ARF1 (2-17) , CAS No.143228-35-7

CAS: 143228-35-7 Cat. No.: A1441119 Summenformel: C₈₅H₁₃₁N₂₁O₂₁ Molekulargewicht: 1783.08

Storage

Store at -20°C

Shipped In

Ice chest + Ice pads

Übersicht

ARF1 (2-17) inhibits both ARF-independent ( PLC-β ) and ARF-dependent ( PLD ) pathways. ARF1 (2-17) inhibits GTP-γ-S-stimulated PLD activity, phospholipase C-β (PLC-β), and exocytosis.

Specifications

Storage

Store at -20°C

Verschickt in

Ice chest + Ice pads

Dieses Produkt erfordert Kühlkettenversand. Grundversand und andere Economy-Optionen sind nicht verfügbar.

Aktionsart

INHIBITOR

Namen und Kennungen

• Molekulargewicht: 1783.08

Application Protocols

Validated, item-specific protocols and tested applications are not provided for this product entry. The following general procedures (literature-based) are commonly used with short synthetic peptides:

• Reconstitution

  • Equilibrate vial to room temperature before opening. Briefly centrifuge to collect material. Add an appropriate solvent (see Solvent Selection), gently vortex, and, if needed, sonicate briefly. Filter sterilize for cell-based uses.

• Aliquoting and storage

  • Prepare single-use aliquots at convenient stock concentrations. Store as directed under Storage & Reconstitution. Avoid repeated freeze–thaw cycles.

• Concentration determination

  • If sequence contains Trp/Tyr, UV at 280 nm can be used with the correct extinction coefficient (requires exact sequence). Alternatively, use peptide assays (e.g., absorbance at 205 nm or colorimetric assays) calibrated with standards.

• Example assay frameworks

  • Liposome co-sedimentation: Incubate peptide with defined lipid vesicles; centrifuge; analyze supernatant/pellet for peptide distribution by LC-MS or absorbance (general method).
  • CD spectroscopy: Record far-UV CD to assess secondary structure in aqueous and membrane-mimetic conditions.

For any application requiring precise conditions or expected performance, consult the CoA/Spec Sheet and perform preliminary optimization with your specific system.

Biological Roles

Context (literature): ARF1 (ADP-ribosylation factor 1) is a small GTPase of the Ras superfamily that regulates vesicular trafficking, particularly COPI coat assembly at the Golgi and endosomal compartments. Its N-terminus contains an amphipathic helix that is crucial for membrane binding and is often myristoylated in the full-length protein.

Relevance of residues 2–17 (literature):

• The 2–17 region encompasses most of the amphipathic helix that inserts shallowly into membranes, contributing to curvature sensing and recruitment of effectors.
• Peptide fragments representing this region are used to dissect sequence features governing membrane affinity, lipid selectivity (e.g., anionic lipids), and the structural propensity to form helices in membrane-mimetic environments.

Use limitations and notes for this catalog item:

• This product is a synthetic peptide fragment for research use only. No claims are made regarding biological activity, post-translational modifications (e.g., myristoylation), or exact sequence for this item in this description. Consult the CoA/Spec Sheet for definitive composition.
• Experimental outcomes (e.g., membrane binding, helix content) are sensitive to peptide sequence, charge distribution, length, and any terminal capping. Verify all parameters before drawing biological conclusions.

Buffer Applications

This product is a peptide reagent and is not a buffering agent. Classical buffer systems (e.g., phosphate, HEPES, Tris) are not applicable as functional components of this product.

Practical notes (general):

• When preparing working solutions, select a buffer compatible with your assay (e.g., PBS, HEPES, or MES) and with the peptide’s solubility and stability requirements.
• Adjust pH to favor peptide ionization states that enhance solubility while maintaining biological relevance where applicable.

For specific buffer recipes or pH ranges, refer to standard laboratory references. No buffer-formulation specifications are provided for this item.

Green Alternatives

Green chemistry considerations for peptide handling center on solvent choice and waste minimization rather than reaction substitution:

• Preferred solvent hierarchy (general, literature)

  • Water/buffer: lowest environmental impact and best for most bioassays. Optimize pH/ionic strength to enhance solubility.
  • Bio-based co-solvents where feasible: ethanol (anhydrous or aqueous) can sometimes replace DMSO for modestly hydrophobic peptides, pending assay tolerance.
  • Minimize DMSO and acetonitrile volumes by pre-wetting peptides with the smallest feasible amount, then diluting into aqueous media.

• Operational strategies

  • Prepare concentrated stocks to reduce total solvent use; aliquot to avoid freeze–thaw and waste.
  • Use micro-scale LC-MS methods and short gradients to cut acetonitrile consumption.
  • Opt for ultrafiltration and aqueous buffer exchange rather than precipitation with large volumes of organic solvents.

Comparison table (general)

• Water/buffer: Greenest; may require pH adjustment for solubility.
• Ethanol: Renewable, lower toxicity; limited solubilizing power versus DMSO.
• DMSO: Excellent solubilizer; higher toxicity/biological impact—use sparingly.
• Acetonitrile: Common for LC-MS; volatile and flammable—minimize and recycle via solvent recovery when possible.

Always balance environmental considerations with experimental requirements and compatibility of the peptide and downstream assays.

Pharmaceutical Uses

This product is supplied strictly for research use only and is not intended for human or veterinary use, diagnostic procedures, or as a drug substance/excipient.

General context (literature):

• Short synthetic peptides can serve as reference standards, analytical surrogates, or process-development tools in pharmaceutical R&D. They may be used to develop LC-MS methods, assess membrane interaction of peptide candidates, or study protein–lipid interactions in discovery-stage research.

Item-specific pharmaceutical status:

• Pharmacopeial monograph status, excipient roles, GMP grade, and regulatory classification: Not specified for this item; refer to CoA/Spec Sheet if applicable.

If your work requires GMP-grade material or documentation for regulated use, please contact us with your specifications. This catalog item is offered for non-clinical laboratory research only.

Physical Properties

• Appearance: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight and formula: Not specified for this item; refer to CoA/Spec Sheet.
• Solubility (general guidance, literature):
  • Many short unmodified peptides are soluble in water, PBS, or dilute acids/bases depending on net charge. Hydrophobic sequences may require co-solvents (e.g., DMSO) or stepwise pH adjustment (literature guidance).
  • For membrane-active N-terminal ARF1 fragments, partial hydrophobicity is common; initial wetting with a small volume of DMSO followed by dilution into aqueous buffer can aid dissolution (literature).
• pKa/logP: Not applicable as single values; properties depend on the specific amino acid composition (not specified for this item).
• State at room temperature: Typically solid (lyophilized) for peptide reagents (general).
• Melting/boiling points, density, refractive index: Not typically defined for peptides; Not specified for this item; refer to CoA/Spec Sheet.
• UV absorbance (general, literature):
  • If the sequence contains aromatic residues (Trp/Tyr/Phe), characteristic absorbance near 280 nm (Trp/Tyr) may be used. Without the exact sequence, an accurate extinction coefficient cannot be provided here; consult CoA/Spec Sheet.

Note: Do not treat these generalities as specifications. For exact values and sequence-dependent characteristics, use the item’s CoA/Spec Sheet and SDS.

Quality and Grades

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

Interpreting peptide quality (general guidance):

• Peptide purity is commonly reported as percentage by HPLC area; typical research grades include ≥95%, ≥90%, or crude. Exact purity level for this item is not provided here.
• Identity confirmation is typically by mass spectrometry (ESI/MS or MALDI) and analytical RP-HPLC. CoA usually includes observed mass and chromatogram.
• Counterions and form: Peptides may be supplied as TFA salts, acetates, or as free bases/acids; this affects mass and solubility. The specific counterion/form for this item is not specified.
• Modifications/stabilizers: Any N-/C-terminal capping (e.g., Ac-, -NH2), labels, or stabilizers would be listed on the CoA/Spec Sheet if applicable. None are specified here.

What this means for your experiments:

• For quantitative studies (e.g., binding isotherms, biophysics), verify purity, salt content, and exact molecular weight from the CoA.
• If UV quantification is planned, confirm the extinction coefficient from the exact sequence and modifications.
• If compatibility with mass-sensitive assays is critical, consider desalting or exchanging counterions after reconstitution as needed.

Please refer to the item’s CoA/Spec Sheet for definitive purity, analytical data, and any stabilizers used.

Reaction and Applications

This product is a peptide tool rather than a small-molecule reagent for synthetic transformations. Accordingly, classical organic reactions (e.g., cross-couplings, Grignards) are not applicable.

Research applications (literature-based context for ARF1 N-terminal peptides):

• Membrane interaction studies: The ARF1 N-terminus forms an amphipathic helix that can associate with lipid bilayers. Short peptides spanning residues 2–17 are often used to probe membrane binding, lipid preference, and curvature sensitivity in model systems such as liposomes and supported bilayers.
• Protein–membrane recruitment assays: In vitro reconstitution of coatomer or adaptor recruitment where the ARF1 N-terminus contributes to membrane anchoring (sequence-specific; verify activity experimentally).
• Biophysical characterization: Circular dichroism (CD) in membrane-mimetic environments (e.g., SDS micelles, TFE/water) to assess helicity; fluorescence methods if aromatic residues are present (sequence-dependent).
• Method development: LC-MS method suitability and retention-time standards for ARF1-derived peptides.

Notes

• Activity is sequence- and modification-dependent. Because the exact sequence and termini of this catalog item are not provided here, users should consult the CoA/Spec Sheet and confirm performance in their specific assay context.
• For covalent conjugation (e.g., to fluorophores or lipids), confirm presence/absence of reactive residues (Lys, Cys) from the exact sequence prior to derivatization.

Reaction Conditions

Classical synthetic reaction conditions are not applicable to this finished peptide. The following are general, literature-based conditions for experimental use in biophysical/biochemical assays involving amphipathic peptides:

• Sample preparation

  • Dissolution: Begin with sterile water or buffer. If insoluble, wet with minimal DMSO or acetonitrile, then dilute into buffer. Gentle warming (≤37°C) and brief sonication can aid dissolution.
  • Concentration range: Application-dependent (e.g., low µM for binding assays; higher for CD spectroscopy). Determine empirically for your system.

• Membrane interaction assays (literature)

  • Liposome binding: Incubate peptide with large unilamellar vesicles (e.g., 100–200 nm) in buffered saline at ambient temperature; quantify binding via co-sedimentation, fluorescence, or CD. Optimize lipid composition to test anionic lipid dependence.
  • CD spectroscopy: Record spectra in aqueous buffer with membrane mimetics (e.g., TFE/water mixtures or detergent micelles) to assess helicity; avoid high absorbance below 200 nm by controlling concentration and pathlength.

• LC-MS analysis

  • Mobile phases: Water + 0.1% formic acid and acetonitrile + 0.1% formic acid; gradients tailored to hydrophobicity. Use low-binding vials to minimize adsorption.

All parameters above are general guidance from literature. Optimize empirically and confirm compatibility with your specific peptide lot and assay.

Safety and Handling

• GHS classification, signal word, hazard and precautionary statements: Not specified for this item; refer to SDS.
• Pictograms: Not specified for this item; refer to SDS.

General laboratory safety for synthetic peptides (literature/good practice):

• Handling/PPE
  • Wear appropriate PPE: lab coat, nitrile gloves, and safety glasses. Avoid generating dust/aerosols when opening lyophilized vials.
  • Work in a clean area; for cell-based assays use sterile technique to avoid bioburden.
• Incompatibilities
  • Avoid strong oxidizers for peptides containing oxidation-sensitive residues (e.g., Met, Cys), sequence-dependent. Specific sensitivities for this item are not specified.
• First-aid overview
  • Inhalation: move to fresh air; seek medical advice if symptoms persist.
  • Skin/eye contact: rinse with water for several minutes; remove contaminated clothing; seek medical attention if irritation develops.
  • Ingestion: rinse mouth; do not induce vomiting; seek medical attention.
• Special risks
  • Peptides are generally non-volatile but may be bioactive in research systems; minimize exposure and avoid ingestion or injection.
  • Avoid repeated freeze–thaw of solutions to limit degradation.
• Waste disposal
  • Dispose of unused material and contaminated disposables as chemical waste following institutional and local regulations.

Always consult the product’s SDS for authoritative hazard, toxicological, and handling information.

Solvent Selection

As a synthetic peptide, solvent choice depends on its amino acid composition and terminal modifications, which are not specified here. Use the following sequence-agnostic strategy (literature-based):

• Primary options

  • Water or buffers (e.g., PBS, HEPES) at pH values that favor ionization of the peptide’s termini/side chains to enhance solubility.
  • For hydrophobic or amphipathic peptides (common for N-terminal ARF1 fragments), pre-wet with a minimal volume of DMSO or acetonitrile, then dilute into aqueous buffer with vigorous mixing to keep final organic content ≤5–10% for most bioassays.
  • For highly basic peptides, a few drops of dilute acetic acid can aid solubilization; for acidic peptides, a few drops of dilute ammonium hydroxide can help (titrate carefully; literature guidance).

• Additives (if compatible with your assay)

  • 0.1% TFA or 0.1% formic acid to improve solubility for LC-MS workflows.
  • 0.01–0.1% nonionic surfactants (e.g., Tween-20) may reduce surface adsorption at very low concentrations; confirm assay tolerance.

• Practical tips

  • Sonication and gentle warming (≤37°C) can assist dissolution; avoid prolonged heating.
  • Filter sterilize through low-protein-binding membranes for cell-based work.
  • Avoid repeated freeze–thaw; aliquot immediately after preparation.

Comparison (general)

• Water/buffer: safest for bioassays; sequence-dependent solubility.
• DMSO: strongest small-volume co-solvent; watch for cell toxicity and protein denaturation above a few percent.
• Acetonitrile: useful for LC-MS and initial wetting; volatile and easy to remove.

Storage and Reconstitution

• Storage conditions (item-specific): Store at -20°C. Avoid exposure to moisture and light. Shipped in an ice chest with ice pads to maintain cold chain.

• Stability notes (general for peptides)

  • Keep peptide lyophilized and desiccated until use. After opening, promptly reseal under inert gas or store with desiccant to limit hydrolysis and oxidation. Specific shelf-life and stability for this item are not specified; refer to CoA/Spec Sheet.

• Reconstitution (general guidance)

  • Bring vial to room temperature before opening to prevent condensation. Spin down contents.
  • Start with sterile water or assay buffer. If insoluble, add minimal DMSO or acetonitrile to wet the peptide, then dilute with buffer. Adjust pH cautiously if needed (e.g., dilute acetic acid/base) while ensuring compatibility with downstream assays.
  • For sterile preparations, 0.22 µm filter through a low protein-binding membrane.

• Working solution management

  • Prepare single-use aliquots to avoid freeze–thaw. Store aliquots at -20°C (short term) or per your lab’s validated practice; avoid repeated warming.
  • For longer-term storage of aqueous solutions, consider -80°C with cryoprotective conditions validated for your application. Monitor for precipitation or activity loss upon thawing.

For definitive instructions on concentration, solvent, and stability of this specific lot, consult the product’s CoA/Spec Sheet.

Structure and Identity

Brief description: ARF1 (2–17) is a short peptide corresponding to residues 2 through 17 from the N-terminus of the small GTPase ARF1. It is supplied for research use as a synthetic peptide fragment.

• Item-specific identifiers

  • SKU: A1441119
  • Product name: ARF1 (2-17)
  • CAS: 143228-35-7
  • 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.
  • CID: Not specified for this item; refer to CoA/Spec Sheet.

• Structural features (general, literature-based)

  • Functional class: synthetic peptide fragment derived from ARF1 N-terminus (literature).
  • Expected motif: ARF1’s extreme N-terminus forms an amphipathic helix implicated in membrane association; residues 2–17 encompass most of this helix (literature). Sequence details for this specific catalog item are not provided here.
  • Stereochemistry: composed of proteinogenic L-amino acids unless otherwise specified; any modifications (acetylation, amidation, labels) are not specified for this item and should be confirmed on the CoA/Spec Sheet.

• 2D structural description (general)

  • Linear oligomer of α-amino acids linked via trans amide (peptide) bonds with side chains defined by the ARF1 2–17 sequence (not provided here). No ring systems are inherent unless sequence contains cyclic residues or post-synthetic cyclization, which are not specified for this item.

Please consult the item’s CoA/Spec Sheet for definitive sequence, modifications, and exact composition.

Synthetic Utility

As a finished peptide reagent, ARF1 (2–17) is not typically a building block for stepwise organic synthesis; however, it has utility in conjugation and materials assembly (general, literature):

• Bioconjugation
  • If the sequence contains nucleophilic residues (e.g., Lys ε-amine, Cys thiol), it may be derivatized with fluorophores, affinity tags, lipids, or crosslinkers. Exact residue availability depends on the specific sequence for this item (not specified here).
• Surface immobilization
  • N- or C-terminal functionalization (e.g., via NHS esters, maleimides, click handles) enables attachment to surfaces for biophysical assays (SPR/QCM-D) and microscopy.
• Supramolecular assembly
  • Amphipathic peptides can drive self-assembly on membranes or in micellar environments, facilitating model system construction for membrane–protein interaction studies.
• Analytical standards
  • Use as retention time or fragmentation benchmarks in LC-MS method development for ARF1-derived peptides.

For any covalent modification, confirm the exact sequence, terminal caps, and counterion of this item from the CoA/Spec Sheet to select appropriate chemistries and avoid side reactions.

Target Specificity

Not applicable. This product is a synthetic peptide fragment and not an antibody or affinity reagent with defined antigen-binding specificity.

• Antigen/epitope, species reactivity, clone/isotype: Not specified for this item; refer to CoA/Spec Sheet if any affinity properties are claimed for a specific lot.

Use this peptide as a research tool according to your assay design; no target-binding specifications are provided.