Anti-P4HA2 antibody

Supplementary info

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

Activity summary

P4HA2 also known as Prolyl 4-hydroxylase subunit alpha-2 is an enzyme with an approximate mass of 60 kDa. It plays a role in catalyzing the hydroxylation of proline residues in collagen strands which is essential for the proper formation of the collagen triple helix structure. P4HA2 can be found most abundantly in tissues that require strong extracellular matrices such as skin tendons and cartilage. Its expression in these tissues suggests a critical role in maintaining structural integrity.

Biological function summary

Prolyl 4-hydroxylase functions within a larger enzyme complex by working alongside other subunits to ensure efficient collagen biosynthesis. This complex modifies proline residues on collagen peptides ensuring structural stability and mechanical strength of the extracellular matrix. By contributing to collagen stability P4HA2 supports cellular functions related to tissue maintenance and repair. Its activity is important in physiological environments where collagen is abundant emphasizing its role in vertebrate development and organism physiology.

Pathways

Collagen biosynthesis and modification serve as significant pathways involving P4HA2. This enzyme contributes to pathways related to the post-translational modification of collagen which is essential for extracellular matrix organization and cellular function. P4HA2 interacts with proteins such as collagen type I and type III playing an important role in the maturation of collagen fibers and influencing tissue resilience and elasticity. Such interactions highlight its involvement in fundamental biological processes that sustain organismal structure and function.

Associated diseases and disorders

P4HA2 has associations with fibrosis and certain cancers. During fibrotic progression dysregulation of collagen production often involves elevated P4HA2 levels driving excessive extracellular matrix deposition and tissue stiffening. This condition can connect P4HA2 to fibrosis-related proteins such as TGF-beta which regulate extracellular matrix production. In cancer P4HA2 may contribute to tumor microenvironment changes influencing tumor growth and metastasis through interactions with proteins like MMPs (matrix metalloproteinases). Understanding these connections not only helps in identifying potential therapeutic targets but also in elucidating the pathophysiology of collagen-related diseases.