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INSL3 (A chain), CAS No.rp174346

CAS: rp174346 Cat. No.: rp174346
COA
INSL3 (A chain), CAS No.rp174346
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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Germania (EU)
USA*
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Qty
500μg
rp174346-500μg
Su ordinazione · 8–12 settimane
2.082,49€
1mg
rp174346-1mg
Su ordinazione · 8–12 settimane
3.470,87€
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SDS
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Specifications Stoccaggio e spedizione Documentazione Advanced Data Certificati (CoA, COO, BSE/TSE e tabella di analisi) Informazioni genetiche Calcolatori di soluzioni Recensioni Application Protocols Biological Roles Buffer Applications Green Alternatives Pharmaceutical Uses Physical Properties Quality and Grades Reaction and Applications Reaction Conditions Safety and Handling Solvent Selection Storage and Reconstitution Structure and Identity Synthetic Utility Target Specificity
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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
INSL3 (A chain), CAS No.rp174346
Sinonimi
insulin-like peptide 3 (A chain)
Grado
Moligand™
Specifiche e purezza
Moligand™
CAS
rp174346
Tipo di molecola
Peptidi
Product Line
Prodotti biologici
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

Certificati (CoA, COO, BSE/TSE e tabella di analisi)
C of A & Other Certificates(BSE/TSE, COO):
Analytical Chart:
Informazioni genetiche
Alternate Namesinsulin-like peptide 3 (A chain)
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 tested applications, recommended dilutions/concentrations, and positive controls: Not specified for this item; refer to CoA/Spec Sheet.

No additional protocol details are provided in the Product Data. Users should design and validate assay conditions appropriate to their system, and consult primary literature for RXFP2 assay setups if applicable.

Biological Roles

Literature/general background (not a specification or clinical claim)

  • Family and maturation: INSL3 (insulin-like peptide 3) is a heterodimeric hormone of the insulin/relaxin superfamily, produced predominantly by Leydig cells (males) and by theca/granulosa cells (females). The mature hormone comprises A and B chains linked by disulfide bonds; the A chain contributes to the conserved insulin-fold and receptor interaction surface.
  • Receptor: RXFP2 (LGR8), a leucine-rich repeat-containing GPCR. Binding activates Gs signaling in many systems, elevating intracellular cAMP; context-dependent coupling to other pathways (e.g., ERK) has been reported.
  • Physiological context: INSL3 is implicated in reproductive development and function, including the gubernacular pathway in testicular descent and aspects of ovarian physiology in nonclinical models. The A chain, through its cysteine framework and surface residues, helps stabilize the active conformation of the heterodimer.
  • Biochemical properties: the A chain often contains an intrachain disulfide that, together with interchain disulfides to the B chain, creates the compact insulin/relaxin fold crucial for receptor selectivity and potency. Sequence variation across species provides a platform for SAR exploration.

Use in research

  • The isolated A chain is valuable for dissecting binding determinants, designing minimized ligands, and engineering conjugates/probes that target RXFP2 signaling pathways, strictly for laboratory research applications.
Buffer Applications

Not a classical buffering reagent. However, buffers are central to preparing and using INSL3 (A chain) in biochemical or cell-based assays.

General, literature-based guidance (not item-specific)

  • Common buffers and pH ranges:
    • PBS (phosphate-buffered saline), pH 7.2–7.4: widely used for receptor-binding assays and dilutions.
    • HEPES, pH 7.2–7.6: good CO2-independent buffering for live-cell work.
    • Acetate buffer, pH 4.5–5.5: can assist initial dissolution of basic peptides before neutralization/dilution.
    • Ammonium bicarbonate, pH ~8.0: useful for MS sample prep and lyophilization (volatile salts), but prolonged exposure at basic pH may promote deamidation.
  • Ionic strength: adjust NaCl (e.g., 100–150 mM) to reduce nonspecific adsorption and mimic physiological conditions.
  • Additives: 0.01%–0.1% carrier proteins (BSA) or 0.01% polysorbate-20 can minimize peptide adsorption to plastics; confirm that additives do not interfere with your assay.
  • Filtration/sterility: for cell assays, sterile-filter final working solutions (0.22 µm) if compatible with the peptide and assay.

Note: Exact buffer composition, compatibility with metals/reducing agents, and pH sensitivity depend on the specific A-chain sequence and disulfide status. Consult the CoA/Spec Sheet for any sequence-specific cautions.

Green Alternatives

Context: As a peptide reagent, INSL3 (A chain) is typically used in aqueous systems. The primary opportunities for greener practice involve solvent selection and waste minimization during dissolution, purification, and analysis.

Greener choices (literature/general)

  • Prefer water-based buffers (PBS, HEPES) over fluorinated alcohols (e.g., HFIP) or strong organic solvents for dissolution. Use minimal DMSO only if required to initiate solubilization of hydrophobic sequences.
  • Choose acetate or chloride counterions where feasible to reduce reliance on TFA. If supplied as TFA salt, a simple buffer exchange (spin desalting) can lower TFA content prior to cell assays.
  • During HPLC method development, employ water–acetonitrile with low TFA or formic acid; consider using MS-friendly, lower-toxicity modifiers (e.g., 0.1% formic acid) and gradient methods that minimize organic consumption.
  • Scale considerations: prepare concentrated stocks to reduce packaging and solvent volumes, and aliquot to avoid repeated freeze–thaw that leads to waste.

Comparison (illustrative; not item-specific)

  • HFIP vs water/0.1% acetic acid: HFIP can dissolve stubborn peptides but is hazardous and has higher environmental impact; water with a small amount of acetic acid is typically sufficient and far greener for A-chain-length peptides.
  • DMSO vs DMF: DMSO is generally preferred for limited cosolvent use due to lower toxicity and better biodegradability.

Implement institutional green-chemistry practices for peptide handling and analytical workflows.

Pharmaceutical Uses

No therapeutic or clinical claims are made for this product. The following pertains to research/formulation contexts only (literature/general):

  • Reference standard: INSL3-related peptides can serve as analytical reference materials in method development and QC for peptide analytics (LC–MS, HPLC), including retention-time markers and response-factor studies.
  • Formulation research: used as a model peptide to evaluate excipient effects (e.g., polysorbates, sugars, amino acids) on peptide stability, adsorption, and oxidative susceptibility, especially for cysteine-rich peptides.
  • Delivery studies: the A chain, due to its modest size, can be employed in feasibility studies for peptide delivery systems (e.g., liposomes, nanoparticles) strictly as a surrogate research cargo.
  • Regulatory status: no pharmacopeial monograph is implied for this item. Any GMP suitability, residual solvent limits, or endotoxin specifications are not provided and must not be assumed.

Item-specific note

  • Grade/Purity: Moligand™; intended for research use only.
  • Specifications such as endotoxin, bioburden, residual solvents, and exact purity are Not specified for this item; refer to CoA/Spec Sheet.

Researchers considering formulation experiments should confirm salt form, counterions (e.g., TFA vs acetate), and peptide content before calculating molar concentrations or dose equivalents.

Physical Properties

Item-specific (from Product Data)

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

Literature/general (typical for short peptide A chains; not a specification)

  • Physical state: typically supplied as a lyophilized solid or film; hygroscopicity varies with sequence and counterions.
  • Solubility: sequence-dependent. Common strategies include dissolution in water, dilute aqueous acetic acid (0.1–1%), dilute ammonia (0.1%), or organic cosolvents (DMSO) before dilution with buffer. For cysteine-rich chains, mild reducing conditions (e.g., 1–5 mM DTT) may be used only when native disulfides are not required.
  • pI/logP: peptides do not have conventional logP; net charge and isoelectric point depend on sequence composition and pH (compute from sequence when available).
  • UV characteristics: peptides show strong absorbance at 214 nm (amide) and, if Trp/Tyr/Phe present, at 280/274/258 nm respectively (qualitative guidance).
  • Stability: solid-state peptides are typically stable for months when kept dry, protected from light, and at ambient to refrigerated temperatures; aqueous solutions are less stable (days to weeks) depending on sequence, pH, and presence of disulfides.
  • Refractive index, density, BP/MP: not meaningful/practical for lyophilized peptides.

Note: For exact mass, counterions (e.g., TFA, acetate), and solubility guidance specific to this lot, consult the CoA/Spec Sheet.

Quality and Grades

Item-specific (from Product Data)

  • Grade/Purity: Moligand™.

Explanation and implications (general; not item-specific specifications)

  • Moligand™ designation indicates inclusion in a small-molecule/ligand-oriented screening collection aimed at discovery, SAR, or receptor-ligand studies. For peptides, this typically emphasizes suitability as a biochemical probe or library component rather than a clinical-grade material.
  • Purity/identity confirmation for peptides is commonly supported by analytical HPLC and MS (ESI/MALDI). However, specific purity percentage, counterion content (e.g., TFA vs acetate), water/solvent content, and residual salts are lot-dependent.
  • What to verify before critical experiments:
    • Certificate of Analysis (CoA) for exact sequence, molecular weight (monoisotopic/average), purity (HPLC area %), and counterion.
    • Disulfide status: whether supplied in oxidized (disulfide-bonded) or reduced/linear form.
    • Salt form and peptide content corrections (e.g., adjust for TFA and water to calculate molar concentration).
  • UV cutoff/metal limits/peroxide/water ppm: Not specified for this item; refer to CoA/Spec Sheet.

Recommendation

  • For quantitative receptor-binding or cell-based assays, verify identity and purity via vendor CoA and, if needed, perform in-house QC (analytical RP-HPLC and HRMS). If sequence contains Met/Trp/Cys, consider antioxidants or inert atmosphere during handling to minimize oxidation.
Reaction and Applications

Item-specific (from Product Data)

  • Manufacturer Applications: Not specified beyond “For research use only.”

Literature/general applications of INSL3 A chain peptides (not item-specific claims)

  • Receptor/ligand studies: INSL3 signals primarily through the RXFP2 (LGR8) receptor. A-chain peptides can be used to probe structure–activity relationships (SAR) when combined with B chain analogs or as part of heterodimer reconstitution studies to assess binding and signaling contributions of the A chain.
  • Biochemical assays: competition binding to RXFP2-expressing membranes/cells; cAMP accumulation assays; β-arrestin recruitment; ERK phosphorylation readouts. A-chain fragments or analogs can serve as negative controls if lacking key binding epitopes.
  • Folding/disulfide studies: model systems to study oxidative folding pathways of insulin/relaxin family peptides, including the role of cysteines and redox buffers (GSH/GSSG ratios) in achieving native disulfide connectivity.
  • Analytical standards: retention-time markers and MS standards in LC–MS peptide method development.
  • Conjugation/probe development: installation of reporter groups (biotin/fluorophores) via N-terminus or lysine side chains, or thiol-selective labeling on cysteines, to create affinity probes for RXFP2 pull-down or imaging (research use).

Practical tips

  • If reconstituting heterodimers from separate chains, maintain mild oxidative conditions and monitor by RP-HPLC and MS. Carefully control pH (≈7–8) and redox buffers to favor native disulfide pairing. Validate activity in a known RXFP2 assay system.
Reaction Conditions

No item-specific reaction conditions are provided. Below are general, literature-based conditions relevant to peptide conjugation and disulfide chemistry involving A-chain peptides (not product specifications):

  • NHS-ester amine coupling: 10–100 µM peptide in 50–100 mM phosphate or HEPES, pH 7.5–8.5, with 2–10 molar equivalents of NHS-activated ester. Incubate 30–120 min at room temperature. Quench with Tris or ethanolamine. Typical conversions: high for exposed amines; monitor by LC–MS.
  • Maleimide–thiol coupling: for free cysteines, perform at pH 6.5–7.2 in PBS or citrate–phosphate buffer. Use 1.1–2.0 eq maleimide per thiol; react 15–60 min at RT, protect from light/oxygen. Avoid amine nucleophiles at basic pH to preserve maleimide selectivity.
  • Disulfide formation (air oxidation): 0.05–0.5 mg/mL peptide in pH 7.5–8.0 buffer, with 1–5% DMSO or defined redox pairs (GSH/GSSG 1–10 mM total) at RT to 4 °C; hours to overnight. Optimize to favor native pairing; analyze by RP-HPLC and MS.
  • Click chemistry (CuAAC) if noncanonical handles present: pH 7–8 aqueous buffer with 0.5–1 mM CuSO4, 2–5 mM sodium ascorbate, 0.1–0.5 mM TBTA or water-soluble ligand; minutes to hours at RT.

Expected yields/times are highly sequence- and site-dependent; always monitor reactions by LC–MS and purify by preparative RP-HPLC if needed.

Safety and Handling

Item-specific (from Product Data)

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

General laboratory safety for research peptides (literature/good practice; defer to SDS)

  • PPE: wear lab coat, nitrile gloves, and safety glasses. Avoid inhalation of powders and generation of aerosols; handle in a clean area or fume hood.
  • Hazards: peptides are generally of low volatility; potential risks include dust irritation, allergic sensitization upon repeated exposure, and sequence-specific bioactivity. Treat as potentially bioactive research material; prevent skin contact and ingestion.
  • Incompatibilities: avoid strong oxidizers and bases/acids that can cause racemization, hydrolysis, or disulfide scrambling. For cysteine-containing peptides, avoid oxidizing conditions if reduced thiols must be preserved; conversely, avoid reducing agents if native disulfide structure is required.
  • First aid (overview): if inhaled, move to fresh air; if on skin, wash with soap and water; if in eyes, rinse cautiously with water for several minutes; if ingested, rinse mouth. Seek medical attention if symptoms persist. Provide SDS to responders.
  • Handling tips: work with small quantities; use antistatic precautions to minimize loss of lyophilized material; reconstitute under sterile conditions if using in cell-based assays.

Always consult the official SDS for authoritative hazard and response information.

Solvent Selection

Applicability: INSL3 (A chain) is a peptide; solvent choice is governed by sequence charge/hydrophobicity and desired bioactivity state (reduced vs oxidized).

General guidance (literature; not item-specific)

  • Primary solvents for stock solutions:
    • Water or buffered saline (e.g., PBS) for hydrophilic sequences.
    • 0.1–1% acetic acid in water to aid dissolution of basic peptides; neutralize/dilute with buffer after full dissolution.
    • Minimal DMSO to pre-dissolve highly hydrophobic peptides, then dilute into aqueous buffer (keep final DMSO ≤0.1–1% for cells).
    • For cysteine-rich peptides where native disulfide must be retained, avoid strong reducing agents and high-pH buffers during dissolution.
  • Buffer options by use case:
    • Binding/biochemical assays: HEPES (pH 7.2–7.6) or PBS (pH 7.2–7.4), low protein-binding plastics.
    • Cell assays: serum-free or defined media; minimize TFA carryover by buffer exchange if necessary.
  • Avoid: neat organic solvents for long-term storage; high pH (>8.5) can promote deamidation/racemization; strong acids/bases can hydrolyze peptide bonds.

Comparison (literature)

  • Water vs 0.1% acetic acid: acetic acid often improves initial wetting/solubilization of cationic peptides; water preserves neutral pH-sensitive motifs.
  • DMSO vs DMF: DMSO is more biocompatible for small cosolvent fractions; DMF is generally avoided in bioassays but can assist initial solubilization for analytical work.

Always confirm sequence-specific solubility and stability on the CoA/Spec Sheet.

Storage and Reconstitution

Item-specific (from Product Data)

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

General guidance for peptides (literature; not item-specific specifications)

  • Solid storage: keep container tightly closed, dry, and protected from light. Although room temperature is indicated for this item, many peptides benefit from cooler storage (2–8 °C or −20 °C) for long-term stability; follow product label/CoA.
  • Reconstitution: use sterile, oxygen-reduced water or buffer appropriate for your assay. Start with water or 0.1% acetic acid; if needed, add minimal DMSO to aid solubilization, then dilute into buffer. Target 0.1–1.0 mg/mL for working stocks, adjusting to sequence solubility.
  • Aliquoting: divide into single-use aliquots to avoid repeated freeze–thaw and adsorption losses. Use low-binding tubes and pipette tips.
  • Stability of solutions: aqueous solutions are typically stable for hours to days at 2–8 °C; for longer storage, freeze aliquots at −20 to −80 °C. Avoid multiple freeze–thaw cycles.
  • Disulfide integrity: if native disulfide bonds are required, avoid reducing agents and high pH during dissolution and storage; add antioxidants (e.g., 0.1 mM methionine) only if compatible with assays.

Always consult the CoA/Spec Sheet for reconstitution solvent, concentration, and any sequence-specific precautions.

Structure and Identity

Item-specific (from Product Data)

  • Product name: INSL3 (A chain)
  • SKU: rp174346
  • Grade/Purity: Moligand™
  • CAS: rp174346 (catalog placeholder)
  • 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.

Literature/general description of structure (for context; not item-specific)

  • INSL3 (insulin-like peptide 3) is a member of the insulin/relaxin family. The mature hormone comprises two chains (A and B) linked by disulfide bridges; the A chain is a short peptide typically in the mid-20–amino-acid range and often contains cysteine residues forming one intrachain disulfide (family-typical) plus two interchain disulfides to the B chain.
  • Functional groups/features: multiple amide bonds (peptide backbone), side-chain functionalities spanning acidic (Asp/Glu), basic (Lys/Arg/His), polar (Ser/Thr/Asn/Gln), hydrophobic (Leu/Ile/Val/Phe), and cysteines providing thiols/disulfides (sequence-dependent).
  • 2D description in words: a linear polypeptide chain with L-α-amino acid residues connected via trans-amide bonds; side chains project alternately; cysteine residues (where present) enable disulfide connectivity critical for the insulin-fold topology.
  • Chirality: peptides are composed of L-amino acids (literature, unless otherwise noted by vendor). Any post-translational modifications and exact sequence length/identity are sequence-specific and should be confirmed by the CoA/Spec Sheet.
Synthetic Utility

From a synthetic chemistry perspective (literature/general), the isolated INSL3 A chain is most useful as a biological probe or as a component in peptide assembly/folding studies rather than as a conventional building block.

  • Functional groups: multiple amide bonds, terminal amine (N-terminus) and carboxylate (C-terminus), and side-chain functionalities (e.g., Lys ε-amine, Asp/Glu carboxylates, Ser/Thr hydroxyls). Cys residues (if present) enable thiol/disulfide chemistry.
  • Bioconjugation handles:
    • NHS-ester coupling to primary amines (N-terminus/Lys) at pH 7.5–8.5.
    • Maleimide–thiol conjugation at pH 6.5–7.2 for cysteines (site-selective labeling).
    • Click chemistry (azide/alkyne) when noncanonical handles are introduced synthetically.
  • Folding chemistry: oxidative folding of A + B chains in the presence of redox buffers (e.g., GSH/GSSG) and catalysts (protein disulfide isomerase mimics) to achieve native disulfide connectivity typical of the insulin/relaxin fold.
  • Retrosynthetic relevance: A chains are assembled by SPPS (Fmoc/tBu) on a solid support, followed by side-chain deprotection and cleavage; orthogonal cysteine protection (Trt/Acm/Mmt) allows programmed disulfide formation.
  • Analytical support: RP-HPLC with water–acetonitrile gradients and MS (ESI or MALDI) for identity, purity, and folding-state confirmation.

Note: Sequence-specific reactivity and protection strategies vary; consult the sequence on the CoA/Spec Sheet if planning conjugation or refolding experiments.

Target Specificity

Item-specific (from Product Data)

  • Target/antigen, receptor specificity, clone/isotype, species reactivity, and validated applications: Not specified for this item; refer to CoA/Spec Sheet.

Literature context (not a specification)

  • INSL3 peptides interact with RXFP2 (LGR8) receptors in mammalian systems. The isolated A chain may not, by itself, recapitulate full receptor affinity without the B chain; specificity and potency depend on correct disulfide connectivity and full heterodimer structure. Any activity of isolated A-chain fragments is assay- and sequence-dependent and should be empirically determined.

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