Adiponectin Fragments

1 Identity

Biological extracts and compositionally undefined preparations — a shelf label rather than a chemical class. and AdipoRon — a non-peptide small molecule frequently shelved under the same heading and not adiponectin-derived at all.

Sequence

No defined sequence — this is a shelf label, not a chemical identity. The parent, adiponectin, is a 244-residue secreted protein with an N-terminal collagenous domain and a C-terminal C1q-like globular domain, carrying hydroxylated and glycosylated lysines and circulating as trimers, hexamers and high-molecular-weight multimers, so even the parent is not one article. Of the entities that trade under this heading, exactly one has a sequence this company can state from a primary source: ADP355, published as H-DAsn-Ile-Pro-Nva-Leu-Tyr-DSer-Phe-Ala-DSer-NH2 — a decapeptide amide containing three D-residues and one non-proteinogenic residue, norvaline. That sequence belongs to ADP355 and not to a product called Adiponectin Fragments.

Molecular formula

None, and none can be assigned. A single formula cannot be written for a name that denotes several unrelated articles spanning nearly two orders of magnitude in mass. Formulas exist only for the individually named entities and are set out in the salt and variant note below.

Average mass

Not established — confirm against a reference standard before listing, and there is no article to establish it for. Any single number printed against this name would be a fabrication, whichever of the candidate articles it happened to be taken from.

Monoisotopic mass

Not established, for the same reason. The candidate entities have monoisotopic masses and they are recorded individually in the note below; the heading does not.

Salt / variant note

Four or more unrelated articles under one heading, spanning nearly two orders of magnitude. Any honest certificate would resolve which one is in the vial, and that is precisely why none is offered. (1) ADP355, the synthetic decapeptide: H-DAsn-Ile-Pro-Nva-Leu-Tyr-DSer-Phe-Ala-DSer-NH2, C53H80N12O14, 1109.29 average / 1108.5917 monoisotopic, built from the published sequence; CAS 1793835-62-7. The formula closes against the two mass spectrometry peaks the primary paper reports: it gives [M+H]+ 1109.599 and [M+Na]+ 1131.581 against the published m/z 1109 and 1131. Three D-centers and a norvaline, so the all-L or valine-substituted counterfeits are isobaric or one methylene away and no achiral method sees them. The des-amido free acid is C53H79N11O15, 1110.28 / 1109.5757 — 0.98 Da heavier and inside any whole-dalton tolerance. (2) AdipoRon, which is not adiponectin-derived and contains no peptide bond: 2-(4-benzoylphenoxy)-N-[1-(phenylmethyl)piperidin-4-yl]acetamide, C27H28N2O3, 428.53 / 428.2100, CAS 924416-43-3 — a small molecule, 2.6 times lighter than ADP355 and roughly forty times lighter than globular adiponectin, shelved under the same heading. (3) Recombinant globular adiponectin (gAd, the C1q-like domain): a protein of roughly 16-18 kDa per monomer depending on the residue range chosen, assembling into trimers near 50 kDa. Unglycosylated from bacterial expression and glycosylated from mammalian — two different articles again, neither with a single exact mass. (4) Full-length human adiponectin: a 244-residue chain that migrates well above its calculated chain mass because of post-translational hydroxylation and glycosylation, which is where the alternative name ACRP30 comes from, and which means the apparent mass on a gel exceeds the calculated mass by design rather than by contamination. (5) ADP399 and assorted proteolytic fragments trade under the same heading with no residue range stated by anyone. The four candidates require three different release panels — P4 for the recombinant protein, P3 for the D-residue-containing synthetic peptide, P6 for the small molecule — and three mutually incompatible storage conditions.

2 Class & testing panel

Form

Single article

Testing panel

P7 — panel definition

3 Primary sources & evidence

The index reports the design and provenance of the literature, not a conclusion about effect.

Rodent and in-vitro literature exists in reasonable volume, but it attaches to specific named entities and not to an undefined fragments article. ADP355: Otvos L et al., BMC Biotechnology 2011;11:90 — synthetic peptide design, characterization and in-vitro and rodent work, and the source of the sequence and the reported mass spectrometry peaks at m/z 1109 and 1131. AdipoRon and recombinant globular adiponectin each carry their own separate in-vitro and rodent literatures. No controlled human trial was identified for any of the candidate entities. The critical point for the citation index page is that the literature cannot be assembled at all until the article is named: work on a recombinant 16 kDa protein is not evidence about a synthetic decapeptide, and presenting the two under one heading would be the specific failure this catalog is built to avoid.

4 Storage & specification

Storage

Cannot be stated, and the reason is the point. A recombinant glycoprotein wants 2-8 degrees C or -80 degrees C in single-use aliquots with no freeze-thaw; a lyophilized synthetic D-peptide wants -20 degrees C under nitrogen protected from light and moisture; a crystalline small molecule wants desiccated storage at controlled room temperature. Three incompatible conditions, one label, no way to choose. No storage condition is assigned, no vial is filled and no label is printed.

Shelf life

None. A retest interval is a property of a defined article measured under a stated condition by a stated method. There is no defined article, no condition and no method, so any number here would be fabricated.