Anti-Elastase 3A antibody

Supplementary info

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

Activity summary

Elastase 3A well-known as pancreatic elastase or ELA3A is a serine protease enzyme with a molecular mass of approximately 26 kDa. It functions by breaking down proteins performing hydrolysis of peptide bonds especially those involving the amino acids alanine glycine and serine. This protein is mainly expressed in the pancreas although traces can be found in other tissues as well. Elastase 3A is important in processes involving the degradation of elastin a major component of the extracellular matrix.

Biological function summary

Elastase 3A plays a significant role in digestive processes within the human body. It is part of a family of elastases that contribute to the breakdown of dietary proteins into smaller peptides facilitating nutrient absorption in the small intestine. Its enzymatic activities support the maintenance of the structural integrity and turnover of extracellular matrix proteins. This process is essential for tissue remodeling and repair.

Pathways

The actions of Elastase 3A integrate into digestive enzyme pathways particularly involving protein digestion where it acts alongside other proteolytic enzymes like chymotrypsin and trypsin. These enzymes work together in a coordinated manner to ensure efficient protein degradation. Elastase 3A is also involved in extracellular matrix reorganization pathways where it relates closely to proteins such as collagen and fibronectin which are targeted for degradation and reuse.

Associated diseases and disorders

Elastase 3A has associations with conditions like pancreatitis and pulmonary emphysema. Variations or imbalances in Elastase 3A activity can contribute to these diseases as uncontrolled proteolysis may lead to tissue damage or inflammation. For instance in pancreatitis Elastase 3A activity can exacerbate tissue injury and inflammation in the pancreas. In the case of pulmonary emphysema excessive elastase activity may break down elastin in lung tissue contributing to loss of elasticity and respiratory complications.