Tirzepatide7 OF 7 FORMATS AVAILABLE
Tirzepatide
Dual incretin agonist research material
INDEXABLE RESEARCH CATALOG / DIRECT CATALOG PRICING
Metabolic research materials
Browse 10 cataloged metabolic research materials, with current formats, listed pricing, and availability. Categories support navigation only and do not establish safety, efficacy, approval, or intended use.
TirzepatideRetatrutide3 OF 3 FORMATS AVAILABLE
Retatrutide
Triple agonist research material
Cagrilintide0 OF 2 FORMATS AVAILABLE
Cagrilintide
Long-acting amylin analogue
MOTS-c1 OF 1 FORMATS AVAILABLE
MOTS-c
Mitochondrial-derived research peptide
AOD-96041 OF 1 FORMATS AVAILABLE
AOD-9604
Modified growth-hormone fragment
Humanin0 OF 1 FORMATS AVAILABLE
Humanin
Mitochondrial-derived research peptide
NAD+ Buffered1 OF 1 FORMATS AVAILABLE
NAD+ Buffered
Buffered nicotinamide adenine dinucleotide research material
NAD+1 OF 1 FORMATS AVAILABLE
NAD+
Nicotinamide adenine dinucleotide research material
5-Amino-1MQ0 OF 2 FORMATS AVAILABLE
5-Amino-1MQ
NNMT-pathway research compound
SLU-PP-3320 OF 1 FORMATS AVAILABLE
SLU-PP-332
ERR-pathway research compound
RESEARCH MATERIALS / CLEARLY CATALOGED
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CATALOG / QUICK START
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VIAL FORMAT / LAB HANDLING
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Reconstituted for research.
PSC catalog items are supplied as lyophilized—freeze-dried—research material.
Reconstitution is required before research use. Solvent choice and procedure vary by material; use a validated compound-specific protocol.
Store unopened lyophilized vials frozen. After reconstitution, refrigerate for short-term research handling unless a validated compound-specific protocol requires different conditions.
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61RESEARCH PEPTIDES
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- 01SHOPChoose a research peptide
Browse available peptides and prices in the retail single-vial catalog.
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MOLECULAR FIELD GUIDE / 02
Peptide science,
mapped visually.
A peptide is not defined by a marketing category. Its amino-acid order, side-chain chemistry, charge, flexibility, and three-dimensional ensemble shape what researchers can observe.
01 / PEPTIDE ANATOMYNCBI SOURCE ↗
A chain with direction.
Amino acids are linked head-to-tail by covalent peptide bonds. By convention, a sequence is written from its amino terminus to its carboxyl terminus: N → C.
H₂N→ALA—GLY—SER—LEU→COOH
NONPOLARALA · VAL · LEU
Side chains that tend to avoid water.
POLARSER · THR · GLN
Side chains that form favorable polar interactions.
ACIDICASP · GLU
Often negatively charged near neutral pH.
BASICLYS · ARG · HIS
Often positively charged, depending on pH.
Property groups are simplified teaching categories; charge and behavior depend on the full sequence and experimental environment.
COMMON BUILDING BLOCKS
One alphabet, enormous variety.
Proteins commonly use 20 encoded amino acids. Reordering even a short chain produces a different primary sequence.
CONFORMATIONAL ENSEMBLE
Shape is more than a static model.
Hydrogen bonding, charge, hydrophobic effects, backbone flexibility, and disulfide bridges can favor different conformations.
CELL SIGNALING
Binding starts a conversation.
Many peptide signals bind cell-surface receptors, which can relay information through intracellular messengers and kinase cascades.
STEPWISE SYNTHESIS
Built one residue at a time.
Solid-phase peptide synthesis anchors a growing chain to a support so amino acids can be added sequentially.
SEQUENCE-TO-SIGNAL MODEL
How a research question moves from molecule to measurement.
Which residues, in what order?
Charge, polarity, and hydrophobicity.
Flexible shapes available to the chain.
Recognition, affinity, and selectivity.
The measured response in a defined model.
Conceptual research map only. A category or binding observation does not establish a health benefit, treatment, safety, or intended use.
PEPTIDE ARCHITECTURE / 03
Small chains.
Complex signals.
Peptides are short chains of amino acids joined by peptide bonds. Their sequence, length, charge, and three-dimensional conformation shape how they behave in laboratory models.
Hydrophobic Polar Charged
Illustrative amino-acid chain—not a product-specific sequence.
PRIMARY STRUCTUREN-TERMINUS → C-TERMINUS
01020304050607
Sequence variants
Researchers compare residue substitutions, truncations, cyclization, and conjugation to study how structure changes an observed interaction.
Affinity is not the whole story
Association, dissociation, receptor selectivity, and experimental context all influence how binding data are interpreted.
Peptides can change over time
Proteolysis, oxidation, deamidation, adsorption, precipitation, and aggregation are distinct research considerations.
Research areas describe subjects of laboratory investigation—not established health benefits, treatments, or intended uses.
RESEARCH READING / 04
Go deeper than a product name.
Authoritative starting points for understanding peptide chemistry, cell signaling, synthesis, stability, and regulatory status. Open the full searchable research library →
From amino-acid sequence to three-dimensional shape
Learn how peptide bonds create a directional chain and how residue chemistry and noncovalent interactions influence molecular structure.
Open NCBI chapter ↗How peptides communicate with cells
A clear introduction to peptide hormones, neuropeptides, growth factors, receptors, and intracellular signal relay.
Explore cell signaling ↗Building peptide chains on a solid support
How Merrifield's stepwise solid-phase method changed peptide synthesis and made automated chain construction possible.
Read the Nobel overview ↗Why peptide molecules can change
An overview of sequence- and environment-dependent oxidation, hydrolysis, adsorption, precipitation, and aggregation.
Read on PubMed Central ↗Peptide versus protein is not a hard wall
Scientific and regulatory communities use overlapping size conventions, so context matters more than one universal residue cutoff.
Review the terminology ↗Research status is not drug approval
Being studied, listed as research material, and FDA-approved are different statuses. Drugs@FDA is the live source for approved drug records.
Check Drugs@FDA ↗