KPV

Description

Compound Specifications

Sequence	Lys-Pro-Val
Single-letter sequence	KPV
Compound class	Synthetic tripeptide
Parent sequence	α-MSH, residues 11–13
Amino acid count	3
Molecular weight	342.4 g/mol
CAS number	67727-97-3
Form	Lyophilized powder
Quantity	10mg per vial
Purity	≥99% (HPLC verified)
Storage (lyophilized)	2–8°C, protected from light
Storage (reconstituted)	2–8°C, 30 days
Long-term storage	-20°C
Third-party testing	Freedom Diagnostics
Manufacturing	Arizona GMP facility, USA

Verify sequence, molecular weight and CAS number against batch COA prior to publication.

Research Background

KPV is a three-residue sequence — lysine, proline, valine — corresponding to positions 11 through 13 of alpha-melanocyte-stimulating hormone, a 13-residue peptide. KPV is therefore the C-terminal tripeptide of α-MSH, the tail end of the parent sequence with everything preceding it removed.

This is a different kind of fragment relationship from the others in this catalog. TB-500 is drawn from the interior of a 43-residue protein. Semax takes an interior ACTH fragment and appends a synthetic tail. KPV is a terminal fragment used unmodified — the smallest fraction of a parent sequence that research groups have worked with as a distinct entity.

At three residues KPV is at the practical lower boundary of what is conventionally called a peptide. That brevity has direct consequences. Synthesis is trivially simple by the standards of this catalog — two coupling steps rather than the forty-three required for Tesamorelin — which means by-product formation is minimal and purity is comparatively easy to achieve. Characterization is likewise straightforward: at 342.4 g/mol the molecule is small enough that mass spectrometry gives an unambiguous result.

The central proline is the structurally significant residue. Its cyclic side chain constrains the backbone into a limited set of conformations, which means this tripeptide is considerably less flexible than a three-residue chain would otherwise be. Proline in a short sequence also confers resistance to exopeptidase activity, the same principle that makes Semax’s Pro-Gly-Pro tail effective.

All statements above describe molecular characteristics and published research contexts. Noxa Labs makes no claim regarding safety, efficacy, or outcomes of any kind, in humans or animals.

Handling & Storage

Lyophilized KPV is stable at 2–8°C when sealed and shielded from light. For storage beyond several months, -20°C is preferred.

Short sequences without cysteine, methionine or tryptophan are among the more robust materials in this catalog — KPV contains none of the residues most prone to oxidation or photodegradation, and is correspondingly less demanding to handle than MOTS-C or Glutathione.

Introduce bacteriostatic water slowly down the inner wall of the vial. Swirl gently; dissolution is rapid. The solution should be clear, colourless and particulate-free.

Once in solution, store at 2–8°C and use within 30 days. A 10mg vial reconstituted with 2mL of bacteriostatic water yields a 5mg/mL concentration.

Concentration and volume calculator →

Purity & Testing

Every batch is synthesized at our GMP-compliant Arizona facility and independently analyzed by Freedom Diagnostics before release. We publish HPLC purity data and endotoxin testing results — we don’t ask you to take our word for it. Certificates of Analysis are available for any lot; contact us with your order number.

View all Certificates of Analysis →

Frequently Asked Questions

What is KPV derived from?
It corresponds to residues 11–13 of alpha-melanocyte-stimulating hormone — the C-terminal three residues of that 13-residue sequence.

Is KPV modified in any way?
No. It is the terminal fragment used unmodified, unlike Semax which appends a synthetic stabilizing tail to a natural fragment.

Why is the proline residue significant?
Proline’s cyclic side chain restricts backbone conformation and confers resistance to exopeptidase activity — meaningful in a sequence this short.

Is KPV easier to verify than longer peptides?
Yes. At three residues and 342.4 g/mol, synthesis produces minimal by-product and mass spectrometry gives an unambiguous result.

What size is available?
10mg lyophilized vials.

Related Research Compounds

• Thymosin Alpha-1 5mg — 28-residue synthetic peptide
• GHK-Cu — copper-complexed tripeptide, also three residues
• Certificates of Analysis — batch testing data

Research Use Only

For Research Use Only. This product is intended solely for laboratory research purposes. It is not a drug, food, or cosmetic and may not be misbranded, misused, or mislabeled as such. Not for human or veterinary use. Not for diagnostic or therapeutic use. Not for resale without authorization.