HCG

For Laboratory Research Use Only — Not for Human or Veterinary Use.

Standard (< 1,000 vials)$210/kit

Volume (1,000+ vials)$140/kit

Quantity (kits)

= 10 vials

Minimum order: 100 vials total. Mix and match across all products.

I confirm this order is for laboratory research use only.For Laboratory Research Use Only — Not for Human or Veterinary Use. By checking this box you affirm this product will not be used for human or animal administration.

Specifications

CAS Number	—
Molecular Formula	—
Molecular Weight	—
Purity	≥98% (HPLC)
Form	Lyophilized Powder
Storage	-20°C, desiccated, protected from light
Reconstitution	Bacteriostatic water

Certificate of Analysis

Lot documentation

Every production lot is independently third-party tested. A batch-specific Certificate of Analysis — documenting HPLC purity, mass spectrometry identity confirmation, and net peptide content — is issued with every shipment. View a sample COA to see the format.

View Sample COA About our testing →

Research context

A heterodimeric glycoprotein of roughly 237 residues across two non-covalently associated chains. It is quantified in units of activity because its mass does not determine what it does.

Structure and chemical class

Chorionic gonadotropin is not a peptide in the sense that the rest of this catalogue uses the word. It is a glycoprotein hormone built from two different polypeptide chains that associate without any covalent bond between them, and each chain carries extensive attached carbohydrate. The scale alone puts it in a different class: a molecule of this size is produced biologically, not by solid-phase synthesis.

The alpha chain is shared with luteinising hormone, follicle-stimulating hormone and thyroid-stimulating hormone. Specificity comes entirely from the beta chain, which in this hormone carries a distinctive C-terminal extension bearing O-linked carbohydrate that its closest relative, luteinising hormone, does not have. That extension is the structural feature that separates the two.

Its receptor is shared with luteinising hormone and is a Gs-coupled receptor signalling through adenylate cyclase and cyclic AMP to steroidogenic pathways. Because the two hormones engage the same receptor, distinguishing their actions in an experimental system requires attention to the differing kinetics rather than to receptor selectivity, of which there is essentially none.

Findings in the published research literature

Gonadal cell models, principally Leydig and granulosa cell preparations, provide the standard in vitro system, with cyclic AMP generation and steroid output as the measured endpoints and receptor binding assays supplying affinity data. Rodent models cover the same receptor axis in vivo.

The most consequential finding running through this literature concerns glycosylation rather than sequence. The carbohydrate attached to both chains varies between preparations, and that variation alters circulating persistence and receptor activation measurably. Two preparations with identical protein sequence and identical mass can differ in measured activity, which is why this material is characterised by biological potency and not by mass.

Analytical verification

A peptide-style Certificate of Analysis quoting a single HPLC purity percentage does not describe this material adequately, and treating it as though it did is the most common error made with glycoprotein preparations. The meaningful specification is potency in international units, established by an immunoassay or bioassay calibrated against a recognised reference preparation.

Structural verification uses the methods appropriate to a protein: electrophoresis under reducing and non-reducing conditions to establish that both chains are present and intact, size exclusion chromatography to detect aggregation and to confirm that the dimer has not dissociated, and mass spectrometric glycan profiling where glycoform composition is relevant to the work.

Dimer dissociation deserves particular attention because the two chains are held together only by non-covalent interaction. Separated subunits retain their sequences and their mass while losing receptor engagement, so an analysis measuring only protein content can pass material that has come apart.

Handling and storage

Solubility	Dissolves in aqueous buffer. Preparations are typically lyophilised with a bulking excipient, which contributes most of the visible solid in the vial.
Reconstitution	Add diluent down the vial wall and swirl gently. Do not shake or vortex: shear and foaming at the air-liquid interface denature glycoproteins far more readily than they affect short synthetic peptides.
Storage	Lyophilised solid at -20C, desiccated and protected from light. Reconstituted material at 2-8C.
Stability	Far less robust than a synthetic peptide. The non-covalent dimer dissociates with heat, extremes of pH and mechanical stress, and reconstituted solutions have a short usable life. Avoid freeze-thaw cycling entirely.