The acronym "OCM" appears in multiple contexts across scientific disciplines, but none align with a compound named "OCM Human":
Outline of Cultural Materials (OCM): A classification system for ethnographic research ([Source 6] ).
Organic Carbon Matter: A general term in environmental science, unrelated to human-specific compounds.
Oxidative Coupling of Methane: A chemical process in industrial catalysis, irrelevant to human biology.
No peer-reviewed publications, clinical trials, or regulatory documents reference "OCM Human" as a discrete compound.
While "OCM Human" remains unidentified, human biology involves critical organic and inorganic compounds. Key findings from reviewed sources include:
| Element | Symbol | % Body Mass | Role | Sources | 
|---|---|---|---|---|
| Iron | Fe | 0.006% | Oxygen transport (hemoglobin) | |
| Zinc | Zn | 0.0032% | Enzyme cofactor | |
| Copper | Cu | 0.0001% | Electron transport | 
If "OCM Human" refers to an uncharacterized compound, methodologies for its identification might include:
Radiolabelled Studies: Tracking absorption, metabolism, and excretion (AME) using isotopes like ¹⁴C ([Source 7] ).
Metabolite Profiling: High-resolution mass spectrometry (HRMS) to identify unknown compounds ([Source 12] ).
Genomic Databases: Cross-referencing with human pangenome data to detect novel biomolecules ([Source 8] ).
Verify Terminology: Confirm whether "OCM Human" is a proprietary term, typographical error, or emerging research concept.
Explore Databases:
Consult Interdisciplinary Sources: Cross-reference anthropology (OCM taxonomy) and biochemistry for potential overlaps.
MKHHHHHHAS ITDVLSADDI S ITDVLSADDI AAALQECRDP DTFEPQKFFQ TSGLSKMSAN QVKDVFRFID NDQSGYLDEE ELKFFLQKFE SGARELTESE TKSLMAAADN DGDGKIGAEE FQEMVHS.
The recombinant human Oncomodulin-1 is produced in E. coli and has a molecular mass of approximately 13.21 kDa. It consists of 117 amino acid residues and is fused to a 9 amino acid His tag at the N-terminus . Oncomodulin-1 contains two EF-hand domains, which are helix-loop-helix structural domains capable of binding calcium ions with high affinity .
Oncomodulin-1 serves several important biological functions:
Recombinant human Oncomodulin-1 is used in various research applications, including: