Cartilage Peptides - BioReagent, Protein (Dry Basis) ≥50%; Chondroitin Sulfate ≥28%

Cat. No.: C1526972
Disponible para pedir
GRADE & PURITY BioReagent ? BioReagent grade — tested suitable for life-science and molecular-biology use. Use for cell culture, assays, and biochemical work needing biological compatibility. Protein (Dry Basis) ≥50%; Chondroitin Sulfate ≥28%
Synonyms
Cartilage Peptide Powder
Storage
Protected from light,Room temperature
Shipped In
Normal
★
Size
Alemania (EU)
USA*
Price
Qty
100g
C1526972-100g
Fabricado bajo pedido · 8–12 semanas
69,33€
500g
C1526972-500g
Fabricado bajo pedido · 8–12 semanas
225,53€
1kg
C1526972-1kg
Fabricado bajo pedido · 8–12 semanas
347,01€
Enter a quantity for the sizes you want to add.
🧪
Why this grade

BioReagent, Protein (Dry Basis) ≥50%; Chondroitin Sulfate ≥28% BioReagent for sensitive chromatographic and analytical workflows requiring minimal baseline interference.

🌡

Storage & shipping

Protected from light,Room temperature Ships Normal Check lot-specific COA for exact specifications.

📋

Quality documents

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

📚

Literature proof

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

Descripción general

This product is a light‑yellow loose powder, free of caking, peculiar odors and visible impurities. It is prepared from chicken breast cartilage by targeted enzymatic hydrolysis. The product features low molecular‑weight distribution and good water‑solubility, with excellent thermal‑acid stability. Its components include cartilage‑derived small‑molecule peptides and chondroitin sulfate. It can be used for formula development of general foods, health foods and relevant scientific research.

Specifications

Sinónimos
Cartilage Peptide Powder
Especificaciones y pureza
BioReagent, Protein (Dry Basis) ≥50%; Chondroitin Sulfate ≥28%
Estabilidad y almacenamiento
Store at room temperature long term (36 months). Store in the dark.
Condiciones de almacenamiento de almacenamiento
Protected from light,Room temperature
Enviado en
Normal
Grado
BioReagent
Product Line
biological_products

Documentation

📋 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

Certificados (CoA, COO, BSE/TSE y tabla de análisis)
C of A & Other Certificates(BSE/TSE, COO):
Analytical Chart:
Propiedades químicas y físicas
SensibilidadLight-sensitive
Preguntas frecuentes y artículos
Calculadoras de soluciones
Reseñas

Reseñas de cliente

Application Protocols

No tested application protocols are provided for this item; refer to CoA/Spec Sheet for any lot-specific guidance.

General, literature-based starting points (to be optimized):

  • Stock preparation: Weigh under low humidity. Dissolve to 1–10 mg/mL in water, PBS, or suitable buffer; for hydrophobic content, pre-wet with minimal DMSO or MeCN before aqueous dilution. Filter sterilize (0.22 µm) if required. Record exact solvent composition.
  • Surface coating (non-covalent): Incubate clean tissue-culture plastic or glass with 10–200 µg/mL peptide solution in PBS for 1–2 h at 22–37°C or overnight at 4°C. Rinse gently with buffer before use. Validate coating stability.
  • Covalent immobilization (example): Activate carboxylated hydrogel with EDC/NHS in MES pH 5.5 (15–30 min), rinse, then incubate with peptide (0.1–2 mg/mL) in PBS/HEPES pH 7.4 for 1–2 h. Quench unreacted sites (e.g., ethanolamine). Verify via colorimetric amine assay or LC–MS of wash fractions.
  • Cell-based assays: After dilution into complete media, keep residual DMSO ≤0.1–0.5% (literature). Include vehicle controls to account for solvent effects.

All parameters should be validated for the specific lot and application.

Biological Roles

Biological roles below are general literature context for cartilage-related peptides and are not specific to the composition of this item.

  • ECM signaling: Short peptide motifs derived from cartilage ECM proteins (e.g., collagens, aggrecan-associated sequences) can interact with cell-surface receptors (integrins, syndecans), influencing adhesion, morphology, and intracellular signaling in vitro.
  • Matrix assembly and turnover: Peptides produced by proteolysis of ECM components can act as matrikines—bioactive fragments that modulate cell behavior or enzyme activity during tissue remodeling (literature concept).
  • Growth factor interaction: Certain ECM-derived sequences can bind or sequester growth factors, altering their local concentration and bioavailability in model systems.
  • Chondrocyte phenotype studies: Defined peptides are often used to examine how ECM cues regulate gene expression and matrix production in cultured cells (research setting).

Important: The specific sequences, activities, or receptor interactions of this product are not provided. Any biological roles for this item must be established experimentally in the user’s system. This product is for research use only and not intended for diagnostic or therapeutic applications.

Buffer Applications

No dedicated “buffering” functionality is implied for this product. However, appropriate buffers are essential for preparing peptide solutions for research use.

General, literature-based guidance:

  • Common buffers: PBS (pH 7.2–7.4), HEPES (pH 7.2–7.6), or Tris (pH 7.4–8.0) depending on downstream assay. Choose buffers that do not interfere with readouts (e.g., avoid Tris when using NHS-ester coupling).
  • Ionic strength: 100–150 mM NaCl is typical for physiological assays; adjust to maintain peptide solubility and prevent aggregation.
  • Additives: 0.01–0.1% nonionic surfactants (e.g., Tween-20) can reduce nonspecific adsorption to plastics in some assays; validate for your system.
  • pH adjustment for dissolution:
    • Acidic peptides: initiate in mildly basic buffer (e.g., 0.1 M NH4HCO3).
    • Basic peptides: initiate in mildly acidic buffer (e.g., 0.1–1% acetic acid), then adjust to assay pH.
  • Sterility: Filter through 0.22 µm membranes for cell-based experiments; confirm that filtration does not significantly adsorb peptide content.

Note: Specific buffer recipes and working concentrations for this item are not provided; optimize empirically given the mixture’s composition.

Green Alternatives

For peptide handling, “green” considerations relate mainly to solvent use and process design rather than replacing the peptide itself.

Greener handling strategies (general, literature):

  • Favor aqueous systems: Dissolve and formulate in water, PBS, or HEPES where feasible, minimizing reliance on high-toxicity organic solvents.
  • Minimize DMSO/MeCN: Use the smallest possible volume for initial dissolution of hydrophobic content, then dilute into aqueous buffer. Evaporate volatile organics under gentle conditions when appropriate.
  • Avoid halogenated solvents: Typically unnecessary for peptide dissolution and less desirable environmentally.
  • Room-temperature processing: This item is stored at room temperature protected from light; plan workflows that avoid energy-intensive cooling or heating unless stability studies indicate need.
  • Waste reduction: Prepare only the volume required for immediate experiments; design experiments to use smaller stock concentrations to reduce expired waste.

Illustrative comparison (general):

  • Aqueous buffers vs DMSO/MeCN:
    • Environmental impact: lower for aqueous buffers.
    • Biocompatibility: higher for aqueous buffers.
    • Solubilizing power: higher for DMSO/MeCN (tradeoff).

Conclusion: Start with aqueous buffers; resort to minimal amounts of organic cosolvent only when necessary to achieve complete dissolution.

Pharmaceutical Uses

No pharmaceutical or clinical uses are claimed or implied for this research product.

General, non-clinical context (literature):

  • Formulation research: ECM-related peptides are sometimes explored as excipient-like components or surface modifiers in prototype delivery systems (e.g., biomaterial coatings) during preclinical R&D. Such uses require rigorous characterization of identity, purity, and bioburden that are not specified here.
  • Analytical development: Peptides may be employed as reference materials, process surrogates, or system suitability standards in method development (e.g., LC–MS), provided composition is well characterized for the intended purpose.
  • Device/biomaterial R&D: Peptide motifs can be grafted onto polymers or surfaces to tune cell interactions in investigative settings.

Important: This product is sold for research use only and is not produced under GMP. It is not intended for use as an active pharmaceutical ingredient, excipient in marketed formulations, or for any clinical application.

Physical Properties

Item-specific physical properties are not provided in the Product Data for this mixture.

  • Molecular weight distribution: Not specified for this item; refer to CoA/Spec Sheet.
  • Molecular formula: Not applicable to mixtures; not specified for this item.
  • Appearance: Not specified for this item; refer to CoA/Spec Sheet.
  • Solubility (general, literature guidance for peptide mixtures):
    • Often soluble in water, PBS, or dilute acids/bases depending on net charge and hydrophobicity.
    • For hydrophobic sequences, co-solvents such as DMSO or small amounts of acetonitrile can assist initial dissolution before dilution into aqueous buffer. Final DMSO content in biological assays is commonly kept ≤0.1–0.5% (literature practice).
  • pKa/logP/refractive index/density, MP/BP: Not specified for this item (mixtures typically lack single-valued constants).
  • Hygroscopicity: Many peptides are mildly hygroscopic; handle quickly in ambient humidity (general practice). Item-specific behavior not specified.

Important: For lot-specific peptide content, residual moisture, counterions (e.g., TFA, acetate, chloride), and residual solvent information, consult the CoA. Do not assume exact values without documentation.

Quality and Grades
  • Grade: BioReagent (per Product Data). Typically indicates suitability for biological research applications such as biochemical assays or cell culture research, with attention to common research contaminants (e.g., microbial bioburden, residual solvents). Exact acceptance criteria for this specific item are not specified; refer to CoA/Spec Sheet.
  • Purity/Composition: Not specified for this item. For peptide mixtures, suppliers may report parameters such as peptide content, moisture, counterion identity (e.g., acetate vs TFA), and residual solvents—verify lot documentation.
  • Stabilizers/Preservatives: Not specified for this item.
  • Endotoxin/bioburden: Not specified for this item. If your application is endotoxin-sensitive, request supporting documentation or perform in-house testing (e.g., LAL assay).
  • Functional verification: For ECM-related peptide mixtures, labs often verify performance using adhesion assays, biochemical binding readouts, or spectroscopic profiling (e.g., LC–MS, amino acid analysis). Recommended where performance is critical.

Guidance on selection:

  • Use BioReagent grade for exploratory biological experiments. For GMP or clinical manufacturing, obtain materials produced under appropriate quality systems (not covered by this listing).
Reaction and Applications

Manufacturer Applications: Not specified in the Product Data.

General research applications for cartilage-associated peptide mixtures (literature context; not item-specific):

  • ECM-mimetic coatings and hydrogels: Incorporation into natural or synthetic matrices (e.g., collagen, gelatin, PEG, hyaluronan) to modulate cell adhesion, spreading, and phenotype in chondrocyte or mesenchymal stem cell culture.
  • Ligand–receptor studies: Use of defined ECM-related motifs to probe integrin binding, growth factor sequestration, or matrix assembly pathways.
  • Proteomics/biochemistry: Standards or substrates for enzyme studies (e.g., matrix metalloproteinases, aggrecanases) to evaluate cleavage preferences in vitro.
  • Bioassay development: Positive controls for antibody binding (when sequences are known) or to establish baseline matrix-derived peptide responses.

Practical tips (literature):

  • Work at low micromolar to millimolar ranges depending on assay sensitivity; optimize empirically due to mixture complexity.
  • Minimize freeze–thaw cycles; aliquot stock solutions.
  • For surface coatings, pre-treat substrates (e.g., plasma or chemical activation) and consider crosslinkers (e.g., NHS–ester chemistry) for immobilization.

Note: Because this item’s exact sequences and composition are not specified, verify performance in your intended assay using small pilot experiments and orthogonal analytics (HPLC/LC–MS) where necessary.

Reaction Conditions

No item-specific reaction conditions are provided. The following are general, literature-based conditions for common peptide conjugation workflows; applicability depends on functional groups present in the mixture.

  • EDC/NHS carboxyl–amine coupling:
    • Solvent: MES buffer pH 5.0–6.0 (activation), then pH 7.0–8.0 (coupling) in PBS/HEPES.
    • Temperature: ambient (20–25°C).
    • Time: 0.5–4 h for activation/coupling; monitor by TNBS/TNBSA assay.
  • NHS-ester coupling (pre-activated surfaces/polymers):
    • Solvent: PBS or carbonate buffer pH 8.3–8.5 (amines deprotonated).
    • Temperature: ambient.
    • Time: 0.5–2 h; protect from moisture and hydrolysis.
  • Maleimide–thiol coupling:
    • Solvent: PBS/HEPES pH 6.5–7.0 (limits maleimide hydrolysis).
    • Reducing conditions: brief pre-treatment with TCEP (0.1–1 mM) if disulfides present; remove excess before coupling.
    • Time/Temp: 0.5–2 h at ambient.
  • Click chemistry (CuAAC):
    • Solvent: water/t-BuOH or water/DMSO mixtures; CuSO4/ligand + sodium ascorbate as catalyst (handle copper with care in biological contexts).
    • pH: near-neutral; degas to limit oxidation.

Expected yields: Highly system-dependent for mixtures; quantify functional incorporation using appropriate surface or bulk analytical methods rather than assuming stoichiometric yields.

Safety and Handling

GHS/CLP information for this item is not specified; consult the SDS for authoritative safety data.

  • Signal word / H-statements / Pictograms: Not specified for this item; refer to SDS.
  • General laboratory precautions (good practice for peptide powders/solutions):
    • Avoid inhalation of dust/aerosols; handle powders in a fume hood or ventilated enclosure.
    • Wear appropriate PPE: lab coat, nitrile gloves, safety glasses. Consider double-gloving if using organic co-solvents (e.g., DMSO).
    • Prevent contact with skin and eyes; wash thoroughly after handling.
    • Avoid microbial contamination; prepare solutions using sterile technique if intended for cell-based work (research use only).
  • Incompatibilities (general):
    • Strong oxidizers may degrade sensitive residues (e.g., Met, Cys, Trp).
    • Prolonged exposure to light can promote photo-oxidation of aromatic/sulfur residues—this item specifies: store protected from light.
    • Elevated temperatures and extreme pH can accelerate hydrolysis/deamidation.
  • First aid (overview; follow SDS):
    • Inhalation: move to fresh air; seek medical attention if symptoms persist.
    • Skin/eye contact: rinse with water for several minutes; remove contaminated clothing; seek medical advice if irritation continues.
    • Ingestion: rinse mouth; do not induce vomiting; obtain medical attention.
  • Waste: Dispose according to local regulations for laboratory chemical waste; avoid drain disposal unless permitted by institutional policy.

Note: This product is designated for research use only.

Solvent Selection

This product is a peptide mixture; solvent choice should be guided by charge/hydrophobicity of the specific lot (consult CoA if available).

General/literature guidance:

  • Primary solvents for initial dissolution:
    • Water or aqueous buffers (e.g., PBS pH 7.2–7.4, HEPES pH 7.2–7.6) for hydrophilic/charged peptides.
    • Dilute acid (0.1–1% acetic acid or 0.1% TFA) can protonate basic residues and facilitate solubility.
    • Dilute base (e.g., 0.1 M NH4HCO3) can help dissolve acidic peptides by deprotonation.
    • DMSO or small volumes of acetonitrile (MeCN) for highly hydrophobic sequences; then dilute into aqueous media while avoiding precipitation (keep final DMSO ≤0.1–0.5% in cell assays; literature guidance).
  • Miscibility and order of operations:
    • For hydrophobic material, dissolve first in DMSO/MeCN, then slowly add buffer with gentle mixing to prevent aggregation.
    • Filter sterilize (0.22 µm) if required for cell-based assays; test for adsorption losses on filters.
  • pH considerations:
    • Maintain near-neutral pH for most biological assays; avoid extremes that can promote hydrolysis or deamidation.

Comparison (literature trends):

  • Water/PBS: biocompatible, simplest; limited for hydrophobic content.
  • HEPES buffer: good pH control around neutrality and low temperature sensitivity.
  • DMSO: powerful cosolvent; potential cytotoxicity at higher percentages; can interact with some assays.
  • MeCN: useful for stock solutions; volatile; mix cautiously with aqueous buffers.
Storage and Reconstitution

Storage (from Product Data):

  • Store protected from light, at room temperature. Shipments: Normal (ambient) shipping.

Additional guidance (general best practices; not item-specific):

  • Keep container tightly closed with desiccant to limit moisture uptake. Open vials briefly and allow to equilibrate to room temperature before opening to minimize condensation.
  • If supplied as a solution (not specified), avoid repeated freeze–thaw; prepare single-use aliquots.

Reconstitution (general, literature-based):

  • Use sterile water or buffer (e.g., PBS, HEPES) appropriate for downstream assays. For hydrophobic content, dissolve first in a minimal volume of DMSO or MeCN, then dilute with buffer while mixing.
  • Target stock concentrations commonly 1–10 mg/mL, adjusted to solubility and assay needs. Record solvent composition and pH.
  • After reconstitution, store working solutions protected from light. If permitted by your workflow and stability tests, short-term storage at 2–8°C is common; for longer-term storage, users often aliquot and keep at lower temperatures. However, specific stability data for this item are not specified; refer to CoA/Spec Sheet.

Research Use Only: Not for human or animal therapeutic use.

Structure and Identity

Item-specific identity parameters (empirical formula, exact sequence, and average molecular weight distribution) are not specified for this item; refer to CoA/Spec Sheet.

General/literature context for “cartilage peptides”:

  • These materials typically comprise a heterogeneous mixture of short to medium-length peptides derived from, or designed to mimic, extracellular matrix (ECM) sequences associated with cartilage (e.g., collagen- and proteoglycan-related motifs). Exact composition varies by lot and source.
  • Structural features (general):
    • Backbone: repeating amide bonds (–CO–NH–) characteristic of peptides.
    • Side chains: mixture of acidic (Asp/Glu), basic (Lys/Arg/His), polar (Ser/Thr/Asn/Gln), hydrophobic (Ala/Val/Leu/Ile/Phe), and possibly sulfur-containing (Cys/Met) residues. Presence and ratio are item-specific.
    • Potential functional motifs (literature): cell-adhesive sequences (e.g., RGD-like), collagen-mimetic triplets (e.g., Gly–X–Y repeats), or aggrecan/versican-related fragments; applicability to this item is not specified.
  • Stereochemistry: amino acids in research peptides are commonly L-configured; however, specific stereochemistry for this item is not specified.
  • 2D structural description: linear (and possibly cyclic) peptidic chains composed of alpha-amino acids joined by peptide bonds; terminal functional groups may include free N-termini (–NH2/–NH3+) and C-termini (–COOH/–COO–), or be capped—item-specific.
  • Identifiers:
    • CAS: Not specified.
    • SMILES / InChIKey / CID: Not specified for complex peptide mixtures.

Conclusion: Treat as a peptide mixture with undefined sequence distribution unless the accompanying CoA provides explicit characterization.

Synthetic Utility

While not a classical “building block” with defined structure, peptide mixtures can be used functionally in conjugation and materials chemistry. The guidance below is general/literature-based and not specific to the exact composition of this item.

  • Conjugation handles: Primary amines (N-termini, Lys), carboxylates (C-termini, Asp/Glu), thiols (Cys), and aromatics (Tyr/Trp) enable diverse coupling strategies.
  • Typical transformations:
    • NHS-ester/EDC coupling to link peptides to carboxyl- or amine-functionalized polymers and surfaces.
    • Maleimide–thiol chemistry for site-selective attachment via Cys residues.
    • Click chemistry (CuAAC/SPAAC) when azide/alkyne groups are introduced synthetically.
    • Enzymatic ligation or sortase-mediated coupling where compatible motifs exist (requires defined sequences; not guaranteed for this item).
  • Materials integration: Immobilization within hydrogels (PEG, HA, gelatin) to present bioactive motifs; density and spatial patterning modulate cell responses (optimize empirically).
  • Analytical control: For mixtures, characterize pre- and post-coupling using LC–MS, amino acid analysis, or ninhydrin/TNBSA assays to quantify accessible amines.

Caveats:

  • Mixture complexity hinders stoichiometric planning; perform small-scale screens to refine coupling conditions.
  • Protect from light during reactions to limit oxidation; maintain neutral pH when possible to reduce side reactions (e.g., asparagine deamidation).
Target Specificity

Not specified for this item; refer to CoA/Spec Sheet.

Note: This product is not supplied as an antibody or affinity reagent with defined antigen/epitope specificity. Any receptor or matrix-binding properties must be determined experimentally for each application.

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