OMD

OMD

Target · Small leucine-rich proteoglycan

OMD Osteomodulin · osteoadherin

OMD (osteomodulin, also known as osteoadherin or SLRP2C) is a secreted extracellular matrix protein of the small leucine-rich proteoglycan family. It may be implicated in biomineralisation and in the binding of osteoblasts through the alpha(V)beta(3)-integrin. Browse Assay Genie's current range of OMD research reagents below, or read on for the biology behind the target.

Extracellular matrix proteinClass II SLRPOsteoblast integrin binding
421 aa
Protein length
~49 kDa
Molecular weight
9q22.31
Gene locus
SLRP class II
Protein family
Target information

What is OMD (osteomodulin)?

OMD, or osteomodulin, is a secreted protein found in the extracellular space and extracellular matrix. UniProt annotates it as possibly implicated in biomineralisation processes, and as having a function in the binding of osteoblasts via the alpha(V)beta(3)-integrin. This links the protein to the interface between the mineralised matrix and the cells that deposit it.

The OMD gene encodes a member of the small leucine-rich proteoglycan (SLRP) family, placed in SLRP class II. HGNC classifies it in the small leucine rich repeat proteoglycans gene group. The mouse and rat both carry an orthologous Omd gene, so the protein can be studied in common rodent models. The NCBI Gene summary notes that OMD is predicted to be involved in cell adhesion and is located in extracellular exosomes.

The protein is known by the alternative names osteoadherin and SLRP2C. The name osteoadherin reflects its reported role in osteoblast adhesion, while osteomodulin is the approved HGNC name. Researchers working with the OMD protein typically focus on matrix biology, cell adhesion and mineralisation, where its extracellular localisation and integrin-binding function are most relevant.

Biomineralisation research

OMD may be implicated in biomineralisation, making it a candidate for studies of how the extracellular matrix supports mineral deposition.

Osteoblast adhesion studies

OMD has a function in osteoblast binding via the alpha(V)beta(3)-integrin, which is relevant to adhesion mechanisms in bone-forming cells.

Extracellular matrix biology

As a secreted class II small leucine-rich proteoglycan, OMD is used to explore proteoglycan organisation in the extracellular matrix.

Cell adhesion and exosomes

OMD is predicted to take part in cell adhesion and is located in extracellular exosomes, pointing to roles in extracellular signalling and adhesion.

Background

OMD frequently asked questions

What does OMD do?

OMD may be implicated in biomineralisation processes. UniProt also reports a function in the binding of osteoblasts via the alpha(V)beta(3)-integrin. NCBI Gene predicts involvement in cell adhesion. The protein is secreted into the extracellular space and extracellular matrix.

What other names does OMD have?

OMD stands for osteomodulin. Its aliases are osteoadherin and SLRP2C. The osteoadherin name reflects the reported osteoblast-binding function, and SLRP2C reflects its place among the small leucine-rich proteoglycans. HGNC lists no previous names.

Is OMD conserved in mouse and rat?

Yes. Both mouse and rat have an orthologous gene named Omd, so OMD can be studied in rodent models. OMD belongs to the SLRP family, class II subfamily. Check the datasheet of any product for its validated reactivity.

Explore

Related targets

Other small leucine-rich proteoglycans, integrins and extracellular matrix proteins relevant to bone and adhesion research.

Gene and protein annotations from HGNC, NCBI Gene and UniProt Q99983; product specifications from Assay Genie datasheets.

OMD Product listing