Anti-ADAM12 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

ADAM12 also known as meltrin-alpha is a member of the ADAM (a disintegrin and metalloproteinase) family and has a mass of approximately 110 kDa. It functions primarily in the modulation of cell-cell and cell-matrix interactions due to its metalloprotease and disintegrin domains. ADAM12 protein is expressed in various tissues including muscle and placenta. Although found in many cell types it is particularly abundant during embryogenesis and development reflecting its role in these processes.

Biological function summary

The ADAM12 protein holds a role in cell signaling migration and proliferation. It is often part of complexes that interact with other extracellular matrix components influencing cell adhesion and motility. Through its protease activity ADAM12 facilitates growth factor signaling by cleaving membrane-bound precursor proteins to release active growth factors. This activity plays an important role in tissue remodeling and repair.

Pathways

The ADAM12 protein is key in the EGFR signaling pathway where it modulates the availability of epidermal growth factor (EGF) by shedding EGF-like ligands from the cell surface. This action connects ADAM12 with proteins such as ERBB receptors influencing cell division and growth. Another significant pathway is the TGF-beta signaling pathway where ADAM12's interaction with latent TGF-beta complexes can impact the bioavailability of this cytokine therefore relating to proliferation and differentiation of cells.

Associated diseases and disorders

ADAM12 is linked to cancer progression and metastasis as its activity can positively influence tumor cell invasiveness and growth. Elevated levels of ADAM12 are observed in certain cancer types including breast and prostate cancer. Additionally it associates with metabolic disorders such as obesity where ADAM12 impacts adipogenesis and insulin sensitivity. In cancer ADAM12 interacts with proteins like matrix metalloproteinases (MMPs) to remodel the tumor microenvironment promoting cancer cell invasion.