ATP-Ndilithium - ≥99% , CAS No.A1441269

CAS: A1441269 Cat. No.: A1441269 Fórmula: C₁₀H₁₄Li₂₁₅N₅O₁₃P₃ Peso molecular: 524.01

GRADE & PURITY ≥99%

Storage

Store at -20°C

Shipped In

Ice chest + Ice pads

Visão geral

ATP - 15 N 5 (Adenosine 5'-triphosphate- 15 N 5 ) dilithium is 15 N labeled ATP. ATP (Adenosine 5'-triphosphate) is a central component of energy storage and metabolism in vivo. ATP provides the metabolic energy to drive metabolic pumps and serves as a coenzyme in cells. ATP is an important endogenous signaling molecule in immunity and inflammation.

Specifications

Especificações e pureza

≥99%

Condições de armazenamento de armazenamento

Store at -20°C

Enviado em

Ice chest + Ice pads

Este produto requer transporte de cadeia fria. Serviços terrestres e outros serviços econômicos não estão disponíveis.

Pureza

≥99%

Nomes e identificadores

• Peso molecular: 524.01

Application Protocols

No manufacturer-validated application protocols are provided for SKU A1441269. Refer to standard literature and method-specific manuals for kinases, ligases, luciferase assays, and cell-free systems for protocol details. Always verify reagent concentration, metal cofactor balance (e.g., Mg2+), pH, and temperature for your assay before use.

Biological Roles

General/literature context (informational; not specific to this item’s performance):

• Central metabolite: ATP is the universal energy currency in cells, coupling catabolic and anabolic pathways via hydrolysis of its phosphoanhydride bonds.
• Phosphoryl donor: Serves as the γ-phosphate donor in kinase-catalyzed phosphorylation of proteins, lipids, and metabolites, modulating signaling pathways and enzyme activity.
• Nucleic acid metabolism: Precursor for RNA synthesis (as ATP/adenosine 5′-triphosphate) and indirectly for DNA via ribonucleotide reduction.
• Allosteric regulation: Acts as an allosteric effector for numerous enzymes and ion channels; ATP/ADP ratios integrate cellular energy status.
• Metal ion complexation: Intracellularly, ATP is largely present as Mg•ATP; metal complexation affects reactivity and enzyme recognition.

Note: The above biological functions describe ATP as a biomolecule. This product is provided strictly for research use only and is not intended for diagnostic or therapeutic use.

Buffer Applications

ATP is not a buffering agent per se, but it is routinely included in buffered reaction systems.

General/literature guidance:

• Typical working stocks: Prepare 10–100 mM in nuclease-free water. Adjust pH to ~7.0–7.5 if necessary after dissolution (monitor because phosphate ionization affects pH). Label as general guidance only; not a specification for this item.
• Reaction buffers: Common systems include Tris-HCl, HEPES, or MOPS (pH 7.0–8.0) with MgCl2 (often 5–20 mM) to form Mg•ATP for kinases and ligases.
• Ionic strength: Control Na+/K+/Li+ and Cl− levels to match enzyme requirements; excessive ionic strength can inhibit some ATP-dependent enzymes.
• Chelators: Avoid high EDTA when Mg•ATP is required; if chelators are present, ensure free Mg2+ exceeds total ATP.

Not typically applicable: ATP does not serve as a pH buffer for preparative chromatography or cell culture media; see Reaction & Applications for its functional roles in enzyme systems.

Green Alternatives

Green chemistry considerations for ATP salts are atypical because ATP is itself a highly specific biochemical reagent rather than a commodity solvent or reagent with interchangeable greener substitutes.

• Substitution potential: There are no direct “green” replacements for ATP in ATP-dependent enzymatic processes. The molecule is required mechanistically (e.g., kinase γ-phosphate donor, ligase cofactor).
• Greener practice strategies (literature):
  • Use minimal effective concentrations and microscale assay formats to reduce material and waste.
  • Optimize buffer systems to extend solution stability, limiting the need for repeated preparations and disposal.
  • Employ recyclable energy regeneration systems (e.g., phosphocreatine/creatine kinase, PEP/pyruvate kinase) in cell-free reactions to minimize total ATP consumption.
  • Select counterion forms (Li+, Na+) based on downstream environmental and biological compatibility; avoid unnecessary heavy-metal additives.

Comparison (informational):

• ATP (Li+ or Na+ salts) vs analogs (e.g., nonhydrolyzable ATPγS): Analog use may reduce turnover in mechanistic studies but is not a greener replacement—rather a functional probe with different fate and disposal considerations.

Waste and disposal: Aqueous ATP solutions are typically disposed as nonhazardous lab aqueous waste unless contaminated; follow institutional and local regulations.

Pharmaceutical Uses

This product is offered for research use only.

General/literature context (informational):

• ATP salts are not commonly used as excipients in pharmaceutical formulations due to chemical lability (hydrolysis) and strong anionic character.
• Specialized uses in manufacturing or analytical development may include ATP as a reagent for enzyme assays, bioluminescent microbial monitoring (ATP assays), or process analytics, but not as a therapeutic agent or excipient.

No pharmacopeial status, excipient role, or GMP applicability is specified for this item; refer to your quality unit and the CoA/Spec Sheet if regulated-use evaluation is contemplated.

Physical Properties

Item-specific specifications (this lot): Not specified for this item; refer to CoA/Spec Sheet.

General/literature characteristics for ATP salts (informational only):

• Physical form: Typically a white to off-white, hygroscopic solid when isolated as alkali metal salts; commonly supplied as lyophilized powder.
• Solubility (literature): Highly soluble in water; practically insoluble in nonpolar organic solvents. Forms complexes with Mg2+ and other divalent cations in aqueous media.
• pKa values (literature, indicative): Multiple phosphate pKa values spanning strongly acidic to near-neutral regime; net charge is strongly negative at physiological pH due to deprotonated phosphate groups.
• Partitioning (literature): Extremely low logP; behaves as a highly polar, polyanionic species.
• UV absorbance (literature): Strong absorption at ~259–260 nm due to adenine chromophore; useful for quantitative determination in aqueous buffers.
• Hygroscopicity (literature): Alkali ATP salts may absorb moisture and CO2; solutions are susceptible to hydrolysis of phosphoanhydride bonds at elevated temperature or extreme pH.

Notes

• Do not construe the above as product specifications. For exact appearance, assay, water content, counterion content, and UV profile for SKU A1441269, consult the CoA/Spec Sheet for the specific lot.

Quality and Grades

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

Interpreting grades for ATP salts (general guidance):

• Enzyme-grade/biochemical grade: Emphasizes low levels of nucleases, phosphatases, and metal contaminants that could degrade ATP or interfere with enzymatic assays. Often includes tight specifications for pH, counterion content, and UV purity at 260 nm.
• Cell-free transcription/translation grade: May specify stringent limits on RNase/DNase/protease and provide performance criteria in coupled assays.
• HPLC grade (when stated for nucleotides): Indicates high chromatographic purity and low UV-absorbing impurities.

What to check on the CoA/Spec Sheet for ATP–dilithium:

• Assay (%), identity (HPLC or LC–MS), inorganic phosphate content, pH of a defined solution, water content (Karl Fischer), residual solvents, and counterion (Li+) assay.
• Functional tests (if provided): e.g., kinase reaction support or luciferase activity retention.
• Stabilizers: Presence/absence not specified for this item; refer to CoA/Spec Sheet. Some ATP preparations include trace stabilizers or are adjusted to defined counterion ratios; implications for enzyme compatibility should be evaluated experimentally.

Reaction and Applications

This product serves as a biochemical reagent rather than a traditional organic reaction solvent or building block. Key research applications (literature, informational):

• Enzymatic phosphorylation: Cofactor/substrate for kinases transferring the γ-phosphate to proteins, lipids, sugars, and small molecules.
• Nucleic acid manipulation: Required for ligases (e.g., T4 DNA ligase) and certain helicases, topoisomerases, and motor proteins in in vitro assays.
• Cell-free systems: Energy source for transcription–translation extracts; often used with energy-regeneration systems (e.g., phosphocreatine/creatine kinase).
• Bioluminescent assays: Substrate for luciferase-based ATP assays and reporter systems; ATP concentration directly modulates signal output.
• Chemical biology: Drives ATP-dependent labeling (e.g., kinome profiling, activity-based probes) and supports ATP-dependent chaperones and proteases in reconstituted systems.

Practical tips (literature):

• Metal ion coordination: Most ATP-dependent enzymes require Mg•ATP; typical free Mg2+ is maintained slightly above ATP concentration to ensure complex formation.
• pH and temperature: Maintain pH ~7–8 and avoid prolonged exposure above ambient temperature to limit hydrolysis to ADP/AMP and Pi/PPi.
• Stock handling: Prepare concentrated stocks (e.g., 10–100 mM) in nuclease-free water; aliquot, snap-freeze, and store at −20 °C or below to reduce freeze–thaw.
• Purity monitoring: UV at 260 nm and HPLC can track degradation (ADP/AMP peaks). Inorganic phosphate assays can reveal hydrolysis during storage.

Note: The above are general literature practices; verify compatibility and performance with your specific assay system.

Reaction Conditions

General literature guidance for ATP-dependent reactions (informational; not item-specific specifications):

• Kinase assays:
  • Solvent/buffer: Tris-HCl or HEPES, pH 7.0–8.0.
  • Cofactor: MgCl2 typically 5–20 mM to generate Mg•ATP; free Mg2+ often maintained slightly above ATP concentration.
  • Temperature: 20–37 °C.
  • ATP concentration: Commonly 10–1000 µM in analytical assays; up to several mM in preparative biocatalysis, depending on Km and desired velocity.
  • Time: Minutes to hours; monitor conversion by LC–MS, radiometric assays, or ADP-coupled enzyme assays.
• DNA/RNA ligation:
  • Buffer: Manufacturer-specified ligase buffers (often include Tris, Mg2+, DTT) with ATP provided exogenously when not pre-included.
  • ATP concentration: Typically 0.1–1 mM.
  • Temperature: 16 °C (sticky-end ligation) to room temperature; time from 10 min to overnight.
• Cell-free protein synthesis:
  • System buffers proprietary/defined; ATP supplied at 1–5 mM with energy regeneration systems (e.g., phosphocreatine + CK).

Monitoring and controls:

• Track ATP/ADP/AMP by HPLC or capillary electrophoresis; UV at ~260 nm for quantitation (literature).
• Avoid metal contaminants (Fe3+, Cu2+) that may catalyze degradation; use nuclease-free, chelex-treated or high-purity water if needed.

These conditions are typical from literature and method manuals; optimize for your specific enzyme and substrate set.

Safety and Handling

Item-specific hazard classification: Not specified for this item; refer to the SDS for authoritative information.

General safety guidance for nucleotide triphosphate salts (informational only):

• GHS/Regulatory: Many nucleotide salts are not classified as hazardous under GHS when used in typical lab quantities; however, always verify the SDS for this specific product/lot.
• Potential hazards: Low acute toxicity expected; dust may cause mechanical eye/respiratory irritation. Avoid inhalation of powders and contact with eyes.
• PPE: Lab coat, safety glasses, and disposable nitrile gloves recommended. Handle powders in a fume hood or ventilated enclosure to minimize dust.
• Incompatibilities: Strong oxidizers and strong acids/bases may promote degradation (hydrolysis of phosphoanhydride bonds). Avoid prolonged exposure of aqueous solutions to elevated temperature or metal contaminants unless intended (e.g., Mg2+ for enzymatic use).
• Special risks: None known for lithium counterions at typical reagent quantities; nevertheless, avoid ingestion and environmental release.
• First aid (general):
  • Inhalation: Move to fresh air; seek medical attention if symptoms persist.
  • Eye contact: Rinse cautiously with water for several minutes; remove contact lenses if present; seek medical attention if irritation continues.
  • Skin contact: Wash with soap and water; seek medical advice if irritation develops.
  • Ingestion: Rinse mouth; seek medical attention if unwell.
• Fire safety: Organic solid; use water spray, CO2, or dry chemical. Combustion may produce nitrogen oxides and phosphorus oxides.

Always defer to the product’s SDS for definitive hazard statements, pictograms, and response measures.

Solvent Selection

ATP–dilithium is a highly polar, polyanionic nucleotide salt; solvent choice centers on maintaining solubility and stability.

• Primary solvent: Water or aqueous buffers (literature). Typical working stocks are prepared in nuclease-free water or Tris/HEPES buffers.
• Miscibility/compatibility (literature):
  • Water: Freely soluble.
  • Alcohols: Limited stability and potential precipitation at high alcohol content; avoid unless necessary.
  • Nonpolar solvents (e.g., ethers, hydrocarbons): Essentially insoluble.
• Buffer considerations (literature):
  • Mg2+: Many ATP-dependent enzymes require Mg•ATP complex; include MgCl2 (commonly 5–20 mM) in reaction buffers as appropriate.
  • pH: Maintain near-neutral pH (approx. 7–8) to limit hydrolysis; avoid strong acids/bases.
  • Counterions: Lithium counterions generally do not interfere with most enzymes, but final ionic strength and cation composition should be optimized per application.

When to choose water vs buffer (literature):

• For long-term stock solutions, nuclease-free water at neutral pH minimizes buffer-derived salt accumulation; adjust pH if needed after dissolution.
• For immediate enzymatic use, dissolve directly in the reaction buffer to reduce dilutions and pH shifts.

Comparators:

• Trisodium ATP, disodium ATP: More common alternatives with similar solubility; choice often driven by total Na+/Li+ load, osmolarity, and enzyme compatibility.

Storage and Reconstitution

Item-specific instructions:

• Storage conditions: Store at −20 °C (per product data). Minimize light and moisture exposure by keeping the container tightly closed. Shipped in an ice chest with ice pads.
• Stabilizers/pH: Not specified for this item; refer to CoA/Spec Sheet.

General/literature guidance for ATP salt handling (informational):

• Reconstitution: Dissolve in nuclease-free water to prepare a stock (e.g., 10–100 mM). Check and, if necessary, adjust pH to ~7.0–7.5 at working concentration. Filter-sterilize (0.22 µm) if sterility is required. Avoid repeated freeze–thaw cycles by dispensing single-use aliquots.
• Storage of solutions: Store aliquots at −20 °C or below. ATP in aqueous solution is susceptible to hydrolysis; consider preparing fresh working solutions on the day of use. For extended storage, snap-freeze aliquots (e.g., liquid nitrogen or dry-ice/ethanol bath) before transfer to −80 °C.
• Stability considerations: Avoid metal contamination unless intended (Mg2+). Maintain near-neutral pH; strong acid/base accelerates hydrolysis to ADP/AMP and inorganic phosphate.

Research use note: For research use only. Not for human or veterinary use.

Structure and Identity

Short description: ATP–dilithium is the lithium salt form of adenosine 5′-triphosphate (ATP), a nucleotide consisting of adenine (purine), D-ribose, and a 5′-triphosphate chain; two lithium cations balance a portion of the anionic phosphate charge.

• Item-specific identifiers
  • CAS: A1441269 (catalog placeholder). Not specified for this item; refer to CoA/Spec Sheet.
  • InChIKey: Not specified for this item; refer to CoA/Spec Sheet.
  • 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 identity (for ATP core, informational only)
  • Core entity: Adenosine 5′-triphosphate (ATP)
  • Typical free-acid formula (literature): C10H16N5O13P3 (counterions not included). The dilithium salt contains two Li+ counterions associated with the phosphate groups (literature).
• Structural features (descriptive)
  • Nucleoside: Adenine fused bicyclic purine base (6-aminopurine) N9-glycosidically linked to D-ribofuranose.
  • Phosphate chain: Three phosphate units linked by two phosphoanhydride bonds (α–β and β–γ) and one phosphoester bond to the 5′-hydroxyl of ribose.
  • Ionization: Multiple ionizable phosphate oxygens; at neutral pH ATP exists as a highly anionic species that can coordinate Mg2+ and other cations (literature).
  • Stereochemistry: D-ribose retains natural stereochemistry at C1′–C4′; no chiral centers in the phosphate chain.
• 2D structure in words: Adenine ring attached via N9 to the anomeric carbon of a five-membered ribose ring; the ribose C5′ extends to an O–P(=O)(O−)–O–P(=O)(O−)–O–P(=O)(O−) chain, with Li+ counterions associating with phosphate oxygens (literature).

Synthetic Utility

While ATP–dilithium is primarily a biochemical cofactor, it has niche utility in synthesis and chemical biology (literature, informational):

• Enzymatic synthesis/enzyme-mediated transformations: Used to drive ATP-dependent ligations (e.g., peptide ligases, DNA/RNA ligases), phosphorylations (protein, peptide, small-molecule), and activation steps (adenylation) in biocatalytic cascades.
• Chemical phosphorylation: ATP can act as a phosphoryl donor in some purely chemical systems under activating conditions, but dedicated phosphorylating reagents (e.g., POCl3-derived reagents, phosphoramidites) are typically preferred for synthetic robustness.
• Affinity probes: Acts as a scaffold for designing ATP analogs (e.g., ATP-γS, ATP-biotin) used to interrogate kinases and ATP-binding proteins; the native ATP salt can serve as a control in such studies.
• Energy coupling: Provides thermodynamic driving force in in vitro metabolic engineering pathways and cell-free biosynthesis modules.

Practical considerations:

• Counterions: Lithium vs sodium counterions rarely alter enzymatic specificity but change ionic strength; adjust buffer composition accordingly.
• Stability: Protect from high temperatures and extreme pH; monitor for ADP/AMP formation by HPLC when reactions are extended.

Target Specificity

Not applicable to this product type. No antigen/epitope, clone, isotype, or species reactivity data are provided for SKU A1441269. This is a small-molecule biochemical reagent rather than an antibody or affinity reagent.