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LVV-hemorphin, CAS No.rp174478

CAS: rp174478 Cat. No.: rp174478
COA
LVV-hemorphin, CAS No.rp174478
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
rp174478-500μg
Su ordinazione · 8–12 settimane
2.082,49€
1mg
rp174478-1mg
Su ordinazione · 8–12 settimane
3.470,87€
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SDS
Safety data
COA
Certificate
DS
Datasheet
SP
Spec sheet
Specifications Stoccaggio e spedizione Documentazione Advanced Data Struttura 3D 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
LVV-hemorphin, CAS No.rp174478
Grado
Moligand™
Specifiche e purezza
Moligand™
CAS
rp174478
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

Struttura 3D
Modello di struttura chimica interattiva





Certificati (CoA, COO, BSE/TSE e tabella di analisi)
C of A & Other Certificates(BSE/TSE, COO):
Analytical Chart:
Informazioni genetiche
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

Tested applications and conditions are not provided for this item in the Product Data. Refer to the CoA/Spec Sheet for any lot‑specific recommendations.

General workflow outline (informational only; not validated for this item)

  • Stock preparation: prepare a concentrated stock in water, buffer, or DMSO based on solubility; record exact concentration by UV or gravimetric means.
  • Serial dilution: perform half‑log or log dilutions into assay buffer; maintain constant solvent percentage across wells.
  • Incubation: follow your assay SOP for time/temperature; protect from light if your readout or peptide contains aromatic residues sensitive to photobleaching/oxidation.
  • Controls: include vehicle, nonbinding peptide control, and (if available) a literature‑reported active analog for benchmarking.

Because no application data are specified for this catalog item, the above is provided solely as general guidance.

Biological Roles

General literature context (informational; not product claims)

  • Origin: Hemorphins are endogenous peptides generated from proteolysis of hemoglobin β‑chain sequences. LVV‑hemorphin variants carry an N‑terminal Leu‑Val‑Val extension relative to core hemorphins.
  • Molecular recognition: Members of the hemorphin family have been reported to interact with peptidergic recognition sites, including opioid‑related binding sites and the angiotensin IV/AT4/IRAP axis in various biochemical studies. Binding profiles can vary with exact sequence length and terminal modifications.
  • Functional themes observed in vitro: modulation of peptidase activity, interactions with transport or receptor proteins, and sequence‑dependent effects on peptide stability and cell permeability.
  • Biophysical properties: Aromatic residues (e.g., Tyr, Trp, Phe) contribute to UV absorbance near 280 nm and facilitate spectroscopic quantitation; basic residues (e.g., Arg) influence net charge and binding to acidic protein surfaces.

Important notes

  • The precise sequence, length (e.g., hemorphin‑6/7 variants), terminal states, and salt form for this catalog item are not specified here; these factors determine detailed biological binding profiles.
  • All uses are limited to research. No medical, diagnostic, or therapeutic applications are implied or permitted for this product.
Buffer Applications

Not a buffer reagent: LVV‑hemorphin is a peptide ligand and is not typically used to prepare buffering systems.

Practical solution preparation for assays (general guidance)

  • Reconstitution solvent: start with ultrapure water or assay buffer (e.g., phosphate‑buffered saline, HEPES). If insoluble, prepare a concentrated DMSO stock and dilute into buffer with mixing.
  • pH considerations: maintain pH compatible with your target assay (commonly pH 6.5–7.5 for many protein binding assays). Avoid extremes that can promote peptide hydrolysis or side‑chain modification.
  • Ionic strength: 100–150 mM NaCl is often used to mimic physiological ionic strength and reduce nonspecific interactions; adjust based on your assay.
  • Filtration: 0.22 μm filtration can clarify working solutions for cell‑free assays.

Recipes and exact pH ranges are assay‑specific and depend on the intended target; none are specified for this item. Refer to your method SOPs for buffer composition.

Green Alternatives

Context: For peptide ligands like LVV‑hemorphin, the principal environmental considerations come from solvent use in dissolution and assay workflows, not from reaction solvents.

Greener solvent choices (general guidance)

  • Prefer aqueous buffers as the primary medium whenever compatible with assay design.
  • Limit DMSO to the minimal concentration needed for solubility and delivery (commonly ≤1–2% v/v in final assay mixtures).
  • Avoid DMF and NMP in bioassay contexts when possible due to higher toxicity and persistence.

Comparison (general; not item specifications)

  • Aqueous buffer (phosphate, HEPES)
    • Pros: benign, low VOC, compatible with most assays.
    • Cons: limited solubility for highly hydrophobic sequences; potential for microbial growth in stored solutions.
  • DMSO (analytical grade)
    • Pros: excellent peptide solvency, miscible with water, low volatility.
    • Cons: cytotoxicity at higher %; may affect binding equilibria; disposal considerations.

Operational tips to reduce footprint

  • Prepare small aliquots of concentrated stock to minimize waste from freeze–thaw cycles.
  • Use micro‑scale high‑throughput formats (384/1536‑well) to reduce solvent consumption.
  • Where feasible, validate lyophilized direct‑to‑assay reconstitution with buffer to eliminate DMSO.
Pharmaceutical Uses

This product is supplied strictly for research use only.

Context (general, non‑clinical)

  • Discovery workflows: peptide ligands such as LVV‑hemorphin may be used as research tools in early screening, target validation, and mechanism studies.
  • Formulation role in R&D: for in vitro assays, peptides are commonly formulated as DMSO or aqueous stock solutions and dispensed into assay buffers. No pharmacopeial monograph or excipient role is indicated for this item.

Regulatory note

  • Not formulated, tested, or intended for human or veterinary use, clinical diagnostics, or as a drug substance/product. No claims are made regarding GMP status, compendial compliance, sterility, apyrogenicity, or stability suitable for clinical applications.
Physical Properties

Item-specific physical data

  • 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.
  • Other specs (BP/MP, density, refractive index, logP, pKa): Not specified for this item; refer to CoA/Spec Sheet.

General/literature expectations for LVV‑hemorphin peptides (informational only; not specifications)

  • State: typically obtained as a white to off‑white amorphous solid or lyophilized powder.
  • Thermal behavior: peptides generally decompose before boiling; melting points (if observed) are often ill‑defined due to decomposition.
  • Solubility: frequently soluble in water, aqueous buffers (pH 4–8), and polar aprotic solvents (DMSO); initial dissolution may benefit from brief sonication. Salt form and terminal capping strongly affect solubility.
  • Isoelectric and charge: presence of basic residues (e.g., Arg) tends to increase solubility under acidic/neutral pH; exact pI depends on the precise sequence.
  • Hygroscopicity: many peptides are moderately hygroscopic; minimize ambient moisture exposure during weighing.

Practical guidance (general)

  • If solubility is uncertain, prepare a concentrated DMSO primary stock (e.g., 10–50 mM), then dilute into aqueous buffer with vigorous mixing to the desired working concentration while keeping final DMSO ≤1–2% v/v for most bioassays.
  • Filter sterilize working solutions (0.22 μm) for cell‑free biochemical assays if required by your protocol.
Quality and Grades

Item-specific grade

  • Grade/Purity: Moligand™ (as provided).

What Moligand™ implies (general description)

  • Moligand™ denotes a screening‑oriented research grade intended for discovery workflows (e.g., biochemical target engagement, binding studies, ligand profiling). While exact acceptance criteria vary by product, such grades typically emphasize identity confirmation and suitability for assay deployment rather than ultra‑trace impurity control for clinical use.

Quality considerations for peptide ligands (general guidance; not item specifications)

  • Identity and purity assessment: commonly verified by LC–MS and analytical HPLC; sequence confirmation via MS/MS when applicable. For assay reproducibility, request CoA data including purity trace, residual solvents, counter‑ion content, and water content when available.
  • Counter‑ion and salt form: TFA‑, acetate‑, or chloride‑salts are common; counter‑ions may influence solubility and bioassay background. The specific salt for this item is not specified here.
  • Endotoxin/bioburden: for purely biochemical assays, low bioburden is typically sufficient; cell‑based assays may require endotoxin information. Not specified for this item; refer to CoA/Spec Sheet.

Documentation

  • For definitive specifications (purity threshold, analytical methods, acceptance limits), consult the product’s CoA/Spec Sheet. Aladdin can provide lot‑specific analytical data on request for regulated or QA‑critical environments.
Reaction and Applications

Focus: As a Moligand™ peptide ligand, LVV‑hemorphin is intended for target binding and screening workflows rather than as a stoichiometric reagent.

Research/application contexts (general, literature-informed)

  • Target engagement studies: hemorphin‑family peptides are employed in biochemical assays to probe peptide–protein interactions relevant to peptidergic recognition sites.
  • Assay development: use as a positive control ligand or competitor in binding displacement, fluorescence polarization, SPR/BLI, or enzyme‑modulation assays where applicable.
  • Structure–activity exploration: LVV‑extensions are studied for their influence on affinity and stability relative to core hemorphins; sequence‑variant panels can map key residues.

Practical assay tips

  • Prepare concentrated primary stocks (e.g., 1–10 mM in DMSO or 1–5 mM in water/buffer depending on solubility). Verify concentration by UV at 280 nm when aromatic residues are present (use literature extinction coefficients) or by amino acid analysis.
  • Minimize adsorption: pre‑rinse plasticware with buffer containing 0.01% Tween‑20 or use low‑bind tubes/plates.
  • Control oxidation: protect Trp/Tyr‑containing peptides from light; consider working under subdued light and using freshly prepared solutions.

Synthesis/derivatization (if applicable to your workflow)

  • For mechanistic studies, N‑terminal acetylation or C‑terminal amidation analogs may be prepared to assess terminal charge effects; fluorescent tags (e.g., FITC, TAMRA) can facilitate binding readouts. These are separate custom derivatives and not part of this specific catalog item.
Reaction Conditions

Conventional reaction condition guidance (temperatures, catalysts, yields) does not apply: this product is a peptide ligand for assays rather than a reagent for chemical transformations.

Assay solution handling conditions (general guidance)

  • Reconstitution: dissolve at room temperature with gentle vortexing or brief sonication. If necessary, add DMSO incrementally to achieve complete dissolution before buffer dilution.
  • Working concentration: determine empirically from your assay’s dynamic range (e.g., use serial dilutions spanning expected KD/IC50 ranges when available in the literature for the specific sequence variant).
  • Temperature: prepare and run assays at temperatures recommended for the target (often 20–25°C for biophysical assays). Avoid prolonged exposure of solutions to elevated temperatures.
  • Light/oxygen: protect from strong light to limit oxidation of aromatic residues; use freshly prepared solutions or store aliquots under inert headspace when practical.
  • Compatibility: verify that plastics, surfactants, and carrier proteins do not interfere with your readout (fluorescence, MS, SPR, etc.).

All parameters above are general best practices and not specifications for this item.

Safety and Handling

GHS information (item-specific)

  • Signal Word: Not specified for this item; refer to SDS.
  • H‑Statements: Not specified for this item; refer to SDS.
  • GHS Classification/Pictograms: Not specified for this item; refer to SDS.

General safe handling for research peptides (informational; defer to SDS)

  • Avoid inhalation of dusts and contact with skin/eyes. Handle powder in a fume hood or ventilated enclosure.
  • Personal protective equipment: lab coat, nitrile gloves, and safety glasses as minimum; use respiratory protection if dust/aerosol formation is possible and local risk assessment indicates.
  • Incompatibilities: strong oxidizers may degrade peptide side chains; avoid prolonged exposure to strong acids/bases and elevated temperature.
  • Spill/accidental release: avoid dust; collect mechanically, then wet-wipe with appropriate detergent. Dispose of in accordance with institutional and local regulations.
  • First aid (overview): rinse eyes/skin with water for 15 minutes if contacted; remove contaminated clothing; if inhaled, move to fresh air; seek medical attention if symptoms persist. Always consult the SDS for authoritative instructions.
  • Thermal/photostability: aromatic residues (e.g., Trp/Tyr) can be light‑sensitive; protect solutions from strong light to minimize oxidation.
  • Waste considerations: classify and dispose as non‑halogenated organic laboratory waste unless institutional policy specifies otherwise for peptide materials.
Solvent Selection

Applicability: LVV‑hemorphin is a peptide ligand; solvent choice focuses on achieving complete dissolution while preserving integrity for screening assays.

General solvent/miscibility profile (literature/guidance)

  • Primary: water or aqueous buffers (pH ~4–8) are often suitable depending on exact sequence and salt form.
  • Cosolvents: DMSO is widely used for high‑concentration primary stocks; DMF can dissolve many peptides but is less common for biological assays.
  • Miscibility: DMSO mixes freely with water; when diluting, add DMSO stocks slowly into vigorously stirred buffer to avoid localized precipitation.

Practical selection tips

  • Start with Milli‑Q water or assay buffer. If insoluble, add small aliquots of DMSO (up to 10–20% v/v for stock preparation) until fully dissolved; then dilute to working strength keeping final DMSO ≤1–2% v/v for most assays.
  • pH leverage: modest acidification (e.g., acetate buffer pH 4.5–5.5) can enhance solubility of basic peptides; avoid extremes that risk backbone/side‑chain hydrolysis.
  • Additives: 0.01–0.1% nonionic surfactant (e.g., Tween‑20) or carrier protein (e.g., BSA) can reduce nonspecific adsorption in binding assays; confirm compatibility with your readout.

When to choose alternatives

  • If oxidation of aromatic residues is a concern, minimize exposure to oxygen, trace metals, and intense light; consider freshly degassed buffers and addition of benign antioxidants (e.g., methionine as scavenger) where compatible.
Storage and Reconstitution

Item-specific storage

  • Storage Conditions (as provided): Room temperature.
  • Shipped In: Not specified for this item; refer to CoA/Spec Sheet.

General storage guidance for peptide ligands (complementary; not to contradict item data)

  • Keep container tightly closed, desiccated, and protected from light at the specified storage temperature. Minimize headspace to reduce moisture ingress.
  • For long-term retention of activity after opening, many users transfer material to a desiccator or dry cabinet; verify compatibility with the packaging.

Reconstitution (general guidance)

  • Solvents: water or assay buffer preferred; use DMSO to aid dissolution if needed. Mix gently; brief sonication can help.
  • Concentration verification: determine using UV at 280 nm when applicable (sequence‑dependent) or by amino acid analysis.
  • Aliquoting: prepare single‑use aliquots of stock solutions to avoid repeated freeze–thaw and adsorption losses.
  • Solution storage: if solutions must be stored, keep refrigerated or frozen (e.g., 2–8°C short‑term; −20°C for longer‑term) and protect from light. Actual stability is sequence‑ and matrix‑dependent; verify empirically for your assay.

Always consult the product CoA/Spec Sheet and SDS for lot‑specific handling and storage instructions.

Structure and Identity

Brief description: LVV‑hemorphin refers to an N‑terminally extended member of the hemorphin peptide family derived from the β‑globin (hemoglobin) sequence. It is supplied here as a Moligand™ screening-grade research ligand.

  • Item-specific identifiers (from Product Data)

    • SKU: rp174478
    • Product Name: LVV-hemorphin
    • CAS: rp174478 (catalog placeholder)
    • InChIKey: 234273 (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.

  • Structural class and features (general/literature)

    • Chemical class: endogenous hemoglobin‑derived peptide (hemorphin family).
    • Typical features: backbone of L‑α‑amino acids with peptide bonds; side chains commonly include hydrophobic (Leu/Val), aromatic (Tyr/Trp/Phe), and basic (Arg) residues depending on length variant.
    • N‑terminal “LVV” extension distinguishes LVV‑hemorphins from core hemorphins (general naming convention).

  • 2D structural description (general)

    • Linear peptide with free or protected termini depending on synthesis; amide bonds linking α‑amino and α‑carboxyl groups in sequence order; side chains decorate the backbone with one phenolic ring (Tyr) and one indole (Trp) in common LVV‑hemorphin variants.

Notes

  • Specific sequence, stereochemistry at each residue, counter‑ions, and terminal modifications are not specified for this catalog item; consult the CoA/Spec Sheet for definitive structural details.
Synthetic Utility

Not a general synthetic building block: LVV‑hemorphin is a finished peptide ligand intended for biochemical screening rather than as a reagent or intermediate in multistep organic synthesis.

Relevant utility in chemical biology (general)

  • Positive control/competitor: employ in binding or enzymatic assays to benchmark or displace probe ligands.
  • SAR benchmarking: compare activity of LVV‑extended hemorphins to truncated analogs to delineate residue contributions to binding.
  • Conjugation handles (sequence‑dependent): if the provided sequence includes Lys/Tyr or N‑terminus, standard bioconjugation chemistries (e.g., NHS‑ester acylation at primary amines, diazonium coupling at Tyr, maleimide if Cys present in analogs) can be explored in separate derivative syntheses. These are not attributes of the current item unless explicitly specified in the CoA.

If your goal is chemical synthesis, consider ordering protected amino acids and resins for SPPS to prepare custom hemorphin variants rather than repurposing this screening‑grade ligand.

Target Specificity

Item-specific target data

  • Antigen/target name, epitope, species reactivity, clone/isotype: Not specified for this item; refer to CoA/Spec Sheet.

General note

  • Hemorphin family peptides have been studied against multiple protein targets in the literature. However, target specificity depends critically on the exact sequence, length, and modifications, which are not defined here for this catalog entry. Users should consult primary literature relevant to the precise LVV‑hemorphin variant they intend to model or benchmark.

Need help choosing the grade?

Our grade selection guide covers purity, stabilizer status, and application suitability for all variants in our catalog.

View Moligand™ grade guide →
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