DSIP Specs: Sequence, MW & CAS
Part of the full DSIP guide - a endogenous amphiphilic neuropeptide reference compound, identity-verified with a COA on every vial.
In brief
This spoke decodes DSIP's physical identifiers, the sequence, molecular weight, molecular formula, and CAS number, and explains what each means for structure-function interpretation at the bench. Every value is drawn directly from the provided entry.
To the molecule
Molecular specifications
Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-GluThe detail
A closer look
01
Sequence and the nonapeptide backbone
DSIP's primary structure is Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu, a chain of nine amino acids that classifies it as a nonapeptide. Reading the sequence reveals its functional chemistry: the N-terminal tryptophan (Trp) carries an aromatic indole side chain responsible for the peptide's characteristic UV absorbance used in laboratory identification. The two glycine pairs (Gly-Gly and a later Gly) confer backbone flexibility, while aspartate (Asp) and glutamate (Glu) contribute acidic, hydrophilic character and serine (Ser) adds a hydroxyl-bearing residue. The interleaving of hydrophilic and hydrophobic residues is precisely what gives the molecule its reported amphiphilic character.
02
Molecular weight and formula
The molecular weight is 848.81 g/mol and the molecular formula is C35H48N10O15. The weight is the conversion constant between mass and moles, the value a researcher divides into a mass concentration to obtain molarity for any in-vitro working solution. The formula's ten nitrogen atoms reflect the peptide bonds and side-chain amides of the nine-residue chain, while the fifteen oxygens are consistent with the multiple carboxylate and hydroxyl groups contributed by Asp, Glu, and Ser. Together these identifiers let a lab confirm material identity by mass spectrometry and elemental composition.
03
CAS number and structure-function notes
The CAS registry number 62568-57-4 is the unambiguous chemical identifier for DSIP, used to source, track, and verify reference material across suppliers and databases. On structure-function: the entry frames DSIP as a modulator rather than a single-receptor ligand, and its specs support that framing. The amphiphilic residue distribution, the GILZ-protein sequence homology noted in the mechanistic record, and the flexible glycine-rich backbone are all consistent with a small peptide that interacts across multiple signaling contexts rather than docking into one defined binding pocket. The tryptophan's UV signature additionally ties the molecule's identity directly to a routine analytical handle.
The fine print: products are sold for laboratory research use only and are not for human or animal consumption. Bodily introduction into humans or animals is strictly prohibited by law. DSIP is not a drug and is not intended to diagnose, treat, cure, or prevent any disease. These statements have not been evaluated by the FDA.