ACTH-(11-24), Antagonist of MC 2 receptor, CAS No.rp173377, Antagonist of MC 2 receptor

CAS: rp173377 Cat. No.: rp173377
Disponibile su ordine
GRADE & PURITY Moligand™ ? Moligand™ — Aladdin's line of ligands and bioactive small molecules. Use for receptor, pathway, and binding studies needing defined small-molecule tools.
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Size
Germania (EU)
USA*
Price
Qty
500μg
rp173377-500μg
Su ordinazione · 8–12 settimane
2.082,49€
1mg
rp173377-1mg
Su ordinazione · 8–12 settimane
3.470,87€
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Why this grade

Moligand™ Moligand™ for sensitive chromatographic and analytical workflows requiring minimal baseline interference.

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Storage & shipping

Room temperature Ships Check lot-specific COA for exact specifications.

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Quality documents

SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.

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Literature proof

Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.

Specifications

Product Name
ACTH-(11-24), Antagonist of MC 2 receptor, CAS No.rp173377
Sinonimi
ACTH (11-24) | adrenocorticotropic hormone (11-24)
Grado
Moligand™
Specifiche e purezza
Moligand™
Tipo di azione
ANTAGONIST
Meccanismo d'azione
Antagonist of MC 2 receptor
CAS
rp173377
Tipo di molecola
Peptidi
Stoccaggio e spedizione
Condizioni di conservazione di stoccaggio
Room temperature

Documentazione

📋 Safety Data Sheet (SDS)

Comprehensive hazard, handling, storage, and regulatory compliance document.

Download SDS →

✅ Certificate of Analysis (COA)

Lot-specific quality data. Enter your lot number to retrieve the exact COA.

Look up COA →

📊 Datasheet

Quick-reference summary of product specifications and applications.

View datasheet →

🔬 Specification Sheet

Full quality attributes and acceptance criteria for this grade.

View spec sheet →

Advanced Data

Taxonomic Classification

Taxonomy Tree

KingdomOrganic compounds
SuperclassOrganic Polymers
ClassePolypeptides
SubclassNot available
Intermediate Tree Nodes Not available
Direct ParentPolypeptides
Alternative Parents Peptides  Valine and derivatives  Proline and derivatives  N-acyl-L-alpha-amino acids  Alpha amino acid amides  Amphetamines and derivatives  Pyrrolidinecarboxamides  Pyrrolidine carboxylic acids  N-acylpyrrolidines  1-hydroxy-2-unsubstituted benzenoids  N-acyl amines  Tertiary carboxylic acid amides  Secondary carboxylic acid amides  Amino acids  Guanidines  Propargyl-type 1,3-dipolar organic compounds  Monocarboxylic acids and derivatives  Azacyclic compounds  Carboximidamides  Carboxylic acids  Carbonyl compounds  Monoalkylamines  Organic oxides  Hydrocarbon derivatives  
Molecular FrameworkAromatic heteromonocyclic compounds
Substituents Polypeptide - Alpha peptide - N-acyl-alpha-amino acid - N-acyl-l-alpha-amino acid - N-acyl-alpha amino acid or derivatives - Proline or derivatives - Valine or derivatives - Alpha-amino acid amide - Amphetamine or derivatives - Alpha-amino acid or derivatives - N-substituted-alpha-amino acid - Pyrrolidine carboxylic acid or derivatives - Pyrrolidine-2-carboxamide - N-acylpyrrolidine - Pyrrolidine carboxylic acid - 1-hydroxy-2-unsubstituted benzenoid - Phenol - Fatty acyl - Monocyclic benzene moiety - N-acyl-amine - Fatty amide - Benzenoid - Pyrrolidine - Tertiary carboxylic acid amide - Amino acid or derivatives - Amino acid - Carboxamide group - Guanidine - Secondary carboxylic acid amide - Azacycle - Organoheterocyclic compound - Organic 1,3-dipolar compound - Carboxylic acid derivative - Carboxylic acid - Propargyl-type 1,3-dipolar organic compound - Carboximidamide - Monocarboxylic acid or derivatives - Amine - Organic oxide - Carbonyl group - Hydrocarbon derivative - Organic nitrogen compound - Primary aliphatic amine - Organic oxygen compound - Primary amine - Organooxygen compound - Organonitrogen compound - Aromatic heteromonocyclic compound
DescrizioneThis compound belongs to the class of organic compounds known as polypeptides. These are peptides containing ten or more amino acid residues.
External Descriptors Not available
Obiettivi associati (umani)
MC2R Tclin Adrenocorticotropic hormone receptor (0 Activities)
Activity TypeActivity Value -log(M)Mechanism of ActionActivity ReferencePublications (PubMed IDs)
Certificati (CoA, COO, BSE/TSE e tabella di analisi)
C of A & Other Certificates(BSE/TSE, COO):
Analytical Chart:
Informazioni genetiche
Alternate NamesACTH (11-24) | adrenocorticotropic hormone (11-24)
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
Calcolatori di soluzioni
Recensioni

Recensioni dei clienti

Application Protocols

Item-specific, validated application protocols were not provided for this product. Below are general, literature-informed procedures to guide use; adjust to your system and consult the CoA for exact concentration calculations.

General dissolution and stock preparation:

  • Allow vial to equilibrate to room temperature in a desiccator before opening.
  • For initial dissolution, add water or 0.1% HCl to achieve 1–10 mM stock; vortex and sonicate gently if needed. Alternatively, dissolve in DMSO and dilute into buffer.
  • Filter through 0.22 µm if assay permits. Aliquot to avoid repeated freeze–thaw.

Receptor/cell-based assay example (outline):

  • Prepare serial dilutions (e.g., 10-point, 1:3) in assay buffer with 0.1% BSA.
  • Incubate with receptor-expressing cells or membrane preparations per platform SOP (e.g., 30–60 min at 37 °C for binding; signal readout per reporter system).
  • Include vehicle and known reference controls.

SPR/BLI binding assay example (outline):

  • Immobilize receptor ectodomain or capture tag on chip/sensor.
  • Inject peptide concentrations spanning anticipated KD (e.g., 0.1–10× KD range) in HEPES-buffered saline with surfactant.
  • Fit association/dissociation to a 1:1 or appropriate kinetic model.

Analytical QC check:

  • Verify identity by LC-MS and purity by analytical RP-HPLC upon receipt when critical to your study.

These protocols are guidance only; optimize parameters for your assay and instrumentation.

Biological Roles

Context (literature, biochemical):

  • Origin: ACTH is a pituitary-derived polypeptide (typically 39 aa) produced from the POMC precursor. The 11–24 region lies within the central basic domain implicated in receptor interaction.
  • Receptor interactions: ACTH engages melanocortin receptors; the 11–24 segment contributes to recognition of the melanocortin 2 receptor (MC2R) and potentially modulates binding affinity/efficacy in conjunction with other ACTH regions. Isolated fragments are valuable to dissect which residues drive binding versus activation.
  • Physicochemical features: The fragment is rich in Lys/Arg, conferring a high positive charge at physiological pH, promoting electrostatic interactions with acidic receptor or membrane regions. Proline residues may introduce conformational constraints affecting receptor docking.
  • Experimental utilities: Fragment-based mutagenesis and truncation studies map determinants of signaling bias, potency, and selectivity across melanocortin receptor subtypes. The Tyr residue offers an intrinsic chromophore/fluorophore for spectroscopic monitoring.
  • Stability/metabolism: In biological matrices, short peptides can be susceptible to endo- and exopeptidases; N- or C-terminal capping, D-residue substitutions, or backbone modifications (e.g., PEGylation, stapling) are common tactics to study stability without altering key binding hotspots. Item-specific modifications, if any, are Not specified for this item; refer to CoA/Spec Sheet.

Note: This information is provided for fundamental biochemical context relevant to research use. No medical/clinical claims are made or implied.

Buffer Applications

Direct use as a buffer is not applicable. ACTH-(11–24) is a peptide tool compound rather than a buffering agent.

Practical guidance for working solutions (literature, peptide-centric):

  • Preparation: Dissolve initially in water or a small volume of dilute acid (e.g., 0.1% HCl or TFA), then dilute into your target buffer (e.g., PBS, HEPES, or Tris) while monitoring for precipitation.
  • pH considerations: Maintain pH 6–7.5 for most assays to keep the peptide protonated and soluble; avoid strong base to limit degradation.
  • Ionic strength: 100–300 mM NaCl can reduce nonspecific adsorption to plastics and experimental surfaces due to the peptide’s high positive charge.
  • Filtration: If assay permits, sterile-filter through 0.22 µm after dissolution to remove particulates.
  • Storage of working solutions: Short-term at 2–8 °C; for longer storage, aliquot and freeze at −20 to −80 °C to minimize degradation (general guidance; item-specific storage is room temperature for the dry material as provided).

If your application requires a defined buffer recipe (e.g., for receptor binding or spectroscopy), choose the system compatible with your detection method (phosphate for UV, HEPES for fluorescence) and verify peptide stability empirically.

Green Alternatives

Peptide handling is primarily aqueous, allowing inherently greener workflows compared with many small-molecule operations. Where organic solvents are needed (e.g., to disrupt aggregates or in analytics), consider the following greener-alternative strategies.

Greener choices and trade-offs (literature guidance):

  • Primary dissolution in water or buffered saline rather than neat organic solvents whenever feasible.
  • Use ethanol or isopropanol for surface wetting steps instead of HFIP where compatible; note reduced efficacy for breaking strong peptide aggregates compared to HFIP.
  • Replace TFA with formic acid (FA) in LC-MS when possible to improve ionization and reduce corrosivity; acknowledge that FA can give slightly worse chromatographic peak shape for very basic peptides versus TFA.

Comparison snapshot:

  • Water/buffer: Lowest environmental impact; excellent biocompatibility; limited ability to disrupt stubborn aggregates.
  • Formic acid (0.1% in water/ACN): Greener than TFA for MS; potential trade-off in chromatographic performance.
  • Acetonitrile vs methanol: Methanol is generally greener but can alter retention/selectivity; for peptide LC, ACN is often necessary for resolution—optimize gradients to minimize consumption.

Operational practices:

  • Minimize solvent volumes via microscale dissolution and high-concentration stocks followed by on-instrument dilution.
  • Implement solvent recycling for LC mobile phases when permitted by method robustness.
  • Prefer ambient-temperature processes; avoid lyophilization repetitions that increase energy use unless purity/stability requires it.
Pharmaceutical Uses

This product is for research use only (from Product Data) and is not intended for human or veterinary use.

Formulation roles in research and development (general, non-clinical):

  • Reference standard or positive control peptide in assay development (e.g., receptor binding, signaling readouts) to benchmark potency and system responsiveness.
  • Process development surrogate: Short peptides like ACTH fragments are used to develop and validate analytical methods (HPLC, LC-MS, capillary electrophoresis) and manufacturing unit operations (dissolution, filtration, lyophilization) before transitioning to production candidates.
  • Excipients/interactions: When formulating peptide solutions for research, common excipients include isotonic salts (NaCl), stabilizing sugars (trehalose, sucrose), bulking agents for lyophilization (mannitol), and antioxidants where compatible (e.g., methionine or ascorbate—note Tyr can also undergo oxidation; evaluate case-by-case).
  • Regulatory status: No pharmacopeial monograph is implied by the Moligand™ designation. Any cGMP or clinical application would require material that meets appropriate regulatory standards; this product is not supplied for such uses.

Practical note: Determine the peptide’s exact salt form and water content from the CoA to compute accurate dosing concentrations during non-clinical method development.

Physical Properties

Item-specific physical constants:

  • Appearance: Not specified for this item; refer to CoA/Spec Sheet.
  • Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
  • Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
  • Melting point, boiling point, density, refractive index, UV cutoff, residual solvent/metals: Not specified for this item; refer to CoA/Spec Sheet.

Literature/computed characteristics for the ACTH-(11–24) peptide motif (informational):

  • Typical sequence: KPVGKKRRPVKVYP (14 residues); calculated properties depend on terminal capping and salt form.
  • Charge state (literature): Strongly basic; at neutral pH, multiple Lys/Arg side chains are protonated, leading to a net positive charge (often +5 to +7 depending on termini and ionic strength).
  • Isoelectric point (pI, literature estimate): High pI, commonly in the ~11–12 range for Lys/Arg-rich 14-mers.
  • Solubility (literature): Generally soluble in water and aqueous buffers; initial dissolution may be aided by small volumes of dilute acid (e.g., 0.1% TFA or HCl) or by DMSO, then dilution into buffer. Hydrophobic contributions from Val/Tyr can reduce solubility at high concentrations or high ionic strength.
  • Hygroscopicity: Peptides can be hygroscopic and may absorb atmospheric moisture, altering apparent mass and concentration.
  • Optical activity: Peptides of L-residues are optically active; specific rotation is sequence- and solvent-dependent (not specified for this item).

Practical note: Because exact salt form (e.g., TFA, acetate), terminal modifications, and water content strongly affect mass and solubility, rely on the item’s CoA for definitive values.

Quality and Grades

Item-specific grade:

  • Grade/Purity: Moligand™ (from Product Data)

Interpretation and implications:

  • Moligand™ (general description): Denotes suitability for ligand- and target-interaction studies in discovery workflows (e.g., receptor binding, signaling pathway interrogation, screening). While this branding highlights research utility, it is not a pharmacopeial or clinical grade.
  • Documentation: Exact purity (HPLC area %), identity confirmation (MS, HRMS, peptide mapping), counter-ion content (e.g., TFA vs acetate), water/volatile content, and residual solvents are critical for peptides but are Not specified for this item; refer to CoA/Spec Sheet.
  • UV characteristics: For HPLC/UPLC monitoring of peptides, low baseline drift and defined chromatographic behavior are expected of screening-grade materials; item-specific UV cutoff/absorbance is Not specified for this item.
  • Lot-to-lot considerations: Peptide lots can vary in salt content and hydration; always normalize concentrations by mass balance with accurate MW from the CoA, or by amino acid analysis when precision is critical.
  • Impurities typical of peptide manufacture (general): Sequence deletions, truncations, oxidized Tyr/Met (Met not present in this fragment), diastereomers/epimerization at sensitive residues (e.g., during coupling), and residual protecting group traces. Moligand™-grade items are intended to minimize such impurities to levels acceptable for discovery research; verify acceptability for your application.

Use case alignment:

  • Recommended for biochemical assays, binding studies, and as a tool compound in peptide SAR. Not intended for clinical or diagnostic use.
Reaction and Applications

Applicability focus: As a bioactive peptide fragment, ACTH-(11–24) is primarily used as a tool compound rather than as a classical synthetic reagent.

Research applications (literature context):

  • Melanocortin receptor studies: Used to probe sequence determinants of melanocortin receptor (e.g., MC2R) recognition and downstream signaling in cell-based or biochemical assays.
  • Structure–activity relationship (SAR): Systematic substitution (Ala-scan, D-amino acid scans) within the 11–24 region helps map critical residues for binding/activation.
  • Receptor binding/competition assays: Labeled or unlabeled ACTH fragments are used to displace radioligands/fluorescent probes, providing Ki/IC50 data.
  • Conformation and aggregation: The Lys/Arg-rich sequence tends to be soluble; proline introduces local rigidity. CD or NMR studies in aqueous media can assess secondary structure propensities.
  • Analytical calibration: Serves as a positive control peptide in LC-MS method development (peptide mapping, retention behavior for basic peptides) and as a QC spike-in standard where appropriate.

Practical tips:

  • Prepare fresh working solutions; filter through 0.22 µm if assay permits to remove particulates/aggregates.
  • For SPR/BLI, minimize nonspecific electrostatic binding by adding salt (e.g., 150–300 mM NaCl) and low levels of surfactant; adjust pH to remain below peptide pI to keep it cationic and soluble.
  • For fluorescence-based assays, consider Tyr intrinsic fluorescence; control for inner-filter effects at higher concentrations.

Note: Manufacturer application specifics were not provided for this item; tailor protocols to your platform and confirm peptide identity/purity via the CoA.

Reaction Conditions

As a finished peptide, ACTH-(11–24) is not typically used in small-molecule reactions. However, literature provides general conditions relevant to peptide manipulation and assay deployment.

Peptide derivatization (general guidance):

  • NHS-ester labeling (e.g., fluorescent dyes, biotin): pH 7.5–8.5 in bicarbonate or phosphate buffer; 1.1–5 equiv of dye per accessible amine; 30–120 min at room temperature; protect from light; quench with Tris or ethanolamine; purify by RP-HPLC.
  • Maleimide coupling: Requires a free cysteine—none is present in the typical ACTH-(11–24) sequence; introduce Cys by design if thiol-selective conjugation is needed.
  • Reductive amination on N-terminus: Conduct in aqueous buffer with aniline catalyst and NaBH3CN at pH ~6.0–6.5; monitor by LC-MS.

Assay deployment:

  • Receptor/cell assays: Prepare stock at 1–10 mM in water or DMSO; dilute into assay medium to nM–µM working concentrations. Include carrier protein (0.1% BSA) if adsorption is observed.
  • Biophysical binding (SPR/BLI): Running buffer e.g., 10 mM HEPES, 150–300 mM NaCl, 0.005–0.05% surfactant; temperature 20–25 °C; regenerate surfaces with mild salt/acid as compatible with ligand.

SPPS context (if synthesizing analogs):

  • Fmoc/tBu strategy, HBTU/HATU or DIC/Oxyma couplings, 3–5 eq amino acid, DMF or NMP solvent, 5–20 min microwave-assisted or 30–60 min room temperature per coupling; final cleavage TFA cocktails 1–3 h at room temperature. These are literature norms and should be optimized per sequence.

Note: The above are general conditions; item-specific reactivity data are not provided.

Safety and Handling

Item-specific hazard data (from Product Data):

  • GHS classification, signal word, pictograms, H-statements: Not specified for this item; refer to SDS.

General laboratory safety for research peptides (informational, defer to SDS):

  • Expected hazards: Low volatility solid; primary risks are dust inhalation, skin/eye contact, and allergic sensitization in susceptible individuals. Avoid aerosolization when opening vials.
  • PPE: Lab coat, safety glasses, and suitable gloves (e.g., nitrile). Use a fume hood or ventilated enclosure during weighing to minimize dust.
  • Handling: Use clean, dry tools. Minimize freeze–thaw and repeated opening to avoid moisture uptake and contamination. When reconstituting, use sterile, filtered solvents if sterility is required for bioassays.
  • Incompatibilities: Strong oxidizers can degrade peptides; avoid prolonged exposure to basic solutions (risk of deamidation/epimerization) and to light/air for aromatic residues (e.g., Tyr oxidation). Metal ions may catalyze oxidation; include metal chelators only if compatible with your assay.
  • First aid (overview): If inhaled, move to fresh air; if on skin/eyes, rinse with water for 15 minutes; if ingested, rinse mouth with water. Seek medical attention as per institutional procedures. Bring SDS to healthcare provider.
  • Spill/cleanup: Avoid creating dust. Gently sweep or HEPA vacuum; wipe with damp disposable towels. Dispose according to institutional and local regulations.

Always consult the product’s SDS for authoritative hazard and response information.

Solvent Selection

Profile and miscibility (peptide-focused):

  • Polarity: Highly polar, cationic at neutral pH due to multiple Lys/Arg residues.
  • Preferred solvents (literature guidance):
    • Water or aqueous buffers (e.g., PBS, HEPES) are first-line once dissolved.
    • Acidified water (e.g., 0.1% HCl or TFA) can aid initial wetting/protonation for stubborn solids.
    • DMSO can be used to prepare concentrated stocks for subsequent aqueous dilution; check assay tolerance.
    • Minimal HFIP or acetonitrile/water with 0.1% TFA may help disrupt aggregates before dilution (analytical contexts).

Selection tips:

  • Start with small-volume pre-wet in water or 0.1% acid, vortex, then stepwise dilute into your assay buffer to avoid precipitation.
  • Maintain ionic strength and pH consistent with the peptide’s high pI; near-neutral buffers keep the peptide cationic and generally soluble.
  • Avoid strong base; prolonged exposure can cause backbone or side-chain modifications.

Comparison to alternatives:

  • Short basic peptides similar to ACTH-(11–24) typically show better solubility profiles than hydrophobic fragments; nonetheless, Tyr and Val content can cause aggregation at high concentrations. If persistent aggregation occurs, include 5–20% acetonitrile or small amounts of DMSO during initial dissolution, then dilute.

Compatibility:

  • Compatible with most aqueous biochemical assays, SPR/biolayer interferometry (BLI) running buffers, and LC-MS mobile phases (water/ACN with 0.1% FA/TFA) after appropriate filtration. Verify surfactant or solvent tolerance for cell-based systems.
Storage and Reconstitution

Item-specific storage and shipping:

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

General best practices for peptides (informational, without contradicting item data):

  • Dry material: Keep tightly closed in the original container, protected from moisture and light. If long-term storage is required, consider transferring to a desiccator with inert atmosphere. Many laboratories store peptides at 2–8 °C or −20 °C for extended periods; however, this item is indicated for room-temperature storage—follow the label and CoA.
  • Reconstitution: Use sterile water, dilute acid (e.g., 0.1% HCl), or assay buffer. To aid dissolution, pre-wet with a minimal volume, vortex, and, if necessary, briefly sonicate. Avoid strong base.
  • Working solution stability: For short-term use (hours to days), store at 2–8 °C. For longer-term storage, aliquot and freeze at −20 to −80 °C to avoid multiple freeze–thaw cycles. Include cryoprotectants (e.g., 10–20% glycerol) if compatible with your assay.
  • Concentration determination: Calculate using the exact MW and salt form from the CoA. Where accuracy is critical, confirm by UV absorbance using Tyr (ε280 ~1490 M−1 cm−1, literature, assuming free Tyr), or by amino acid analysis.
  • Thawing: Thaw on ice or at room temperature; mix gently to avoid foaming. Discard aliquots showing precipitation or contamination.

Always consult the product label and CoA/SDS for item-specific instructions and stability information.

Structure and Identity

ACTH-(11-24) is a mid-sequence peptide fragment of adrenocorticotropic hormone (ACTH), commonly used as a biochemical tool in melanocortin receptor studies and peptide SAR.

Item-specific (from Product Data):

  • SKU: rp173377
  • Product name: ACTH-(11-24)
  • CAS: rp173377 (as provided)
  • Grade/Purity: Moligand™
  • Storage conditions: Room temperature
  • InChIKey: 403395 (as provided)
  • 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 and structural features (for ACTH-(11–24)):

  • Typical peptide sequence (literature): Lys–Pro–Val–Gly–Lys–Lys–Arg–Arg–Pro–Val–Lys–Val–Tyr–Pro (KPVGKKRRPVKVYP).
  • 2D structural description: A linear 14-mer polypeptide of L-amino acids with a predominance of basic side chains (Lys, Arg) interspersed with hydrophobic residues (Val, Pro, Tyr) and a single small neutral residue (Gly). N-terminus is a primary amine (unless capped); C-terminus is a carboxylate (unless amidated) — specific termini for this item are not specified.
  • Functional groups: Multiple protonatable primary amines (ε-NH2 of Lys, N-terminus), guanidinium groups (Arg), phenolic ring (Tyr), secondary amide backbone; proline imino acid introduces local conformational constraint.
  • Stereochemistry: Typically all-L configuration for natural ACTH fragments (literature); item-specific stereochemistry not specified.

Note: Exact elemental formula, mass, and any terminal modifications for this catalog item are not specified; confirm on the CoA/Spec Sheet.

Synthetic Utility

While supplied as a peptide tool compound, ACTH-(11–24) is informative in peptide chemistry and can serve as:

  • A model substrate for solid-phase peptide synthesis (SPPS) validation: The sequence includes challenging features (multiple Lys/Arg, Pro) to test coupling efficiency, deprotection completeness, and resin selection (e.g., Rink amide vs Wang) under Fmoc/tBu strategies.
  • A template for analog design: Ala scans, D-residue substitutions, N- or C-terminal capping, and side-chain modifications (e.g., acylation of Lys ε-amines, incorporation of noncanonical residues) can probe structure–activity relationships relevant to melanocortin receptor interactions.
  • A calibration analyte in analytical method development: Useful to benchmark retention/ionization behavior of basic peptides in LC-MS and to optimize gradients and ion-pairing choices (e.g., FA vs TFA).
  • Conjugation chemistry testbed: The primary amines (N-terminus and Lys side chains) allow conjugation to dyes, biotin, or affinity handles via NHS esters, isothiocyanates, or click-compatible handles after appropriate derivatization.

Considerations:

  • Protecting-group strategy: For SPPS of Lys/Arg-rich sequences, ensure complete removal of side-chain protections (Boc on Lys, Pbf on Arg) and mitigate aggregation on resin via pseudoproline dipeptides or chaotropic co-solvents.
  • Purification: Basic peptides often benefit from ion-pairing modifiers (TFA) in RP-HPLC; for MS-sensitive uses, switch to FA or post-purification counter-ion exchange.

Item-specific synthetic details (e.g., termini, salt form) are Not specified; consult the CoA if you plan derivative syntheses.

Target Specificity

Not applicable. This catalog entry is a peptide tool compound, not an antibody or affinity reagent, and no target-binding specificity data are provided as item-specific specifications.

Literature context: ACTH fragments are often used to interrogate melanocortin receptor systems; however, any binding parameters (e.g., Ki, EC50) depend on sequence details, modifications, assay format, and receptor subtype. Item-specific potency/selectivity data are Not specified for this item; refer to the CoA/Spec Sheet or generate in-house under your assay conditions.

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