This compound belongs to the class of organic compounds known as indolyl carboxylic acids and derivatives. These are compounds containing a carboxylic acid chain (of at least 2 carbon atoms) linked to an indole ring.
External Descriptors
Not available
1. Djoumbou Feunang Y, Eisner R, Knox C, Chepelev L, Hastings J, Owen G, Fahy E, Steinbeck C, Subramanian S, Bolton E, Greiner R, and Wishart DS. ClassyFire: Automated Chemical Classification With A Comprehensive, Computable Taxonomy. Journal of Cheminformatics, 2016, 8:61.
Zertifikate (CoA, COO, BSE/TSE und Analyse-Diagramm)
C of A & Other Certificates(BSE/TSE, COO):
Analytical Chart:
Chemische und physikalische Eigenschaften
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Schmelzpunkt (°C)
280-285℃ (dec.) (lit.)
Molekulargewicht
206.210 g/mol
XLogP3
-1.100
Hydrogen Bond Donor Count
3
Hydrogen Bond Acceptor Count
3
Rotatable Bond Count
3
Exact Mass
206.084 Da
Monoisotopic Mass
206.084 Da
Topological Polar Surface Area
79.100 Ų
Heavy Atom Count
15
Formal Charge
0
Complexity
245.000
Isotope Atom Count
2
Defined Atom Stereocenter Count
1
Undefined Atom Stereocenter Count
0
Defined Bond Stereocenter Count
0
Undefined Bond Stereocenter Count
0
The total count of all stereochemical bonds
0
Covalently-Bonded Unit Count
1
Lösungsrechner
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Application Protocols
No immunoassay/antibody application protocols apply to this product. For general laboratory use:
LC–MS internal standard (general): Prepare a ~1–5 mM stock in water or 0.1% formic acid; verify concentration gravimetrically; store aliquots at −20 °C; dilute into samples to achieve 1–10 µM final.
NMR sample (general): Dissolve 2–20 mM in D2O or appropriate deuterated solvent; adjust pD/pH to probe protonation states of the α-amine and indole nitrogen; acquire 1H–15N HSQC if paired with a 15N-enriched protein or in concentrated small-molecule samples.
These are general/literature-style workflows and should be adapted to specific instruments and experimental designs.
Biological Roles
L-Tryptophan is an essential amino acid and a biosynthetic precursor in several central metabolic and signaling pathways; the 15N2 label enables tracing without altering its biochemical function (literature/general):
Protein incorporation: Incorporated into proteins during translation; indole side chain contributes to hydrophobic packing, π–π interactions, and intrinsic fluorescence used to probe protein environments.
Tryptophan catabolism (kynurenine pathway): Oxidative cleavage by tryptophan 2,3-dioxygenase/indoleamine 2,3-dioxygenase leads to kynurenine derivatives, quinolinic acid, and ultimately NAD+ biosynthesis; 15N labels allow mapping of nitrogen transfer and loss steps.
Serotonin/melatonin branch: Decarboxylation and hydroxylation yield tryptamine/serotonin and, in animals/plants, downstream melatonin; 15N at the indole and α-amino nitrogens can differentiate amine nitrogen fate versus ring nitrogen retention.
Indole chemistry in microbiomes/plants: Microbial tryptophanases and plant auxin (IAA) biosynthesis utilize tryptophan; isotope tracing clarifies pathway contributions and exchange with environmental nitrogen pools.
Transport and regulation: Competes at large neutral amino acid transporters; participates in nitrogen homeostasis studies with 15N tracers.
Use considerations (general):
Maintain defined nitrogen sources in culture media to preserve high atom% labeling in downstream metabolites/proteins.
For NMR studies, pairing 15N with 13C-labeled counterparts (e.g., 13C11,15N2) increases spectral resolution and assignment power.
Buffer Applications
This product is not a buffering reagent and is not typically used to prepare buffer systems.
Practical note: As an amino acid with two ionizable groups (pKa ~2.38 and ~9.39; literature), it does exhibit pH-dependent acid/base behavior, but its low solubility near the isoelectric point and lack of a wide, flat buffering range make it unsuitable as a primary buffer.
Relevant laboratory use: Intrinsic indole fluorescence (Ex ~280 nm, Em ~350 nm; literature) makes L-tryptophan a useful probe or standard in fluorescence assays performed in common biological buffers (e.g., phosphate, Tris). Choose the buffer based on your assay; the amino acid does not dictate buffer selection.
Green Alternatives
For isotopically labeled amino acids, environmental impact is driven more by synthesis/production routes and solvent choices during use than by the compound itself.
Greener sourcing and handling (general guidance):
Biosynthetic production: Fermentation using 15N-enriched ammonia or nitrate can provide 15N-labeled amino acids with lower solvent use and milder conditions compared to purely chemical routes. Verify the route with the supplier when lifecycle impact matters.
Aqueous processing: Favor water-based dissolutions and buffer systems over polar aprotic solvents when feasible; adjust pH to improve solubility and avoid DMSO/DMF.
Micelle/biocatalytic media: For derivatizations, consider enzymatic coupling or peptide ligation under aqueous conditions (e.g., EDC/sulfo-NHS in water) to minimize hazardous solvent usage.
Waste minimization: Prepare concentrated stocks to reduce container count and rinses; use reusable glassware and limit single-use plastics where compatible with trace-isotope work.
Comparison snapshot (general):
Conventional peptide coupling in DMF (HATU/DIPEA): High-performance but uses problematic solvent; generates guanidinium waste.
Aqueous EDC or carbodiimide coupling: Greener solvent matrix, but may require pH control and careful removal of urea byproducts; coupling efficiency can be lower for sterically hindered sequences.
Enzymatic ligation (e.g., sortase/transglutaminase-based): Minimal hazardous reagents, highly selective; narrower substrate scope and often higher cost.
Tradeoffs: Avoiding DMF/DMSO improves EHS profile but may impact solubility and rate; optimizing pH and using surfactants/co-solvents can bridge performance gaps.
Pharmaceutical Uses
No therapeutic/clinical claims are made. The following describes non-clinical, manufacturing, and analytical contexts (general):
Cell culture and bioprocessing: Component of chemically defined media and feeds for microbial, mammalian, and plant cell cultures; 15N2 variants are used in metabolic studies and labeling experiments to support process characterization by LC–MS/NMR.
Analytical reference standard: 15N2-labeled L-tryptophan serves as an internal standard for quantitative assays (e.g., content uniformity of tryptophan-containing formulations, stability studies, or impurity profiling by LC–MS), enabling isotope-dilution accuracy.
Excipient research: Amino acids are explored as stabilizers/osmolytes in protein formulations; tryptophan’s role is typically investigative due to its UV absorbance, which aids monitoring. Any specific excipient role for this SKU is Not specified for this item; refer to CoA/Spec Sheet.
Pharmacopeia status: Isotopically labeled analogs are generally not monographed; if compendial alignment is needed, qualify against in-house specifications and relevant general chapters (e.g., residual solvents, elemental impurities) as applicable.
Implementation notes:
Use high-purity water and low-binding plastics/glass to minimize adsorption losses during standard preparation.
Verify isotopic purity and absence of unlabeled carryover to ensure accurate isotope-dilution quantitation.
Physical Properties
Item-specific values beyond storage are not provided in the Product Data. The following are literature/computed properties for the L-tryptophan scaffold and generally apply to the 15N2 isotopolog (mass-shift only):
Appearance: Not specified for this item; refer to CoA/Spec Sheet.
Melting point: ~289 °C (dec.) (literature, unlabeled L-tryptophan).
Boiling point: Not applicable (decomposes before boiling) (literature).
Density: Not specified for this item; refer to CoA/Spec Sheet.
Aqueous solubility (25 °C): ~11–12 g/L at neutral pH; substantially higher in acidic/basic media due to ionization (literature, L-tryptophan).
pKa values (literature, 25 °C): pKa1 (CO2H) ~2.38; pKa2 (NH3+) ~9.39. Indole [N–H] is very weakly acidic (pKa ~16–17 in DMSO; conjugate acid pKa ~−2) (literature).
Isoelectric point (pI): ~5.89 (literature).
logP (XlogP3-AA): ~−1.1 (literature, neutral form); effective distribution depends strongly on pH (zwitterion at physiological pH) (literature).
UV–Vis: Strong indole absorbance near 280 nm (ε ≈ 5.5–5.8 × 10^3 M−1 cm−1, literature), useful for quantitation and fluorescence excitation (ex ~280 nm, em ~350 nm for indole) (literature).
Refractive index, vapor pressure, specific conductance: Not applicable/not specified for solids of this type.
Important: Treat all numerical values here as literature guidance for the unlabeled parent; the 15N2 label changes mass but not bulk physical behavior to a meaningful extent.
Quality and Grades
Grade/Purity: Not specified for this item; refer to CoA/Spec Sheet.
Isotopic enrichment: Critical performance attribute for 15N2 materials; typical market offerings are ≥98 atom% 15N per nitrogen, but the exact enrichment for this SKU is Not specified for this item; refer to CoA/Spec Sheet.
Enantiomeric purity: L-form is indicated; laboratories typically expect ≥98–99% ee for peptide/synthesis work. Actual value Not specified for this item; refer to CoA/Spec Sheet.
Residual solvents, water content, metals, and UV-cutoff: Not specified for this item; refer to CoA/Spec Sheet.
Stabilizers/additives: Not specified for this item; refer to CoA/Spec Sheet.
How to interpret grades for this class of product (general guidance):
Isotopic grade: Specifies atom% 15N and isotopologue distribution (e.g., 15N2 vs 15N1/unlabeled). High-resolution MS or isotope-ratio MS is typically used to verify.
Synthesis/peptide grade: Low inorganic residues and tight control of water facilitate coupling efficiency; low fluorescent/UV impurities help with spectroscopic assays.
Bio/Cell culture grade: Low endotoxin/bioburden and documented trace metals; if intended for media preparation, confirm relevant quality attributes on the CoA.
Recommended QC upon receipt (practical tips):
Verify isotopic pattern by HRMS (look for +2.0067 Da vs unlabeled).
Confirm enantiomeric purity by chiral HPLC or Marfey’s analysis.
Assess water content by Karl Fischer if sensitive applications are intended.
Reaction and Applications
Key research uses leverage the dual 15N labels and the indole chromophore:
Stable-isotope tracing (general):
Metabolic flux analysis through the kynurenine and serotonin pathways; track 15N incorporation into downstream metabolites and nucleotides (literature).
Protein turnover studies: Incorporation of 15N into newly synthesized proteins enables 15N-HSQC NMR and global 15N-labeling experiments in microbes or cell-free systems.
Quantitative mass spectrometry: Internal standard for isotope-dilution LC–MS of tryptophan in biochemical matrices; the +2 Da shift (15N2) provides clear resolution from the unlabeled analyte (literature practice).
NMR spectroscopy:
15N direct detection and 1H–15N correlation (HSQC/HMQC) on the α-amino and indole nitrogens when appropriately protonated; useful for probing local environments, hydrogen bonding, and protonation states in peptides/proteins (literature).
Peptide/protein synthesis:
Use as a chiral building block to introduce site-specific 15N labels. Compatible with standard protecting groups (e.g., Fmoc on the α-amine; indole N typically left unprotected or transiently protected when required).
Photophysics/biophysics:
Exploit intrinsic indole fluorescence to monitor folding, binding, or microenvironment polarity; isotopic labeling does not perturb fluorescence significantly but facilitates orthogonal MS/NMR readouts.
Practical notes:
For MS standards, prepare gravimetrically in water or 0.1% formic acid and store aliquots at ≤−20 °C to prevent degradation (general guidance).
For biosynthetic incorporation, ensure nitrogen sources in media are controlled to maintain high atom% 15N in biomass.
Reaction Conditions
General literature guidance for transformations involving L-tryptophan and its protected derivatives (applicable to 15N2 analog with identical reactivity):
Peptide coupling (solution or SPPS):
Solvent: Dry DMF or NMP; DCM co-solvent for resin swelling in SPPS.
Reagents: HATU or HBTU (3–4 equiv), with DIPEA (4–6 equiv) relative to the incoming amine; or EDC·HCl (1.1–1.5 equiv) with HOAt/HOBt or NHS in aqueous/DMF.
Temperature/time: RT, 30–120 min per coupling cycle (SPPS) or 2–12 h in solution-phase; monitor by Kaiser/ninhydrin tests or LC–MS.
Expected outcomes: High conversion with minimal racemization when base is limited and reactions are kept at RT (literature best practice).
Indole electrophilic substitution:
Formylation (Vilsmeier–Haack): POCl3/DMF (0–25 °C), hours; C3-formyl tryptophan derivatives formed; protect α-amine (Fmoc/Boc) to avoid side reactions.
Halogenation: NBS/NIS (C3-selective) in DMF/AcOH at 0–25 °C; short reaction times (10–60 min) to limit overbromination.
N-Protection strategies:
α-Amine: Fmoc-OSu or Boc2O in dioxane/water with Na2CO3 (0–25 °C). Indole N typically unreactive under these conditions.
Indole N: Boc protection via (Boc)2O with catalytic DMAP in THF at RT–40 °C when needed.
Hydrolysis/deprotection:
Fmoc removal: 20% piperidine/DMF, RT, 10–20 min.
Boc removal: TFA/DCM (1:1 to neat TFA), RT, 0.5–2 h.
All values are literature/general conditions. Optimize stoichiometry, temperature, and time for your substrate and scale; confirm 15N retention by HRMS/NMR as needed.
Safety and Handling
GHS and hazard details are not provided for this item. Always consult the SDS for authoritative information.
GHS classification, signal word, pictograms, H-statements: Not specified for this item; refer to SDS.
General hazard profile (amino acid, literature): Low acute toxicity profile is typical for amino acids; handle as a laboratory chemical. Avoid dust formation and inhalation. Not known as a strong sensitizer; avoid contact and ingestion.
PPE: Lab coat, safety glasses, appropriate gloves (e.g., nitrile). Use a dust mask/respirator if handling large quantities of powder that may become airborne.
Handling: Work in a clean, dry environment to avoid moisture uptake and contamination that could affect isotopic enrichment or chiral purity. For spectroscopy or isotopic applications, avoid cross-contamination with unlabeled nitrogen sources.
Incompatibilities: Strong oxidizers may degrade the indole ring. Avoid prolonged exposure to strong acids/bases at elevated temperatures (can lead to decomposition/oxidation). Indole chromophore is light-sensitive—minimize strong UV exposure to limit photooxidation (general precaution).
First aid (general): If inhaled—move to fresh air. Skin/eye contact—rinse with water for at least 15 minutes; remove contaminated clothing. If ingested—rinse mouth and seek medical advice. Always follow institutional protocols.
Waste: Dispose of in accordance with local regulations. Minimally hazardous organic/biological laboratory waste stream is typical; verify with SDS.
Note: This product is for research use only.
Solvent Selection
L-tryptophan-15N2 is a zwitterionic, polar solid with pH-dependent solubility.
Polarity/miscibility (literature):
Water: Moderately soluble at neutral pH; solubility increases in acidic (e.g., 0.1 M HCl) or basic (e.g., 0.1 M NaOH) solutions due to ionization.
Alcohols: Poorly soluble in lower alcohols unless water is present.
Polar aprotics (DMF, DMSO): Generally soluble; often used to prepare stock solutions for coupling reactions or spectroscopy.
Aqueous biochemistry: Use water or buffer near pH 2–3 (to protonate the amine) or pH 9–10 (to deprotonate the carboxyl) to enhance solubility. For neutral pH stocks, dissolve first at slightly acidic pH, then titrate to target pH.
Peptide coupling: Dissolve in dry DMF/DMSO with base (e.g., DIPEA) and coupling reagent (e.g., HATU/HBTU/EDC); minimize water to prevent premature hydrolysis.
Spectroscopy (UV/fluorescence/NMR): Water, D2O (for NMR), or dilute acid; for 15N NMR/HSQC, deuterated aqueous buffers or DMSO-d6/CD3OD can be used as matrix-solvents.
Comparison to related amino acids (general): Among aromatic amino acids, tryptophan is the least soluble in pure water; phenylalanine and tyrosine show similar or slightly higher solubility profiles but lack the same indole fluorescence signature.
Tip: Warm gently (≤40 °C) and sonicate to aid dissolution; avoid strong heating which can accelerate oxidation of the indole moiety.
Shipping: Not specified for this item; refer to CoA/Spec Sheet.
Long-term handling (general best practice for indole-containing amino acids): Store tightly capped in a desiccator, protected from light to minimize slow oxidation of the indole ring. Keep container closed to avoid moisture uptake and isotopic dilution via adventitious ammonia.
Reconstitution:
Aqueous: Dissolve in purified water; if solubility is limited, acidify slightly (e.g., to pH 2–3 with HCl) or basify to pH 9–10 with NaOH, then adjust to the desired working pH. Filter-sterilize (0.22 µm) for cell culture/media uses.
Organic: For coupling chemistry, dissolve in dry DMF/DMSO; prepare immediately before use.
Solution stability (general): Aqueous solutions are best stored at 2–8 °C for short term (days) or aliquoted and frozen (≤−20 °C) for longer-term storage (weeks to months); minimize freeze–thaw cycles. Protect solutions from light.
Note: Where specific, item-level parameters (e.g., appearance, exact purity, isotopic enrichment, stabilizers) are required, consult the product’s CoA/Spec Sheet.
Structure and Identity
Isotopically labeled essential amino acid; L-tryptophan with both nitrogens as 15N (15N2).
SKU: L467009
Product name: L-Tryptophan-¹⁵N₂ (for research use only)
CAS: 204634-20-8; PubChem CID: 16217285
InChIKey (as provided): 298112
Molecular formula (backbone): C11H12N2O2 with two nitrogens as 15N (isotopolog-specific notation)
Molecular weight: ~206.23 g/mol (computed for 15N2 isotopolog; literature calculation: +2.0067 vs unlabeled L-Trp 204.23)
SMILES (literature, unlabeled backbone for L-tryptophan): NC@@HC(=O)O. Isotopic specification: both nitrogens correspond to 15N in this product.
Stereochemistry: L-configuration at the α-carbon (S absolute configuration).
Functional groups: α-amino (15NH2/15NH3+), α-carboxylate (CO2H/CO2−), indole ring with [15nH] pyrrolic nitrogen.
Structural features (2D description): An α-amino acid bearing an indole substituent on the β-carbon; the indole is a fused bicyclic (benzene + pyrrole) ring. The chiral center connects the amino group, carboxyl group, hydrogen, and a methylene tether to the indole.
Notes: Structural identifiers above (other than the InChIKey provided in Product Data) are literature/computed descriptions of the L-tryptophan scaffold; isotopic labeling is specific to both nitrogens.
Synthetic Utility
As a chiral, bifunctional building block with an indole side chain, L-tryptophan-15N2 offers multiple handles for synthesis while introducing 15N labels at both the α-amino and indole nitrogens.
Peptide synthesis: The α-amine (15N) couples readily via standard peptide coupling reagents (HATU/HBTU/TBTU, EDC/NHS). Fmoc protection of the α-amine is standard for SPPS; indole N is typically left unprotected but can be Boc-protected if required for harsh conditions.
Side-chain chemistry (indole): Electrophilic substitution predominantly at C3 (e.g., Vilsmeier formylation, Mannich reactions, halogenation) allows late-stage diversification of labeled frameworks. N-alkylation/acylation of the indole (on 15N) can position the isotopic label within target motifs for mechanistic probes.
Carboxylate transformations: Activation to acid chlorides, mixed anhydrides, or formation of active esters (e.g., NHS, pentafluorophenyl) enables coupling to amines, resins, or surfaces while retaining 15N labels.
Resolution/chirality: L-configuration provides a defined stereocenter for chiral transfer in syntheses; racemization risk during coupling is mitigated with mild bases and modern uronium reagents.
Isotope placement strategy: Dual 15N labeling allows differentiation of amine-derived versus ring-derived nitrogen in product mapping via MS/MS or NMR, enhancing mechanistic insight.
Tip: When indole N protection is applied (e.g., N-Boc), deprotect under mild acid (TFA) after coupling to avoid scrambling or decomposition; monitor by LC–MS to confirm 15N retention.
Target Specificity
Not an antibody or affinity reagent; no target specificity, epitope, clone, or isotype information applies to this product.
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