neuropeptide EI, CAS No.rp174613

CAS: rp174613 Cat. No.: rp174613

GRADE & PURITY Moligand™

Specifications

Product Name

neuropeptide EI, CAS No.rp174613

Sinonimi

NEI | neuropeptide E-I | neuropeptide-glutamic acid-isoleucine

Grado

Moligand™

Specifiche e purezza

Moligand™

CAS

rp174613

Tipo di molecola

Peptidi

Product Line

Prodotti biologici

Stoccaggio e spedizione

Condizioni di conservazione di stoccaggio

Room temperature

Informazioni genetiche

• Alternate Names: NEI | neuropeptide E-I | neuropeptide-glutamic acid-isoleucine
• 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

Item-specific facts (from Product Data)

• Tested applications, assay formats, or recommended dilutions: Not specified for this item; refer to CoA/Spec Sheet.

General guidance for peptide ligand testing (not item-specific)

• Stock solution: Prepare at high concentration (e.g., 1–10 mM or as solubility allows) in water, buffer, or DMSO; aliquot and store to avoid repeated freeze–thaw.
• Dose–response: Generate 10-point half-log serial dilutions spanning anticipated potency; include vehicle controls and, when available, a known reference ligand.
• Assay windows: For GPCR readouts, measure rapid responses (Ca2+, cAMP) within minutes; for phosphorylation endpoints, typical time points are 5–60 min. For gene expression, 2–24 h.
• Plate handling: Use low-bind plastics; pre-wet tips; mix gently to avoid foaming/adsorption losses.
• Data QC: Confirm actual concentration by UV or amino acid analysis if critical; back-calculate delivered dose considering adsorption and dilution errors.

Note

• Without item-specific validation data, these are starting points only. Optimize parameters for your cell line, receptor expression level, and detection method.

Biological Roles

Item-specific facts (from Product Data)

• No target, sequence, or organismal context is provided for neuropeptide EI (SKU: rp174613).

General background on neuropeptides (class-level, literature; not item-specific)

• Neuropeptides are signaling peptides used by neurons and neuroendocrine cells to modulate synaptic transmission, hormonal release, and diverse physiological processes. They typically act via G protein–coupled receptors (GPCRs) or, in some cases, ligand-gated channels.
• Biosynthesis: Generated as larger prepropeptides, processed in the ER/Golgi, and packaged into dense-core vesicles; post-translational modifications (amidation, acetylation, sulfation, disulfides) tune receptor affinity and stability.
• Pharmacology: Often exhibit high potency (nM range) and receptor-subtype selectivity; efficacy and bias can be influenced by sequence truncations, PTMs, and conformational constraints.
• Deactivation: Cleared by peptidases (e.g., neprilysin, aminopeptidases, endopeptidases) and by receptor-mediated internalization; sequence motifs strongly affect half-life in extracellular environments.
• Experimental implications: For in vitro work, use protease-free buffers or add protease inhibitors; for live-cell assays, limit exposure times or use serum-free windows to reduce degradation.

Caveat

• Without sequence/target attribution, no specific receptor family, tissue distribution, or pathway involvement can be ascribed to this SKU. Consult the CoA or technical datasheet for any available biological context.

Buffer Applications

Item-specific facts (from Product Data)

• No buffer recommendations or pH specifications are provided for this SKU.

General peptide buffer practices (not item-specific)

• Stock preparation: Dissolve the peptide in a small volume of compatible buffer. Common choices include water, PBS (pH ~7.2–7.4), HEPES (pH 7.2–7.6), or acetate (pH 4–5) depending on sequence charge properties.
• pH adjustment strategy: Slight acidification (0.1% acetic acid or TFA) tends to aid solubility of basic peptides; slight basification (≤10 mM NH4OH) can help acidic sequences. After dissolution, back-titrate to assay pH if required.
• Additives for stability: 0.1% BSA or inert sugars (trehalose) can reduce adsorption and aggregation for low-concentration working solutions, provided they are assay-compatible.
• Filtration: Use 0.22 µm sterile filters for cell-based work; pre-wet filters with buffer to minimize non-specific binding.
• LC/MS workflows: Mobile phases often employ 0.1% formic acid (positive mode) or 0.1% ammonium hydroxide (negative mode) in water/acetonitrile gradients; ensure the peptide is compatible with these conditions.

Important

• Because the exact sequence and pI are unknown for this item, optimize buffer composition empirically and verify integrity by LC–MS/HPLC after dissolution. Refer to the CoA for any item-specific guidance if available.

Green Alternatives

Context

• Specific solvent/process data for this item are not provided. Nevertheless, handling peptides often allows greener choices by leveraging aqueous media and minimizing hazardous organic solvents.

Greener choices for peptide work (general guidance)

• Prefer water-based buffers: Use PBS, HEPES, or acetate buffers in place of high fractions of acetonitrile, DMF, or DMSO where assay compatibility permits.
• Minimize DMSO: Keep DMSO ≤1–2% v/v in final assay solutions to reduce cytotoxicity and environmental load; validate solubility beforehand.
• Use ethanol or isopropanol as co-solvents when feasible instead of chlorinated solvents.
• Energy efficiency: At bench scale, most peptide operations occur at ambient temperature; avoid unnecessary heating/cooling cycles and use lyophilization rather than solvent-intensive evaporation when preparing solids.

Illustrative comparison (general)

• Organic-heavy dissolution (DMF/DMSO >20%): Higher environmental and safety burden; may increase assay artifacts.
• Aqueous-first strategy with mild pH adjustment: Lower hazard, compatible with most bioassays, reduced waste.

Waste and lifecycle considerations

• Neutralize and dispose of buffer wastes through aqueous waste streams per institutional rules; segregate high-organic fractions for solvent waste.

Note

• Always balance greenness with integrity of the peptide and the assay readout; sequence-specific behavior may necessitate limited use of less green solvents.

Pharmaceutical Uses

Item-specific facts (from Product Data)

• Research Use Only: For research use only (not for human or veterinary use).
• No pharmacopeial status or excipient role is provided for this SKU.

General context for peptide materials in pharmaceutical R&D (not item-specific; no therapeutic claims)

• Reference standards and controls: Peptides are frequently used as analytical standards in method development/validation (e.g., LC–MS peptide assays) and as positive controls in bioassays during discovery.
• Formulation research: Early-stage studies may evaluate solubility enhancers, stabilizers (antioxidants for Met/Cys; chelators to limit metal-catalyzed oxidation), and delivery matrices (e.g., lipidic systems) using model peptides.
• Manufacturability studies: Screen lyophilization cycles, counter-ion exchange (e.g., acetate vs. TFA salts), and excipient compatibility to improve solid-state stability—activities strictly within preclinical and process development labs.
• Impurity profiling: Forced degradation (pH, temperature, oxidants) can map degradation pathways (deamidation, oxidation, isomerization) to inform control strategies.

Compliance reminder

• This product is not intended for clinical administration. No claims are made regarding GMP status, pharmacopeial compliance, or clinical suitability. For regulated applications, obtain GMP-grade materials and full regulatory documentation.

Physical Properties

Item-specific facts (from Product Data)

• Physical state/appearance: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
• Other specifications (mp, solubility limits, pKa, logP/logD, UV cutoff, refractive index): Not specified for this item; refer to CoA/Spec Sheet.

General/literature guidance for peptides (not item-specific)

• Form: Synthetic peptides are typically supplied as lyophilized solids or amorphous powders; hygroscopicity can vary with sequence and counter-ions.
• Solubility: Depends strongly on sequence. Common strategies include:
  • Start with water or physiological buffers; if insoluble, add small amounts of acetonitrile or isopropanol, or adjust pH (acidify with dilute acetic acid/TFA for basic peptides; basify with dilute NH4OH for acidic peptides).
  • For highly hydrophobic sequences, pre-dissolve in DMSO or DMF and then dilute with aqueous buffer to desired concentration.
• Stability (qualitative): Peptides are generally stable as dry solids under desiccation. In solution, susceptibility to hydrolysis, oxidation (Met, Cys), and aggregation increases with time, temperature, and pH extremes.
• Spectroscopy: Aromatic residues (Trp, Tyr, Phe) provide UV absorbance near 280/274 nm (literature); exact ε depends on composition.

Note

• Without the exact sequence and counter-ion content, quantitative properties (exact pI, extinction coefficient, and solubility limits) cannot be asserted for this item.

Quality and Grades

Item-specific facts (from Product Data)

• Grade/Purity designation: Moligand™
• Appearance: Not specified for this item; refer to CoA/Spec Sheet.

What Moligand™ typically implies (general program description; not a specification)

• Moligand™ offerings are positioned for small-molecule/ligand discovery workflows (e.g., screening, hit validation, basic pharmacology/biochemistry). In practice, such collections emphasize clear identity confirmation and fitness for in vitro research use.
• Typical quality elements in ligand screening materials may include analytical identity checks (e.g., LC–MS, HRMS) and purity adequate for screening; however, exact tests and acceptance criteria vary by item. Do not assume a specific purity percentage, counter-ion, or salt form without the item’s CoA.

How to use quality information effectively

• Verify identity and purity on receipt using the product’s CoA and your internal acceptance testing (e.g., LC–MS, HPLC area %, peptide mapping if sequence is provided).
• For bioassays, consider secondary purification or desalting if matrix effects are observed. Document the lot number in all data records for reproducibility.

Non-negotiable reminder

• Do not infer unstated specifications (water content, residual solvents, metal content, UV cutoff, stabilizers). If a value is required for your method validation, request the current CoA/Specification Sheet for this exact SKU/lot.

Reaction and Applications

Item-specific facts (from Product Data)

• Manufacturer Applications: Not specified in the listing beyond inclusion in a small-molecule/compound library category.

General research applications for neuropeptide-class ligands (not item-specific)

• Receptor pharmacology: Peptides often serve as reference ligands in GPCR, ion channel, or receptor tyrosine kinase assays to establish signal windows, calibrate EC50/IC50 determinations, or benchmark antagonist/agonist responses.
• Cellular signaling studies: Evaluate pathway activation (e.g., second messengers, phosphorylation cascades) in relevant cell lines or primary cultures. Include appropriate positive/negative controls and desensitization checks.
• Systems biology: Use as inputs in network perturbation experiments, time-course transcriptomics/proteomics, or secretome response profiling.
• Analytical standards: Calibrate LC–MS methods for peptide detection/quantification, retention time indexing, and instrument performance checks.

Practical tips (general)

• Prepare fresh working solutions and minimize adsorption to plastics by using low-bind tubes or adding carrier proteins (e.g., 0.1% BSA) if compatible.
• Titrate concentration carefully; many peptide ligands act at low nM–µM. Validate concentration by UV at 205–215 nm or 280 nm if aromatic residues are present (extinction coefficient is sequence-dependent).
• Control for peptidase degradation in biological media (consider protease inhibitors or short exposure times). Avoid repeated freeze–thaw of stock solutions by aliquoting.

Note

• No specific biological target or assay format is provided for this SKU; design studies accordingly and confirm identity/purity with the CoA.

Reaction Conditions

Item-specific facts (from Product Data)

• No reaction/coupling conditions or sequence are provided for this SKU.

General conditions for common peptide modifications (literature; not item-specific)

• Amide coupling (solution phase): NHS ester (activated carboxylate) with primary amines in pH 7.5–8.5 buffers (e.g., phosphate/borate); typical times 0.5–2 h at RT. Control hydrolysis by using fresh reagents and organic co-solvents as needed.
• Thiol conjugation: Maleimide–thiol addition near pH 6.5–7.0 to minimize maleimide ring opening; rapid (minutes to 1 h) at RT. Alternative: iodoacetamide alkylation at pH 7.5–8.3.
• Click chemistry: CuAAC between azide/alkyne handles using CuSO4/sodium ascorbate with TBTA or water-soluble ligands; often RT, 30–120 min. Copper-free SPAAC for live-cell contexts.
• Oxidation state control: For cystine formation, air oxidation or mild oxidants (e.g., DMSO) at pH ~8; monitor by LC–MS to avoid over-oxidation to sulfinic/sulfonic acids.
• Labeling stoichiometry: Use 1.1–1.5 equiv of reagent per available site; verify completion and preserve bioactivity by minimal over-labeling.

Notes

• Sequence dictates optimal pH/solvent and the need for chaotropes (urea/guanidine) or organics (DMSO, acetonitrile). Validate conditions on micro-scale before committing valuable material.
• No yield or kinetic claims are made for this SKU; consult the CoA and perform pilot studies.

Safety and Handling

Item-specific facts (from Product Data)

• GHS classification, signal word, hazard statements, and pictograms: Not specified for this item; refer to SDS.
• Storage condition (as supplied): Room temperature (per Product Data).

General safety guidance for peptide research materials (not item-specific; defer to SDS)

• PPE: Wear lab coat, safety glasses, and appropriate gloves. Avoid generating dust/aerosols; handle powders in a fume hood or ventilated enclosure.
• Inhalation/dermal risks: Although many peptides are of low volatility, avoid inhalation of particulates and skin contact. Some sequences can be biologically active at low concentrations; prevent exposure.
• First aid overview: In case of contact, rinse skin/eyes with water for several minutes. If inhaled, move to fresh air. If ingested, rinse mouth and seek medical advice. Always consult the SDS for definitive measures.
• Incompatibilities (general): Strong oxidizers may degrade susceptible residues (Cys, Met, Trp). Avoid prolonged exposure to basic or strongly acidic conditions unless required for solubilization and used briefly.
• Housekeeping: Use clean, dedicated tools to prevent cross-contamination. Cap containers promptly; minimize headspace to reduce moisture uptake.
• Waste: Dispose of aqueous or organic peptide solutions and contaminated consumables according to institutional chemical waste procedures.

Authoritative reference

• Always consult the product-specific SDS and CoA for definitive hazard, handling, and decontamination guidance.

Solvent Selection

Item-specific facts (from Product Data)

• Solubility and solvent preferences: Not specified for this item; refer to CoA/Spec Sheet.

General, sequence-dependent strategies for dissolving peptides (literature/good practice)

• Start simple: Attempt dissolution in ultrapure water (or buffer) at a modest concentration (e.g., 0.1–1 mg/mL), gently vortex/sonicate.
• Adjust pH strategically:
  • Basic/arginine/lysine-rich peptides: Slight acidification with dilute acetic acid or 0.1% TFA can improve solubility.
  • Acidic/aspartate/glutamate-rich peptides: Slight basification with dilute NH4OH or Tris base may help.
• Use co-solvents judiciously: DMSO or DMF can pre-solubilize hydrophobic sequences; subsequently dilute into aqueous buffer to reduce organic content (<1–5% v/v) for biological assays.
• Additives: 0.1% TFA or 0.1% formic acid aids LC compatibility; 10–20% acetonitrile with water can aid poorly soluble hydrophobic peptides for analytical work.

Choosing among alternatives

• If strong hydrophobicity persists, consider mild detergents compatible with the assay (e.g., 0.01% Tween-20) or cyclodextrins; verify they do not interfere with readouts.
• For long-term stock solutions, prefer buffers that minimize oxidation (e.g., add antioxidant for Met/Cys-containing peptides) and avoid metal-catalyzed degradation (use plastic or passivated glass).

Important

• Final solvent systems should be validated in your exact assay. When in doubt, consult the CoA or contact technical support for sequence-specific recommendations.

Storage and Reconstitution

Item-specific facts (from Product Data)

• As supplied storage: 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 reconstitution guidance for peptides (not item-specific)

• Reconstitution: Dissolve the material in an appropriate solvent (water, buffer, or minimal DMSO/DMF) using the solvent selection strategy described above. If sequence is unknown, begin with water or mildly acidic buffer, then adjust as needed.
• Working stocks: Prepare concentrated stocks and aliquot into low-bind tubes to minimize adsorption and freeze–thaw cycling. Label aliquots with concentration, solvent, and date.
• Storage after reconstitution: Although the solid is listed for room-temperature storage, peptide solutions are typically kept at 2–8°C for short term (≤1 week) or −20 to −80°C for longer term, protected from light and air; include inert atmosphere if oxidation-prone residues are suspected. Validate stability empirically.
• Handling: Allow frozen aliquots to thaw on ice; mix gently. Avoid repeated freeze–thaw by using single-use aliquots.

Critical reminder

• Because item-specific stability data are not provided, confirm integrity over time by LC–MS/HPLC and consult the CoA/SDS for any special instructions (e.g., counter-ion, recommended solvents, or stabilizers).

Structure and Identity

Item-specific facts (from Product Data)

• Product name: neuropeptide EI (SKU: rp174613)
• Grade: Moligand™
• CAS: rp174613 (internal identifier)
• Storage: Room temperature
• 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.

General chemistry notes (class-level, literature)

• “Neuropeptide EI” suggests a peptide-class ligand; peptides are linear polymers of amino acids linked by amide (peptide) bonds, commonly bearing an N-terminal amine and a C-terminal carboxylate (often capped or modified).
• Typical peptide structural features may include side-chain functionalities (e.g., basic residues such as Lys/Arg; acidic residues such as Asp/Glu; aromatic residues such as Phe/Tyr/Trp), potential post-translational modifications (PTMs) like amidation, phosphorylation, or disulfide bridges (if Cys present).
• 2D description (generic peptide): a backbone of repeating –NH–CH(R)–C(=O)– units, with variable side chains R defining sequence-specific properties (charge, hydrophobicity, H-bonding, aromaticity). Stereochemistry is usually L for proteinogenic residues.

Important limitation

• The exact sequence, length, modifications, and stereochemical details for this specific item are not provided here. Consult the Certificate of Analysis (CoA) or specification sheet for definitive identity data (sequence, exact MW, purity verification).

Synthetic Utility

Item-specific facts (from Product Data)

• No sequence or functional handles are provided; synthetic derivatization potential is therefore unspecified.

General utility of peptides as synthetic/scaffold tools (not item-specific)

• Conjugation handles: Side chains (Lys ε-NH2, Cys thiol, Asp/Glu carboxylates, N-terminus) offer orthogonal points for bioconjugation (NHS-ester amide formation, maleimide–thiol coupling, click chemistry via azido/alkynyl modifications).
• Probe development: Attaching fluorophores, affinity tags (biotin), or photo-crosslinkers enables receptor mapping, trafficking studies, and pulldown experiments.
• SAR exploration: Systematic alanine scans or conservative substitutions (e.g., Leu→Nle) help parse binding hot-spots; backbone N-methylation or cyclization can modulate potency and proteolytic stability.
• Solid-phase peptide synthesis (SPPS) compatibility: If sequence is known, on-resin diversification allows rapid generation of analog libraries; post-assembly modifications (acetylation/amidation) tune charge and solubility.
• Materials science: Peptide motifs can serve as self-assembling building blocks; aggregation propensity is sequence-specific and can be harnessed for nanostructures.

Caveat

• The above strategies are general. Without the specific sequence of neuropeptide EI, concrete synthetic routes, protecting-group strategies, or site-selective derivatizations for this item cannot be prescribed.

Target Specificity

Item-specific facts (from Product Data)

• Target/antigen, receptor subtype(s), species selectivity, and binding parameters: Not specified for this item; refer to CoA/Spec Sheet.

Statement on applicability

• This section typically applies to biologics/antibodies or well-annotated ligands with defined receptor targets. Because no target information is supplied for neuropeptide EI (SKU: rp174613), target specificity cannot be summarized here.

Recommendation

• If target identity is critical to your study, request sequence and any available binding data (Kd, EC50/IC50, assay format) from the CoA or technical support, and verify under your assay conditions.

Domande frequenti

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 rp174613.

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.