MOTS-C 20mg — Vial Spec, Reconstitution Math & COA

MOTS-C 20mg Vial Specification and Laboratory Applications

A 20mg vial of MOTS-C contains a high-yield lyophilized cake of mitochondrial-derived peptide formulated specifically for demanding laboratory applications, including high-throughput in vitro cell assays and multi-week preclinical rodent studies. Laboratory procurement specialists and principal investigators select this elevated 20mg mass unit to preserve single-lot batch uniformity across extensive assay plates or longitudinal animal cohorts, thereby minimizing intra-study variance.

While custom high-mass vials like 20mg are produced for high-volume research institutions, researchers evaluating standard inventory can review all active catalog items at the PX1 Research catalog or inspect the primary MOTS-C product page to examine available stock sizes such as 5mg and 10mg vials. Regardless of the physical fill mass, every batch supplied by PX1 Research undergoes uniform analytical testing, including high-performance liquid chromatography and mass spectrometry verification.

Molecular Identification and Chemical Properties

MOTS-c (Mitochondrial Open Reading Frame of the 12S rRNA Type-c) is a 16-amino-acid peptide encoded within the mitochondrial genome. Its primary sequence—Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg—yields a theoretical molecular weight of approximately 2174.6 Da. As a member of the mitochondrial-derived peptide (MDP) family, MOTS-c plays a central role in nuclear-mitochondrial communication.

In a sterile, lyophilized format, MOTS-c appears as a compact white to off-white cake sealed under inert argon gas to prevent premature oxidation of sulfur-containing methionine residues. Maintaining pristine chemical purity is essential for preclinical researchers studying retrograde signaling, metabolic adaptation, and cellular bioenergetics in culture models.

Reconstitution Mathematics for a 20mg Mass

Accurate stock concentration calculations are critical when reconstituting a 20mg lyophilized peptide vial for quantitative bioassays. Adding specific solvent volumes yields exact mass-to-volume concentrations required for micro-pipetting into cell culture media or microfluidic chips. To confirm volumetric calculations, researchers frequently consult our inline reconstitution calculator prior to solvent introduction.

When 1.0 mL of sterile bacteriostatic water or laboratory-grade phosphate-buffered saline (PBS) is added to a 20mg vial, the resulting stock concentration is 20.0 mg/mL (20.0 µg/µL). Introducing 2.0 mL of diluent yields a working concentration of 10.0 mg/mL (10.0 µg/µL), whereas a 3.0 mL addition results in a concentration of approximately 6.67 mg/mL (6.67 µg/µL).

For example, if an in vitro bioassay protocol specifies a target dose of 50 µg per microplate well, using a 10.0 mg/mL stock solution (prepared with 2.0 mL diluent) requires pipetting exactly 5.0 µL into each well. Establishing consistent volumetric stock protocols reduces pipetting margin-of-error across multi-well assays.

Aliquot Planning and Workflow Management

Handling larger peptide masses like 20mg requires deliberate aliquot planning to avoid freeze-thaw degradation. Repeated freeze-thaw cycles subject the peptide backbone to thermal and physical shear stress, which can lead to aggregation or peptide bond hydrolysis over time.

Immediately following full reconstitution, the stock solution should be subdivided into single-use, low-binding micro-centrifuge tubes based on daily projected experimental consumption. For instance, a 20mg vial reconstituted in 2.0 mL (10 mg/mL) can be divided into twenty 100 µL aliquots, each containing 1.0 mg of MOTS-C. These aliquots should be flash-frozen and maintained at -20°C or -80°C until immediate use in an assay.

Selecting the Optimal Fill Size: 5mg, 10mg, or 20mg Formulations

Determining whether to order 5mg, 10mg, or 20mg unit sizes depends primarily on protocol duration, storage infrastructure, and solvent stability limits. Smaller 5mg vials are generally preferred for short-term exploratory studies or low-volume cell culture assays where reconstituted liquid will be completely consumed within 7 to 14 days.

Conversely, larger 20mg or 10mg sizes are optimal for high-throughput screening platforms and longitudinal rodent models requiring identical lot characteristics over several weeks. High-volume academic laboratories and contract research organizations (CROs) frequently establish institutional accounts through our wholesale research portal to secure single-lot production runs tailored to large experimental matrices.

Comparative Analysis: Mitochondrial and Metabolic Research Compounds

In bioenergetic and metabolic research, MOTS-c belongs to a distinct class of mitochondrial regulators. When structuring comparative preclinical studies, investigators often compare MOTS-c to SS-31, a inner-mitochondrial-membrane targeting tetrapeptide evaluated for cardiolipin preservation and ROS attenuation, as well as Humanin, another mitochondrial-derived peptide investigated for cytoprotection and stress-response pathways. Furthermore, non-peptide small molecules such as 5-Amino-1MQ are frequently studied alongside MOTS-c in metabolic regulation models due to their role in NNMT inhibition and energy homeostasis.

While SS-31 interacts directly with lipid membranes to optimize electron transport chain efficiency, MOTS-c functions predominantly via translocation to the nucleus under metabolic stress to regulate genomic expression. Profiling these distinct mechanisms in rodent models allows researchers to isolate specific pathways governing exercise capacity, cellular respiration, and substrate oxidation.

Preclinical Literature Summary: Metabolic Function and Physical Performance

Preclinical evidence indicates that MOTS-c acts as a key metabolic signal that coordinates cellular energy balance. In vitro data show that under conditions of glucose deprivation or metabolic stress, MOTS-c translocates from the mitochondrion to the nucleus, where it binds to antioxidant response elements (ARE) and interacts with transcription factors such as Nrf2 to upregulate adaptive gene expression.

In rodent models, animal study data demonstrate that exogenous MOTS-c administration correlates with enhanced exercise capacity, superior metabolic flexibility, and improved skeletal muscle insulin sensitivity. Investigators studying metabolic homeostasis frequently utilize MOTS-c to explore AMPK activation pathways without inducing non-specific cellular toxicity.

Analytical Quality Verification: HPLC, MS, and Endotoxin Standards

Rigorous quality verification is imperative when utilizing synthetic peptides in cell culture or animal research. PX1 Research mandates that every batch of MOTS-c—regardless of fill volume—is manufactured in USA-based, GMP-compliant facilities and thoroughly tested by independent ISO 17025 accredited analytical laboratories.

Every shipment provides transparent access to a lot-matched certificate of analysis accessible via our COA lookup page. Quality testing includes High-Performance Liquid Chromatography (HPLC) to confirm peptide purity exceeds 98.0%, Mass Spectrometry (MS) to confirm sequence molecular weight, and chromogenic Limulus Amebocyte Lysate (LAL) testing to ensure endotoxin levels remain strictly under <0.01 EU/mg for safe cell culture application.

Storage Parameters, Solvent Selection, and Handling

Unreconstituted, lyophilized MOTS-C 20mg powder should be stored long-term at -20°C or -80°C in a desiccated environment protected from light exposure. Under these conditions, the dry peptide cake remains stable for up to 24 months. Prior to reconstitution, the vial must be equilibrated to room temperature inside a laminar flow hood to prevent atmospheric moisture condensation on the cake.

Reconstitution should be performed using sterile, laboratory-grade solvents such as 0.9% sterile saline or bacteriostatic water. Once dissolved, liquid stock solutions stored at 2°C to 8°C should be utilized within 7 to 14 days. For extended storage, aliquots must be maintained at -80°C. Further analytical resources and handling protocols are published in the PX1 research library hub.