HMG 75IU is a urinary-derived glycoprotein preparation (CAS 9002-68-0) containing two heterodimeric glycoprotein components that share a common α-subunit. Standardized to 75 IU per vial. Supplied as lyophilized powder, third-party tested by Janoshik Analytical. Research compound — not for human use.
Compound Specifications
HMG (CAS 9002-68-0) is a preparation of urinary-derived glycoproteins consisting of two heterodimeric components. Both components share a common 92-amino-acid α-subunit (~14.5 kDa protein core) and differ by their unique β-subunits of 111 and 121 amino acids, respectively. The α-subunit contains two N-linked glycosylation sites (Asn-52, Asn-78), contributing to the characteristic heterogeneity observed in electrophoretic and chromatographic analyses. Research compound — not for human use.
Product Details
- Compound: HMG (Urinary Glycoprotein Preparation)
- CAS: 9002-68-0
- Components: Two heterodimeric glycoproteins with shared α-subunit
- α-Subunit: 92 amino acids, ~14.5 kDa (protein core), two N-glycosylation sites
- β-Subunits: 111 aa (~15.5 kDa) and 121 aa (~16.7 kDa), each with 1–2 N-glycosylation sites
- Native MW: ~30–38 kDa per heterodimer (glycosylation-dependent)
- Potency: 75 IU (standardized bioassay)
- Form: Lyophilized powder (white to off-white)
- Solubility: Soluble in aqueous buffers
- Testing: Third-party verified by Janoshik Analytical → View COA
- Storage: 2–8°C desiccated, protect from light.
- Testing: View COA (Verified by Janoshik Analytical) →
Research Studies
Structural Characterization
HMG preparations consist of non-covalently associated α/β heterodimers. The α-subunit is encoded by a single gene (chromosome 6q21.1-23) and is structurally conserved across both glycoprotein components. It features a cystine knot motif formed by three intramolecular disulfide bonds, a structural element common to the cystine knot growth factor superfamily. The distinct β-subunits each contribute additional disulfide bonds (six in the 111-aa subunit, six in the 121-aa subunit), yielding the characteristic tightly folded tertiary structure.
Physicochemical Properties
The isoelectric point of HMG glycoprotein components ranges from pH 3.5–5.5, reflecting extensive sialylation of the N-linked oligosaccharide chains. Charge heterogeneity arises primarily from variable terminal sialic acid residues. The preparations can be resolved by isoelectric focusing into multiple glycoforms, a property used in quality control characterization. The lyophilized form demonstrates excellent long-term stability when stored desiccated at 2–8°C.