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Pioneer Labs

Fragments / Research guide

PE-22-28.

A little deeper. A clearer picture.

A seven-residue fragment investigated in ion-channel research. PE-22-28 is related to spadin and studied in the context of TREK-1, a two-pore-domain potassium channel.

For research use onlyView PE-22-28 sizes
Published by Pioneer LabsUpdated Sources & editorial standards

01 / Reference identity

Identity at a glance.

Public records describe PE-22-28 as one seven-residue peptide, GVSWGLR, ending in a free acid. The same seven residues end the longer spadin chain. The values below are for the free peptide; the salt form of a supplied lot follows its own record.

PE-22-28 reference identity
Sequence, three-letterGly–Val–Ser–Trp–Gly–Leu–Arg
Sequence, one-letterGVSWGLR
Length7 residues
C-terminusFree acid
Formula, free peptideC35H55N11O9
Molecular weight, free peptide773.9 g/mol
CAS number1801959-12-5
PubChem CID165437303
Reference values from public records, not a Pioneer lot specification.

References: [1][2][3]

02 / Molecular architecture

A closer look at the chain.

Its reference chain is Gly–Val–Ser–Trp–Gly–Leu–Arg. The reference record shows a C-terminal acid rather than an amidated ending.

Pioneer / Reference notesMolecular features
  • 7 amino acids
  • Spadin-related fragment
  • TREK-1 research
  1. Gly
  2. Val
  3. Ser
  4. Trp
  5. Gly
  6. Leu
  7. Arg
GVSWGLR–OH reference chain. Counterion is separate from the amino-acid sequence.

Reference information: [1][2][3]. Actual lot identity must be verified separately.

A seven-residue fragment identity.

The GVSWGLR sequence is the compact reference shown for PE-22-28. A fragment designation relates the molecule to a larger reference, but the fragment is its own specified material. The C-terminal acid and residue order distinguish the described chain beyond the spadin-related naming history.

Reading an ion-channel experiment.

TREK-1 is the ion-channel context in the cited reference. Electrophysiological measurements report electrical behavior under defined experimental conditions. They are a different type of evidence from a receptor-binding result or a mass spectrum, so the expression system and measured electrical endpoint belong alongside any comparison.

Structure and research references: [1]

03 / Read the evidence

Research & analytical context.

The reference describes electrophysiological measurements in cells expressing TREK-1. This is an ion-channel assay context. The named fragment, terminal chemistry and expression system are necessary details when comparing experimental records.

Read the references: [1][2][3].

The distinction that matters

PE-22-28 and full-length spadin are different reference materials. Confirm the fragment and terminal chemistry rather than treating a shared research target as proof of identical structure.

04 / From reference to record

Know the lot, too.

A publication describes its own test material. Your lot’s certificate describes what was tested on that lot. Keep the compound name, batch number and reported methods together when reviewing a result.

Identity & composition

Check sequence or chemical form, terminal modifications, counterion and—where relevant—each blend component.

Analytical results

Read purity, content, sterility and endotoxin results as separate measurements. Only call a test passed when the actual report supports it.

Handling & storage notes

Lyophilized material: Store at −20°C; protect from light and moisture.

Follow the material-specific label and supporting storage documentation. These temperatures do not establish a shelf life.

How to store lyophilized peptides

05 / Reference questions

A few details, explained.

Does PE-22-28 contain twenty-eight residues?

No. The reference shown is a seven-residue fragment. Numbers in a fragment designation should not be assumed to state the total length of the final peptide.

What does the OH at the end mean?

It denotes the C-terminal acid in the reference notation. It is not another residue and is chemically distinct from an amidated ending written NH₂.

Read alongside the references: [1]

06 / Continue reading

Go to the source.