$241.00 - $241.00
Interleukin-1β Convertase Substrate is a 14-residue peptide derived from the precursor form of human IL-1β. Its sequence, Asn-Glu-Ala-Tyr-Val-His-Asp-Ala-Pro-Val-Arg-Ser-Leu-Asn (NEAYVHDAPVRSLN), contains the physiological caspase-1 cleavage region used during maturation of pro-IL-1β.
Unlike short reporter substrates such as YVAD-AMC, this peptide retains native sequence on both sides of the cleavage bond and provides a useful model for studying caspase-1 recognition of its cytokine substrate.
Product Information
| Property | Specification |
|---|---|
| Product Name | Interleukin-1β Convertase Substrate |
| CAS No. | 143305-11-7 |
| Sequence | Asn-Glu-Ala-Tyr-Val-His-Asp-Ala-Pro-Val-Arg-Ser-Leu-Asn |
| One-Letter Sequence | NEAYVHDAPVRSLN |
| Peptide Length | 14 amino-acid residues |
| Molecular Formula | C68H105N21O23 |
| Molecular Weight | Approximately 1584.7 Da |
| Primary Research Enzyme | Caspase-1 / ICE |
| Protein Context | Pro-IL-1β residues surrounding the maturation cleavage site |
Native Pro-IL-1β Cleavage Site
Caspase-1, historically called interleukin-1β-converting enzyme (ICE), processes pro-IL-1β by cleavage after Asp116.
Within this substrate, the relevant sequence can be represented as:
NEAYVHD↓APVRSLN
The Asp–Ala bond therefore provides a native-sequence model of cytokine precursor processing.
Native-Sequence Substrate Versus Reporter Peptides
Short fluorogenic substrates are convenient for continuous enzyme assays because cleavage directly releases a reporter group. NEAYVHDAPVRSLN serves a different purpose: it preserves natural amino-acid context on both sides of the scissile bond.
Cleavage products can be resolved by chromatography or mass spectrometry, making the peptide useful for substrate-recognition and proteolytic-processing studies.
We recommend choosing between a native-sequence substrate and a reporter conjugate according to whether the experiment prioritizes physiological sequence context or assay throughput.
Research Applications
This peptide can support caspase-1 enzymology, pro-IL-1β processing studies, cleavage-site validation and comparison with shorter YVAD-based substrates.
Related enzyme substrates are available in our Caspase Substrates & Inhibitors collection.
Frequently Asked Questions
Where does caspase-1 cleave this sequence?
The physiological cleavage occurs after Asp116 of pro-IL-1β, corresponding to the Asp–Ala bond within NEAYVHDAPVRSLN.
Is this peptide fluorogenic?
No. It is an unlabeled native-sequence substrate and does not release an intrinsic fluorescent reporter after cleavage.
Can labeled versions be prepared?
Fluorophore, quencher or affinity-tagged versions can be evaluated through Chemical Peptide Synthesis.