neuropeptide-γ, Agonist of NK 1 receptor, CAS No.rp174616, Agonist of NK 1 receptor

CAS: rp174616 Cat. No.: rp174616

GRADE & PURITY Moligand™

Specifications

Product Name

neuropeptide-γ, Agonist of NK 1 receptor, CAS No.rp174616

Note

Moligand™

Spezifikationen & Reinheit

Moligand™

Aktionsart

AGONIST

Mechanismus der Wirkung

Agonist of NK 1 receptor

CAS

rp174616

Molekültyp

Peptide

Product Line

Biologische Produkte

Lagerung und Versand

Storage

Room temperature

Zugehörige Ziele (menschlich)

TACR1 Tclin Substance-P receptor (0 Activities)

Discover Target: TACR1

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

Genetische Informationen

• Referenz:
  • 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 manufacturer-verified application protocols, assay types, or recommended dilutions are provided for this item in the Product Data.

• General workflow suggestions (not item-specific)
  • Stock solution: Prepare at the highest feasible concentration in sterile water or 0.1% acetic acid; aliquot and store according to your laboratory’s practices. Record exact solvent composition and concentration.
  • Titration: Generate serial dilutions (e.g., 1:3 or 1:10) in low-bind plates to map a full concentration–response curve. Include vehicle controls matching the stock solvent (e.g., DMSO %) and appropriate assay standards.
  • Assay examples: GPCR functional assays (Ca2+ flux with fluorescent indicators), GTPγS binding (membranes), β-arrestin recruitment, or SPR/BLI for binding kinetics. Validate buffer composition and temperature to minimize degradation.
  • Stability tracking: Time-course activity checks at relevant temperatures; confirm integrity by LC–MS if loss of potency is observed.

For any validated, item-specific protocol parameters, consult the CoA/Spec Sheet or in-house method SOPs.

Biological Roles

• Literature/general biology (not item-specific; no clinical claims)

  • Family: Neuropeptide-γ is classified within the tachykinin peptide family, which includes neurokinin A and substance P. Tachykinins share a conserved C-terminal motif that interacts with neurokinin (NK) receptors.
  • Origin: Typically produced by proteolytic processing of a tachykinin precursor protein. Neuropeptide-γ represents an extended or alternative processing product relative to other tachykinins.
  • Molecular function: Acts as a neuromodulatory signaling peptide in vitro, capable of engaging tachykinin receptors (NK1/NK2/NK3) with receptor preference patterns that depend on the exact sequence and species origin (details vary in literature and are not specified for this item).
  • Biochemical features: The peptide backbone and side-chain composition confer receptor-binding affinity through electrostatic and hydrophobic contacts. Post-translational modifications (e.g., C-terminal amidation) can strongly influence potency and stability; specific modifications for this product are not specified.
  • Degradation pathways: Susceptible to proteolysis by endo- and exopeptidases; stability is enhanced under mildly acidic conditions and by using protease-free buffers and low temperatures during experiments.

• Research use context

  • Useful as a tool ligand in receptor-binding studies, second messenger assays (e.g., Ca2+ flux), and pathway mapping in biochemical systems. Confirm the receptor subtype selectivity and potency empirically for the batch in hand.

Item-specific details such as sequence, receptor selectivity, and activity values are not provided for this product; consult the CoA/Spec Sheet and primary literature for assay design.

Buffer Applications

Peptide performance in assays depends heavily on buffer composition and handling.

• General buffer guidance for peptides (not item-specific)

  • Stock preparation: Dissolve in water or 0.1% acetic acid, then dilute with the assay buffer of choice (e.g., PBS pH 7.2–7.4, HEPES pH 7.2–7.5). For adsorption-sensitive applications, include 0.01–0.1% carrier protein (BSA) if compatible.
  • pH range: Prepare concentrated stocks at mildly acidic pH (4–6) to minimize deamidation and oxidation; adjust to physiological pH after dilution into working buffer.
  • Ionic strength: Moderate ionic strength (50–150 mM total salts) helps maintain peptide solubility and reduces nonspecific interactions.
  • Protease control: Use protease-free buffers; add protease inhibitors only if they do not interfere with the assay readout.
  • Surfactants: Trace amounts (0.01%) of nonionic surfactants (e.g., Tween-20 or Pluronic F-68) can mitigate surface adsorption in microplates and vials; verify assay compatibility.
  • Filtration: If sterilization is necessary, use low-protein-binding 0.22 µm filters; avoid shear-sensitive handling.

• Not typically applicable

  • Classical acid/base buffer capacity design (Henderson–Hasselbalch) with defined pKa pairs is less relevant here because the peptide does not itself serve as a buffering agent; instead, select a buffer that preserves peptide integrity and receptor/assay performance.

Item-specific buffer recipes and stability data are not provided; consult the CoA/Spec Sheet and perform pilot stability checks.

Green Alternatives

For peptide ligands like neuropeptide-γ, greener practice centers on aqueous media, minimizing hazardous solvents, and reducing waste.

• Preferred media (general guidance)

  • Use water or biocompatible buffers (PBS, HEPES) as the primary solvent system. These are inherently greener than aprotic polar organics.
  • Employ minimal DMSO only to aid initial dissolution of hydrophobic sequences; keep final assay concentrations as low as feasible.

• Small comparison (general, not item-specific)

  • Water/buffer: renewable, low toxicity, ideal for bioassays; may require pH control for solubility/stability.
  • DMSO: effective co-solvent but with higher environmental footprint; limit volume and ensure proper waste segregation.
  • Acetonitrile: commonly used in analytics; consider water-rich gradients or methanol alternatives when chromatographically acceptable.

• Operational improvements

  • Prepare concentrated stocks to reduce solvent volumes over multiple assays.
  • Use low-bind consumables to avoid overdosing due to adsorption losses, thereby minimizing repeat runs and waste.
  • Adopt microplate formats and automation to cut reagent consumption.

• Trade-offs

  • Lower organic content can slow dissolution for hydrophobic sequences; brief sonication or gentle warming (≤25–30°C) can compensate without resorting to larger volumes of organic solvents.

Note: No specific greener substitute for the peptide itself applies; optimization focuses on solvent choice, waste minimization, and energy-efficient handling.

Pharmaceutical Uses

This catalog item is supplied strictly for research use only.

• Applicability

  • Peptide ligands like neuropeptide-γ are not typically used as general excipients. In pharmaceutical development contexts, related peptides may be investigated as active research substances in preclinical assays; however, this listing does not imply suitability for clinical, diagnostic, or therapeutic use.

• Formulation context (general, not item-specific)

  • For laboratory formulations (e.g., in vitro dosing solutions), peptides are commonly prepared as sterile aqueous stocks and diluted into assay media. Stabilization strategies may include mildly acidic pH, antioxidants compatible with the system, and avoidance of multivalent metal contaminants that can promote aggregation in some sequences.
  • For analytical reference purposes, peptides can serve as system suitability standards in LC–MS or HPLC; exact acceptance criteria must be defined by the user and are not specified for this item.

• Compliance

  • No pharmacopeial monograph, GMP status, or clinical-grade certification is claimed or provided for this item. Users must not apply this material to human or animal administration.

Item-specific regulatory or excipient information is not provided; refer to the CoA/Spec Sheet for available analytical documentation.

Physical Properties

• Item-specific (from Product Data)

  • Appearance: Not specified for this item; refer to CoA/Spec Sheet.

• Literature/general values for peptides of this class (not item-specific)

  • Physical state: typically lyophilized solid or film; may appear as white to off-white powder depending on counterions and residual moisture.
  • Solubility: peptides in the tachykinin family are generally soluble in aqueous buffers; initial dissolution often benefits from a small volume of sterile water or dilute acid (e.g., 0.1% acetic acid), followed by dilution with buffer. For hydrophobic sequences, co-solvents like DMSO can be used sparingly.
  • pH stability: many neuropeptides are most stable in mildly acidic solutions (pH ~4–6) during stock preparation; neutral pH is suitable for most bioassays after dilution. Avoid prolonged exposure to strong base which can promote deamidation/epimerization.
  • Hygroscopicity: peptides can be hygroscopic; minimize atmospheric exposure during handling.
  • Partition behavior: predominately hydrophilic with local hydrophobic domains; logP is not typically defined for peptides.

Important

• Exact melting point, density, refractive index, UV cutoff, and other analytical constants are sequence- and salt-form dependent and are not specified for this item; refer to the CoA/Spec Sheet and SDS for measured values if available.

Quality and Grades

• Item-specific (from Product Data)

  • Grade/Purity: Moligand™

• Interpretation and context (general, not item-specific specifications)

  • Moligand™ designation: In Aladdin Scientific’s catalog context, Moligand™ denotes compounds suited for ligand discovery, screening, and chemical biology applications. This typically implies suitability for routine in vitro assays, with identity verified and impurities controlled to a level compatible with screening workflows. Exact purity percentage, counterion content, water/solvent residuals, and peptide form (acetate/trifluoroacetate/free base) are not specified for this item; refer to the CoA/Spec Sheet.
  • Analytical controls commonly used for peptides: LC–MS for intact mass confirmation, analytical HPLC for purity profiling, and, where relevant, amino acid analysis or sequence confirmation. UV trace characteristics depend on aromatic residues and are not standardized across sequences.
  • Practical implications: For HTS or binding assays, prepare stock solutions under clean conditions (low bioburden), use low-binding plastics to reduce adsorption, and document solvent content (e.g., DMSO %) precisely. For quantitative studies, confirm batch-specific purity and counterion to enable accurate molar calculations.

• Documentation

  • For batch-specific grade attributes, impurity thresholds, and recommended analytical methods, consult the lot CoA and Spec Sheet. Do not infer water, metal, or peroxide limits beyond the supplied documentation.

Reaction and Applications

• Item-specific application domain (from Product Data)

  • Category: small-molecule and compound libraries (Moligand™); Research use only.

• Practical applications (general, not item-specific claims)

  • Receptor pharmacology: Neuropeptide-γ, as a tachykinin-family neuropeptide, is commonly used as a tool ligand to interrogate neuropeptide receptor function in vitro (e.g., binding, signaling, β-arrestin recruitment, calcium mobilization). Suitable for biochemical assays, target engagement, or comparative studies alongside other tachykinins. No specific activity or receptor profile is provided for this item; consult literature and validate in-house.
  • Assay development: Utilize as a positive control/reference agonist or as a component in concentration–response curves in GPCR-focused assays. Implement rigorous dilution schemes (serial 1:3 or 1:10) in low-bind plates to minimize adsorption and ensure reproducibility.
  • Analytical workflows: Calibrate LC–MS methods (intact mass) or HPLC retention time using the supplied material as a reference standard for sequence-confirmed lots; verify identity per CoA.

• Practical tips

  • Reconstitution: Start with sterile water or dilute acetic acid to achieve a concentrated stock (e.g., 0.5–2 mM, as solubility permits), then dilute into assay buffer. Filter through 0.22 µm if compatible, or prepare under aseptic conditions to avoid bioburden.
  • Stability: Keep working solutions on ice during experiments and aliquot stocks to avoid repeated freeze–thaw. Track on-bench time and discard aged solutions if activity drifts.

Note: No item-specific potency, receptor selectivity, or bioactivity data are provided; users should determine conditions empirically.

Reaction Conditions

Classical organic reaction conditions (solvent, catalyst, temperature, yields) are generally not applicable to a supplied peptide ligand. Instead, the focus is on solution preparation and assay handling.

• Solution handling conditions (general, not item-specific)

  • Reconstitution: Add sterile water or 0.1% acetic acid to reach a high-concentration stock as solubility permits. Gentle vortexing or brief sonication aids dissolution. Avoid vigorous agitation that can introduce bubbles and surface denaturation.
  • Temperature: Prepare and maintain working solutions on ice or at 2–8°C during experiments to limit proteolysis and degradation. Room-temperature bench time should be minimized.
  • Light/oxidation: Protect from strong light if fluorescent tags are present (not specified here). Minimize air exposure; purge headspace with inert gas for long-term storage of solutions when feasible.
  • Compatible media: Aqueous buffers (PBS, HEPES) at neutral pH for bioassays; mildly acidic conditions (pH 4–6) for stock stability.
  • Concentration ranges: For in vitro receptor assays, typical working concentrations span pM to µM, established empirically. No item-specific potency data are provided; perform preliminary titrations.

• Analytical QC during use

  • Monitor integrity by LC–MS or analytical HPLC after extended storage or if activity drifts. Check for aggregation by light scattering if solubility issues arise.

Note: No thermal, catalytic, or yield data apply; this section provides handling conditions analogous to “reaction conditions” for biochemical assays.

Safety and Handling

• Item-specific (from Product Data)

  • GHS Classification: Not specified for this item; refer to SDS.
  • Signal Word: Not specified for this item; refer to SDS.
  • H-Statements: Not specified for this item; refer to SDS.
  • Pictograms: Not specified for this item; refer to SDS.
  • Storage conditions: Room temperature (per Product Data).

• General guidance for peptide research reagents (not item-specific)

  • Hazards: Peptides are generally considered to have low acute toxicity; however, avoid inhalation of powders and contact with skin/eyes. Some neuroactive peptides can be biologically potent; handle with care to avoid accidental exposure.
  • PPE: laboratory coat, gloves (nitrile), and safety glasses. Use a dust mask or work in a ventilated enclosure when weighing lyophilized material.
  • Handling: Minimize aerosol generation. Reconstitute in closed containers. Avoid repeated freeze–thaw of solutions to limit degradation and aerosol risks.
  • Incompatibilities: Strong oxidants, strong bases (can cause backbone/side-chain degradation), proteases (biodegradation). Avoid prolonged exposure to elevated temperatures in solution.
  • First aid (overview): In case of skin/eye contact, rinse with water for several minutes. If inhaled, move to fresh air. If ingested, rinse mouth. Seek medical attention if symptoms persist. Always follow institutional EHS protocols.

Deferral

• For authoritative safety information, consult the product-specific SDS and institutional risk assessments. This product is for research use only.

Solvent Selection

Neuropeptide-γ is a peptide; solvent strategy focuses on achieving complete dissolution while preserving integrity.

• General solvent behavior (literature/general; not item-specific)

  • Primary medium: water or aqueous buffers are preferred. Initial wetting with a minimal volume of water or 0.1% acetic acid can facilitate dissolution, followed by dilution with assay buffer (e.g., PBS, HEPES).
  • Co-solvents: If hydrophobic residues impede solubility, use ≤10–20% DMSO or ≤20% acetonitrile in water as a co-solvent. Avoid neat organic solvents for storage; they can promote aggregation or denaturation.
  • pH considerations: Slightly acidic solutions (pH 4–6) often enhance solubility and stability for stock preparation; adjust to physiological pH after dilution into assay media.
  • Adsorption: Peptides can adsorb to glass and untreated plastics. Use low-bind polypropylene or silanized glass vials. Adding 0.01–0.1% carrier protein (e.g., BSA) or 0.01% nonionic surfactant may reduce losses in trace applications (evaluate for assay compatibility).

• When to choose alternatives

  • For highly hydrophobic sequences: consider buffered aqueous solutions with small amounts of chaotropes (e.g., 2–4 M urea) for temporary solubilization, then dilute to compatible conditions for the assay. Validate that additives do not interfere with readouts.

• Comparison (general)

  • Water/buffer: best for bioassays; minimal interference.
  • DMSO: strong solvating power; watch for cell-based assay tolerance (commonly ≤0.5–1% final).
  • Acetonitrile: useful in LC workflows and short-term stocks; less biocompatible than aqueous media.

Storage and Reconstitution

• Item-specific (from Product Data)

  • Storage conditions: Room temperature.
  • Shipped in: Not specified for this item; refer to CoA/Spec Sheet.
  • Appearance: Not specified for this item; refer to CoA/Spec Sheet.

• General best practices for peptides (not item-specific)

  • Short-term storage: If supplied lyophilized and sealed, room temperature storage is typically acceptable over the short term; protect from moisture. Upon opening, promptly reseal under dry conditions (desiccant) to limit hygroscopic uptake.
  • Long-term storage after reconstitution: Prepare aliquots to avoid repeated freeze–thaw. Store aqueous stocks at −20°C or −80°C depending on assay timelines; mildly acidic pH (4–6) can improve stability. Label with date, concentration, solvent, and pH.
  • Reconstitution procedure: Allow vial to equilibrate to room temperature in a desiccated environment before opening. Add a measured volume of sterile water or 0.1% acetic acid, gently vortex, and, if needed, briefly sonicate. For hydrophobic sequences, dissolve first in minimal DMSO, then dilute with buffer. Verify complete dissolution visually and, if critical, by analytical HPLC.
  • Handling: Use low-bind tubes and tips to minimize adsorption. Avoid strong base and oxidants during preparation and storage.

Note: Exact solubility, sequence, counterion, and stability data are not specified for this item; refer to the lot-specific CoA/Spec Sheet and SDS for authoritative guidance.

Structure and Identity

Neuropeptide-γ is a peptide ligand belonging to the tachykinin family. For peptide entries, conventional small-molecule identifiers may be incomplete or not applicable.

• Item-specific (from Product Data)

  • SKU: rp174616
  • Product name: neuropeptide-γ
  • CAS: rp174616 (catalog identifier as provided)
  • Grade/Purity: Moligand™
  • InChIKey: 280736 (as provided; note that peptides may not have a canonical small-molecule InChIKey)
  • SMILES: Not specified for this item; refer to CoA/Spec Sheet.
  • Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
  • Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.

• Literature/general description (not item-specific)

  • Structural class: peptide (tachykinin-derived). Typically linear, composed of standard proteinogenic amino acids, with a conserved C-terminal motif common to tachykinins.
  • Functional groups: amide backbone, side-chain functionalities depending on sequence (e.g., basic, acidic, aromatic residues). Terminal groups usually free or amidated/acetylated depending on biosynthetic context.
  • 2D structural features (conceptual): a linear chain of α-amino acids linked by amide (peptide) bonds, with potential post-translational modifications depending on source. No defined stereochemical ambiguity—L-configuration at α-centers is typical for ribosomal peptides.

Notes

• Sequence-level identity, exact residue count, and any modifications are not specified for this catalog item; consult the CoA/Spec Sheet for definitive structural details.

Synthetic Utility

Neuropeptide-γ is a finished peptide ligand intended as a research tool rather than a building block; it is not commonly used as a substrate in traditional small-molecule synthesis.

• General synthetic context (not item-specific)

  • Solid-phase peptide synthesis (SPPS): Peptides of this class are commonly prepared via Fmoc/tBu SPPS, followed by global deprotection and cleavage, HPLC purification, and counterion exchange as needed. If the user’s application involves analog design, the known tachykinin motif can be diversified to probe structure–activity relationships (SAR).
  • Derivatization: N-terminal acetylation or C-terminal amidation, fluorescent tagging (e.g., FITC, Alexa dyes), or biotinylation may be introduced in custom syntheses for binding and trafficking studies. Such modifications can influence potency and stability and must be validated empirically.
  • Conjugation chemistry: Amine-reactive (NHS esters) or thiol-reactive (maleimides) tags can be appended where sequence permits; site-selective strategies (orthogonal protecting groups or enzymatic approaches) improve homogeneity.

• Retrosynthetic value

  • Peptide serves primarily as a biological probe for receptor engagement rather than as a versatile synthon. For small-molecule medicinal chemistry, use peptide-derived pharmacophores to inspire non-peptidic mimetics.

Item-specific protecting group strategy, sequence, or modification pattern is not provided; consult the CoA/Spec Sheet if such details are included for the supplied lot.

Target Specificity

No item-specific target information is provided in the Product Data.

• General note (literature; not item-specific claims)

  • Neuropeptide-γ belongs to the tachykinin family whose members interact with neurokinin receptors (NK1, NK2, NK3). Exact receptor subtype preference, potency, and species dependence for this product are not specified and should not be inferred.

• Guidance

  • Users should determine receptor specificity empirically using binding assays, functional readouts (e.g., Ca2+ mobilization), or β-arrestin recruitment, with appropriate positive controls and antagonists. Consult primary literature for assay design relevant to the tachykinin system.

For validated, item-specific target data (if available), refer to the CoA/Spec Sheet.

Häufig gestellte Fragen

What is Moligand??

Moligand? is one of Aladdin Scientific's premium product lines, formulated for high-purity applications across multiple workflows. Compared to standard grades in the same workflow, Moligand? products typically offer tighter specifications, more rigorous QC, and stronger lot-to-lot consistency.

How should this product be stored?

Store at room temperature.

What are the CAS number, molecular formula and molecular weight?

The CAS Number is rp174616. InChIKey PLSDWRYNZIVQKX-BGKYVOMCSA-N.

What documentation is provided?

Available product documentation, including Certificates of Analysis (COA), Safety Data Sheets (SDS), and specification sheets, is shown in the product document area. Document availability and access follow the current site policy.