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What are peptides?

Peptides are short chains of amino acids (typically 2–50 residues) that serve as versatile tools in biochemical research. They mimic natural sequences found in proteins and hormones, allowing scientists to probe receptor interactions, enzymatic pathways, cellular signaling, and structural biology. Common research includes binding affinity assays, pharmacokinetics, and in vitro/in vivo modeling. Peptides are synthesized via solid-phase methods for high consistency and are often lyophilized for stability.

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🧬 Retalynt™ (Retatrutide)

Category: Dual GLP-1/GIP receptor agonist

Chemical Structure: A synthetic 39-amino acid peptide with modifications for enhanced stability, including fatty acid conjugation for prolonged half-life (similar to tripeptide analogs). Sequence features GLP-1 and GIP mimetic domains fused for dual agonism.

Historical Development: Developed in the early 2020s as an advancement over single-receptor agonists, first reported in pharmaceutical patents around 2021 for metabolic research. Builds on GLP-1/GIP fusion concepts from earlier incretin studies.

Research Applications: Explored in models of receptor co-activation, including dual incretin signaling pathways, energy homeostasis, and glucose-dependent insulinotropic effects. Commonly used in cell culture assays for receptor binding (Kd values ~0.1-1 nM), animal models for pharmacokinetic profiling (half-life ~7-10 days), and combination studies with other metabolic modulators. Potential for high-throughput screening in obesity-related biochemistry.

Purity: ≥99% (HPLC verified, with COA including mass spectrometry data).

Reconstitution: Dissolve in 1–2 mL bacteriostatic water (0.9% benzyl alcohol); gently swirl to avoid foaming. Final concentration typically 5-10 mg/mL for dosing accuracy.

Storage: −20 °C for lyophilized powder (stable 2+ years); 2–8 °C for reconstituted solution (use within 2-4 weeks to prevent degradation). Avoid freeze-thaw cycles.

Experimental Considerations: Sensitive to pH (optimal 7.0-7.4); monitor for aggregation in high-concentration stocks. Research often involves ELISA for receptor activation quantification.

🧬 Velatix™ (Tirzepatide)

Category: Dual GLP-1/GIP receptor agonist

Chemical Structure: 39-amino acid chain with C-terminal amidation and acylation for albumin binding, extending half-life. Incorporates Aib (aminoisobutyric acid) substitutions for protease resistance.

Historical Development: Patented in 2016 as a GIP/GLP-1 hybrid, emerging from incretin research in the 2010s aimed at multi-receptor targeting. First synthesized for diabetes modeling studies.

Research Applications: Investigated in insulin secretion pathways, beta-cell function assays, and lipid metabolism models. Used in rodent studies for dose-response curves (EC50 ~0.05-0.5 nM), ex vivo tissue experiments for GIP/GLP-1 synergy, and long-term stability tests in simulated physiological buffers. Valuable for comparative analyses with mono-agonists.

Purity: ≥99% (HPLC, with impurity profile <0.5% per peak).

Reconstitution: 1-2 mL sterile water or saline; agitate minimally to preserve structure. Aim for 2-5 mg/mL.

Storage: −20 °C dry (shelf life 24+ months); 2–8 °C reconstituted (stable 4-6 weeks). Protect from light.

Experimental Considerations: Half-life extension via acylation requires albumin-free media in some assays; monitor pH sensitivity (avoid extremes).

🧬 Semalor™ (Semaglutide)

Category: GLP-1 receptor analog

Chemical Structure: 31-amino acid sequence with Lys26 acylation and Aib8 substitution for DPP-4 resistance, mimicking native GLP-1 but with extended pharmacokinetics.

Historical Development: Introduced in 2008 patents, derived from exendin-4/GLP-1 hybrid research in the 2000s for prolonged action. Widely adopted in metabolic labs by 2010s.

Research Applications: Studied in appetite signaling cascades, receptor desensitization models, and glycemic variability simulations. Employed in binding kinetics (Kd ~0.1 nM), once-weekly dosing protocols in animal models, and in vitro assays for cAMP production. Often benchmarked against native GLP-1 for half-life comparisons (~12-14 hours vs. minutes).

Purity: ≥98% (HPLC, MS confirmation).

Reconstitution: 1 mL bacteriostatic water; swirl gently. Typical concentration 1-5 mg/mL.

Storage: −20 °C powder; 2–8 °C solution (up to 4 weeks).

Experimental Considerations: Prone to fibril formation if agitated; use in neutral pH buffers for stability.

🧬 NotionVault™ (BPC-157)

Category: Body Protection Compound

Chemical Structure: 15-amino acid synthetic fragment (Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val) from gastric pentadecapeptide. Highly stable, no modifications needed.

Historical Development: Isolated in the 1990s from human gastric juice, synthesized for research in 2000s focusing on regenerative pathways. Gained traction in wound healing labs post-2010.

Research Applications: Examined in tissue integrity models, cytokine modulation, and extracellular matrix remodeling. Used in cell migration assays (scratch tests), rodent injury models for healing kinetics, and combination studies with growth factors. Noted for NO-independent vasoprotection in vascular research.

Purity: ≥99% (HPLC, with TFA salt form standard).

Reconstitution: 1-2 mL sterile saline; stable at room temp briefly during prep. 5 mg/mL common.

Storage: −20 °C dry (3+ years); 2–8 °C reconstituted (2-4 weeks).

Experimental Considerations: Oral bioavailability in models; avoid metal chelators in buffers.

🧬 ThermaBind™ (TB-500)

Category: Thymosin Beta-4 fragment

Chemical Structure: 43-amino acid actin-sequestering peptide (Ac-LKKTETQ), N-acetylated for stability. Derived from thymosin beta-4.

Historical Development: Fragmented from thymosin beta-4 in 1980s immunology research, popularized in 2000s for repair models.

Research Applications: Investigated in actin cytoskeleton dynamics, endothelial cell migration, and ischemia models. Applied in Boyden chamber assays for chemotaxis, cardiac tissue cultures for angiogenesis, and dermal punch wound studies. Synergistic with VEGF in vascular research.

Purity: ≥98% (HPLC).

Reconstitution: 1 mL water; 2-5 mg/mL.

Storage: −20 °C powder; 2–8 °C solution.

Experimental Considerations: Binds G-actin tightly; use in serum-free media for purity.

🧬 MelanoSyn™ (Melanotan I)

Category: Alpha-MSH analog

Chemical Structure: 13-amino acid linear peptide (Ac-Ser-Tyr-Ser-Nle-Glu-His-D-Phe-Arg-Trp-Gly-Lys-Pro-Val-NH2) with Nle4/D-Phe7 substitutions for potency.

Historical Development: Synthesized in 1980s from alpha-MSH for pigmentation studies, patented in 1990s.

Research Applications: Probed in MC1R signaling, melanogenesis enzyme induction (tyrosinase), and photoresponse models. Used in cell lines for cAMP elevation assays, animal skin models for eumelanin shift, and UV-irradiation experiments.

Purity: ≥99%.

Reconstitution: 2 mL bac water; 5 mg/mL.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Light-sensitive; store in amber vials.

🧬 Synara™ (PT-141 / Bremelanotide)

Category: Melanocortin receptor agonist

Chemical Structure: Cyclic 7-amino acid (Ac-Nle-cyclo[Asp-His-D-Phe-Arg-Trp-Lys]-OH) with lactam bridge for rigidity.

Historical Development: Derived from MT-II in 1990s, optimized for MC3R/MC4R selectivity in 2000s CNS research.

Research Applications: Studied in hypothalamic melanocortin pathways, behavioral modeling, and vascular CNS interactions. Employed in radioligand binding (IC50 ~1 nM), rat models for arousal signaling, and EEG-monitored experiments.

Purity: ≥98%.

Reconstitution: 1 mL saline; 10 mg/mL.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Nasal/injectable routes in models; monitor for receptor desensitization.

🧬 Grostyrex™ (IGF-1 LR3)

Category: Growth factor analog

Chemical Structure: 83-amino acid chain with Arg3 substitution and 13-residue N-terminal extension for reduced binding protein affinity.

Historical Development: Engineered in 1990s from IGF-1 for extended activity, used in cell biology since 2000s.

Research Applications: Explored in PI3K/Akt signaling, satellite cell activation, and anabolic models. Used in myoblast cultures for proliferation assays, nerve regeneration studies, and bone cell differentiation.

Purity: ≥99%.

Reconstitution: 1 mL acetic acid (0.6%); neutralize before use.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Avoid insulin co-administration in assays.

🧬 Chronovix™ (Epitalon)

Category: Pineal tetrapeptide

Chemical Structure: Ala-Glu-Asp-Gly (simple tetrapeptide, amidated C-terminus).

Historical Development: Synthesized in 1980s from pineal extracts, researched in Russia for telomere studies post-1990s.

Research Applications: Investigated in telomerase expression, epigenetic models, and oxidative damage assays. Used in fibroblast cultures for telomere length PCR, animal longevity models, and melatonin pathway interactions.

Purity: ≥99%.

Reconstitution: 0.5 mL water; 2 mg/mL.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Short half-life; frequent dosing in models.

🧬 Tesmagen™ (Tesamorelin)

Category: GHRH analog

Chemical Structure: 44-amino acid with trans-3-hexenoyl N-terminus for stability.

Historical Development: Developed in 1990s for GH research, FDA-noted in 2010s for lipodystrophy models.

Research Applications: Studied in pituitary GH release, IGF-1 feedback loops, and neuroendocrine assays. Applied in radioimmunoassays for GH pulses, fat cell cultures for lipolysis.

Purity: ≥98%.

Reconstitution: 2 mL bac water.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Daily dosing protocols.

🧬 Cerebrase™ (CJC-1295, no DAC)

Category: Short-acting GHRH analog

Chemical Structure: 29-amino acid with drug affinity complex modifications omitted for pulsatile action.

Historical Development: Variant of sermorelin in 2000s, designed for natural GH rhythm research.

Research Applications: Pulsatile secretion models, GHRH/GHRP synergy, sleep-stage GH studies. Used in ELISA for GH quantification.

Purity: ≥98%.

Reconstitution: 1 mL saline.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Pair with Ipamorelin for amplification.

🧬 Noctivex™ (CJC-1295 with DAC)

Category: Long-acting GHRH analog

Chemical Structure: 29-amino acid with DAC (maleimido propionic acid) for albumin binding.

Historical Development: DAC added in 2000s for weekly dosing research.

Research Applications: Sustained GH/IGF-1 models, recovery kinetics, hormonal steady-state assays.

Purity: ≥98%.

Reconstitution: 1 mL water.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Monitor IGF-1 levels long-term.

🧬 Curessin™ (GHK-Cu)

Category: Copper tripeptide complex

Chemical Structure: Gly-His-Lys bound to Cu2+ ion.

Historical Development: Discovered in 1970s in blood proteins, copper complex researched 1980s onward.

Research Applications: Matrix metalloproteinase regulation, fibroblast activation, inflammation models. Used in skin cell cultures for collagen assays.

Purity: ≥99%.

Reconstitution: Distilled water (copper-sensitive).

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Avoid EDTA chelators.

🧬 Lipothera™ (AOD-9604)

Category: hGH fragment (176–191)

Chemical Structure: 16-amino acid C-terminal hGH fragment.

Historical Development: Isolated in 1990s from GH lipolytic domain.

Research Applications: Beta-3 adrenergic receptor activation, lipid metabolism pathways.

Purity: ≥98%.

Reconstitution: Saline.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Non-GH receptor binding.

🧬 Gravinox™ (MOD-GRF 1-29)

Category: GHRH fragment

Chemical Structure: 29-amino acid with D-Ala2/Q8/A15 substitutions.

Historical Development: Modified sermorelin in 2000s for potency.

Research Applications: Pituitary stimulation, endogenous GH models.

Purity: ≥98%.

Reconstitution: Water.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Short-acting; time-sensitive assays.

🧬 Hexanova™ (Hexarelin)

Category: Growth hormone secretagogue (GHS)

Chemical Structure: 6-amino acid (His-D-2-Me-Trp-Ala-Trp-D-Phe-Lys-NH2).

Historical Development: Developed 1990s as ghrelin mimic.

Research Applications: GHSR agonism, cardiac protection models.

Purity: ≥98%.

Reconstitution: Saline.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Oral activity in some models.

🧬 Myogenyx™ (Follistatin-344)

Category: Myostatin inhibitor

Chemical Structure: 344-amino acid glycoprotein.

Historical Development: Cloned 1980s from follicular fluid.

Research Applications: Activin binding, muscle regulatory pathways.

Purity: ≥95%.

Reconstitution: Buffer pH 7.4.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: High molecular weight; gel filtration for purity.

🧬 Pegraflex™ (PEG-MGF)

Category: IGF splice variant

Chemical Structure: Pegylated 24-amino acid MGF isoform.

Historical Development: Pegylated in 2000s for stability.

Research Applications: Mechanical stress signaling, satellite cell models.

Purity: ≥98%.

Reconstitution: Acetic acid.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Local injection models.

🧬 Thymorix™ (Thymosin Alpha-1)

Category: Immunomodulatory peptide

Chemical Structure: 28-amino acid acetylated sequence.

Historical Development: Isolated 1970s from thymus.

Research Applications: TLR signaling, dendritic cell maturation.

Purity: ≥98%.

Reconstitution: Water.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Adjuvant in vaccine research.

🧬 Somnyrex™ (DSIP)

Category: Neuropeptide

Chemical Structure: 9-amino acid (Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu).

Historical Development: Discovered 1970s in rabbit brain.

Research Applications: Delta sleep induction, HPA axis modulation.

Purity: ≥98%.

Reconstitution: Saline.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: BBB permeability studies.

🧬 Provenyx™ (HCG)

Category: Glycoprotein hormone

Chemical Structure: Alpha (92 aa) + Beta (145 aa) subunits with glycosylation.

Historical Development: Extracted 1920s, recombinant 1990s.

Research Applications: Leydig cell stimulation, steroidogenesis pathways.

Purity: Pharmaceutical grade.

Reconstitution: Bac water.

Storage: −20 °C / 2–8 °C.

Experimental Considerations: Urine-derived vs. recombinant comparisons.