esters (e.g., biotin‑NHS, fluorescent NHS dyes) at room temperature for 0.5–2 h. Control stoichiometry to limit over‑acylation of Lys ε‑NH2; alternatively, protect/selectively activate to target a single site.
• Lys ε‑amine selective acylation: Protect N‑terminus (e.g., Boc) or perform at slightly lower pH (7.5–8.0) to exploit pKa differences, using activated esters or carbonylimidazole reagents. Monitor by LC‑MS.
• Tyrosine modification: Diazonium coupling (in mildly basic aqueous media) or enzymatic tagging (tyrosinase/laccase) under ambient temperature; protect other nucleophiles as needed.
• Conjugation via click chemistry: Introduce azide/alkyne handles using NHS‑activated linkers, then perform CuAAC in water/t‑BuOH with Cu(I) catalysts and stabilizing ligands; keep metal exposure minimal if downstream biological assays are planned.
• Purification: RP‑HPLC with water/acetonitrile gradients containing 0.05–0.1% TFA or formic acid at ambient temperature. Detect at 214 nm and 254–280 nm (aromatics).

Note: Times, temperatures, and yields are application‑dependent and should be optimized empirically. No item‑specific reaction performance data are provided; consult primary literature and perform small‑scale pilots.

Safety and Handling

GHS classification and pictograms are not provided for this specific item. Always consult the SDS for authoritative safety information.

• Signal word: Not specified for this item; refer to SDS.
• Hazard statements (H‑statements): Not specified for this item; refer to SDS.
• GHS classification/pictograms: Not specified for this item; refer to SDS.

General laboratory safety for synthetic peptides (good practice):

• PPE: laboratory coat, safety glasses, and appropriate gloves (e.g., nitrile). Avoid aerosolization of powders; handle in a clean, dry area or fume hood.
• Inhalation/ingestion: Avoid breathing dust and avoid ingestion. Wash hands thoroughly after handling.
• Skin/eye contact: Rinse with copious water for at least 15 minutes if contact occurs. Remove contaminated clothing.
• Sensitization: Peptides can, in rare cases, be sensitizers. Minimize skin exposure.
• Chemical stability: Protect from strong oxidants (Tyr phenol is oxidation‑sensitive) and from prolonged basic conditions that may cause deamidation/isomerization.
• Incompatibilities: Strong oxidizers; strong bases; metal-catalyzed oxidants; avoid sodium hypochlorite and peroxides. Limit exposure to UV/visible light to mitigate photooxidation of tyrosine.
• Spills: Avoid dust formation; gently wipe with damp disposable towels, clean area with mild detergent. Dispose of waste per institutional guidelines.
• Fire: Organic solid; use CO2, dry chemical, or foam extinguishing media. Combustion may produce COx and nitrogenous fumes.

Note: For research use only. Not for human or veterinary use.

Solvent Selection

Peptide dissolution strategy focuses on achieving complete wetting and ionization control before dilution into the final assay buffer.

• Primary choices:
  • Water or aqueous buffers (e.g., PBS, HEPES) are preferred when feasible. The lysine side chain and C‑terminal amide typically support aqueous solubility.
  • Acidified water (e.g., 10–50 mM HCl or 0.1% TFA) can protonate basic sites and suppress aggregation during initial dissolution.
• Co‑solvents:
  • DMSO or DMF can be used to create a concentrated stock (e.g., 10–50 mM), subsequently diluted into aqueous media. Keep final DMSO below assay‑tolerated levels (commonly ≤0.5–1% v/v, assay‑dependent).
• Avoid:
  • Strongly basic solutions for initial dissolution (risk of tyrosine oxidation and backbone side reactions). If basic pH is necessary for an application, dissolve first under neutral/acidic conditions, then titrate.
• Miscibility profile (general):
  • Highly miscible with water when ionized; DMSO/DMF fully miscible with water allow gradient dilution.

Comparison (general guidance):

• Water vs DMSO: Water is greener and often sufficient; DMSO improves solubility for hydrophobic sequences (here, Phe/Tyr). Start with water; escalate to DMSO only if needed.
• Methanol/Acetonitrile: Useful for analytical work (HPLC mobile phases) but less ideal for long‑term storage stocks due to volatility and potential peptide denaturation.

Practical tips:

• Sonication and gentle warming (≤30–37°C) can aid dissolution.
• Filter sterilize (0.22 µm) if sterility is required; avoid filters that bind peptides (use low‑protein‑binding membranes).

Storage and Reconstitution

• Storage conditions (from Product Data): Room temperature.
• Shipped in: Not specified for this item; refer to label/CoA.
• Appearance: Not specified for this item; refer to CoA/Spec Sheet.

General best practices for peptides:

• Short‑term: Store tightly capped in a desiccator at room temperature away from light. Minimize exposure to ambient humidity.
• Long‑term: If extended storage is anticipated, consider 2–8°C or −20°C in desiccated conditions to limit oxidation/hydrolysis (literature practice), unless the label specifies otherwise.
• Reconstitution solvent: Start with water or aqueous buffer. If needed, pre‑dissolve in a minimal volume of DMSO/DMF, then dilute with buffer. Avoid strong bases initially to protect tyrosine.
• Concentration: Prepare concentrated stocks (e.g., 1–10 mM) to minimize storage volume. Determine peptide content from CoA to calculate accurate molarity.
• Aliquoting: Divide into single‑use aliquots in low‑bind tubes to avoid repeated freeze–thaw cycles and adsorption losses.
• Stability of solutions: Use aqueous solutions within 24–72 h when stored at 2–8°C. For longer durations, store frozen (−20°C) and protect from light; verify stability by LC‑MS/HPLC.
• Filtration: For sterile use, filter through 0.22 µm low‑protein‑binding membranes.

Note: Exact stability, counterion identity, and water/residual solvent content are Not specified for this item; consult the lot‑specific CoA/Spec Sheet for authoritative guidance.

Structure and Identity

Short description: GYPGKF-NH2 is a C‑terminally amidated hexapeptide with the sequence Gly–Tyr–Pro–Gly–Lys–Phe (free N-terminus, –CONH2 at C-terminus).

• SKU: rp174187
• Product name: GYPGKF-NH2
• CAS: rp174187 (internal identifier)
• Grade/Purity: Moligand™ (see Quality & Grades)
• Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
• SMILES: Not specified for this item; refer to CoA/Spec Sheet.
• InChIKey: Not specified for this item; refer to CoA/Spec Sheet.

Structural features (general description):

• Composition: 6 L-α-amino acid residues in the order G–Y–P–G–K–F.
• Functional groups: primary amine at the N-terminus; phenolic aromatic ring (Tyr); secondary amine in proline ring; ε-amine side chain (Lys); two phenyl rings (Tyr, Phe); peptide amide bonds along backbone; C-terminal carboxamide (–CONH2) rather than –CO2H.
• Ring systems: pyrrolidine ring in Pro; phenyl rings in Tyr and Phe; Tyr bears a para‑phenolic –OH.
• Net charge (qualitative, physiological pH): typically cationic due to Lys ε‑NH3+; Tyr phenol largely neutral; C‑terminal amidation removes the terminal carboxylate.
• Stereochemistry: peptide building blocks are conventionally L-configured (literature expectation for synthetic research peptides unless specified otherwise). Specific stereochemical confirmations are not provided for this item; refer to CoA/Spec Sheet.
• 2D description in words: a linear hexapeptide backbone with side chains extending: Gly (H), Tyr (p‑HO‑C6H4‑CH2‑), Pro (pyrrolidine ring bound to backbone N), Gly (H), Lys ((CH2)4‑NH2), and Phe (C6H5‑CH2‑), ending with –CONH2.

Synthetic Utility

While primarily a bioactive tool/ligand, GYPGKF‑NH2 can serve as a modular building block or reference standard in peptide chemistry.

Potential utilities (general):

• Derivatization at termini: The free N‑terminus enables acylation, succinylation, or conjugation (NHS esters, isocyanates) to attach labels (biotin, fluorophores) or carriers. The C‑terminal amide enhances stability against exopeptidases and mimics internal sequences.
• Side‑chain conjugation: The lysine ε‑amine offers a selective handle for orthogonal labeling if the N‑terminus is protected or differentially activated. Tyr phenol can undergo electrophilic substitution (e.g., diazonium coupling) or be used for click‑like enzymatic tagging (e.g., tyrosinase-mediated), subject to experimental design (literature techniques).
• Solid‑phase method development: Useful as a reference for RP‑HPLC method setup (retention behavior of mixed aromatic/basic peptides) and for calibrating MS detection (peptide mass fingerprinting; exact mass not specified here—refer to CoA).
• Affinity capture: Post‑functionalization (e.g., N‑terminal biotinylation), the sequence can be used to pull down binding partners from lysates, with the unlabeled peptide serving as a competition control.

Caveats:

• Maintain control over site‑selectivity during labeling (e.g., protect N‑terminus when targeting Lys ε‑NH2).
• Monitor for oxidation of Tyr during oxidative coupling methods; include antioxidants or perform under inert atmosphere if necessary.

This section provides general synthetic perspectives; no item‑specific reactivity data are provided in the Product Data.

Target Specificity

No target, receptor, enzyme, or antigen specificity is provided for GYPGKF‑NH2 in the Product Data.

• Target identity: Not specified for this item; refer to literature or in‑house screening results if available.
• Species reactivity/epitope: Not applicable; this is a synthetic peptide tool, not an antibody or antigen‑validated reagent.

Users should determine binding partners or biological effects empirically using appropriate controls (e.g., scrambled sequence, alanine scan, competition with unlabeled peptide).