IL-2 (44-56) is a 13-residue fragment of human interleukin-2 with the sequence Ile-Leu-Asn-Gly-Ile-Asn-Asn-Tyr-Lys-Asn-Pro-Lys-Leu (ILNGINNYKNPKL).

The fragment has been used as a defined cytokine-derived model peptide in chemical modification research, including studies of site-specific peptide PEGylation.

Product Information

A Useful Model for Peptide Modification Chemistry

IL-2 (44-56) contains multiple chemically distinct side chains, including Lys, Asn and Tyr residues, within a relatively short sequence.

This structural diversity led to its use as a model peptide in solid-phase studies of N-terminal, side-chain and C-terminal PEGylation strategies.

For peptide chemists, this makes the fragment useful beyond its cytokine origin: it provides a compact sequence for evaluating site-selective modification and analytical characterization.

Relationship to Full-Length IL-2

The isolated 44-56 fragment lacks the complete tertiary structure required for normal IL-2 receptor recognition.

We recommend keeping experiments with this fragment conceptually separate from studies using recombinant full-length IL-2. A response produced by intact cytokine should not automatically be assigned to this isolated sequence.

Research Applications

Applications include peptide modification chemistry, PEGylation method development, cytokine-fragment analysis and sequence-specific binding or epitope studies.

A second IL-2-derived sequence is available as IL-2 (60-70) Peptide.

Frequently Asked Questions

How many residues are in IL-2 (44-56)?

The peptide contains 13 amino-acid residues.

Has this fragment been used in peptide modification studies?

Yes. IL-2 (44-56) has been used as a model sequence in published solid-phase PEGylation methodology.

Can site-specific PEG or other linkers be introduced?

Defined linker placement, labeling and side-chain modification can be evaluated through Chemical Peptide Synthesis.

Research Use Only.