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C-Terminal Proghrelin Isoform Peptide, mouse is an 11-residue sequence encoded by an alternatively spliced mouse proghrelin transcript. Its sequence, Arg-Arg-Gln-Leu-Thr-Ser-Asn-His-Gly-Gln-Ala (RRQLTSNHGQA), arises from a proghrelin variant in which exon 4 is deleted.
This peptide provides a defined tool for investigating ghrelin-gene alternative splicing, precursor organization and the molecular diversity of proghrelin-derived products.
Product Information
| Property | Specification |
|---|---|
| Product Name | C-Terminal Proghrelin Isoform Peptide, Mouse |
| Catalog No. | AS2636 |
| Sequence | Arg-Arg-Gln-Leu-Thr-Ser-Asn-His-Gly-Gln-Ala |
| One-Letter Sequence | RRQLTSNHGQA |
| Peptide Length | 11 amino-acid residues |
| Molecular Formula | C50H86N22O17 |
| Molecular Weight | Approximately 1267.38 Da |
| N-Terminus | Free amino terminus |
| C-Terminus | Free carboxyl terminus |
| Biological Context | Exon-4-deleted mouse proghrelin splice variant |
| Research Areas | Alternative splicing, prohormone processing, ghrelin precursor biology |
Generated by Alternative Splicing of Mouse Proghrelin
A mouse ghrelin transcript lacking exon 4 was identified in tissue-expression studies. Removal of this exon changes the translated C-terminal region of the precursor while retaining the sequence encoding mature ghrelin.
The resulting alternative domain contains the unique sequence RRQLTSNHGQA.
This makes the peptide fundamentally different from native 28-residue ghrelin: it is associated with an alternative precursor isoform rather than representing an acylated GHSR1a agonist.
The N-Terminal RR Motif
The sequence begins with two consecutive arginine residues. The original characterization noted that this dibasic motif could provide a potential site for proteolytic processing.
However, the exact endogenous processing products and physiological role of this region have not been established to the same degree as mature ghrelin. We recommend distinguishing experimentally demonstrated precursor expression from proposed downstream peptide processing.
Tissue Expression and Precursor Biology
The exon-4-deleted proghrelin transcript was detected in multiple mouse tissues, and immunochemical studies using antibodies directed against its unique C-terminal region supported expression in tissues including stomach, kidney and reproductive organs.
The peptide can therefore support studies focused on ghrelin-gene splice variants, tissue-specific precursor expression and sequence-specific antibody or analytical method development.
Distinct from Ghrelin and Obestatin
| Peptide | Sequence Context | Key Feature |
|---|---|---|
| Ghrelin | 28-residue N-terminal proghrelin product | Ser3 octanoylation; GHSR1a agonist |
| Obestatin | C-terminal proghrelin-derived sequence | Distinct 23-residue amidated sequence historically proposed |
| RRQLTSNHGQA | Exon-4-deleted mouse proghrelin isoform | Unique alternative-splicing-derived C-terminal sequence |
These molecular forms should not be used as interchangeable names in precursor-processing experiments.
Research Applications
Applications include alternative-splicing studies, proghrelin precursor mapping, peptide-antibody specificity experiments, targeted mass-spectrometry method development and investigation of ghrelin-gene-derived molecular diversity.
Researchers studying mature receptor-active ghrelin can also review Rat Ghrelin.
Frequently Asked Questions
Is RRQLTSNHGQA mature mouse ghrelin?
No. Mature mouse/rat ghrelin is a 28-residue Ser3-octanoylated peptide. RRQLTSNHGQA is a unique C-terminal sequence encoded by an alternatively spliced proghrelin variant.
Is this peptide the same as obestatin?
No. It is a distinct sequence produced by a different proghrelin transcript context.
Is RRQLTSNHGQA an established GHSR1a agonist?
Its established identity is as an alternative-splicing-derived proghrelin sequence. A canonical GHSR1a agonist role comparable with acyl ghrelin should not be assumed.