Mast Cell Tryptase Recombinant Rabbit Monoclonal Antibody

Function

Mast cells are connective tissue cells derived from blood-forming tissues that line arterial walls and secrete substances, which mediate inflammatory and immune responses. Mast cell chymase, known as CMA1, is a major secreted serine protease that is involved in vasoactive peptide generation, extracellular matrix degradation and regulation of gland secretion. The human chymase gene, which maps to human chromosome 14q11.2, encodes a preproenzyme with a 19-amino acid signal peptide, an acidic 2-amino acid propeptide and a 226-amino acid catalytic domain. Tryptases comprise a family of trypsin-like serine proteases that are enzymatically active as heparin-stabilized tetramers. There are four functional genes for tryptase: α I, β I, β II and γ I, which map to human chromosome 16p13.3, with β tryptases representing the main isoenzymes expressed in mast cells. Mast cell proteases are a family of rodent protein homologs to human tryptases that are specifically expressed in mast cells and may serve as highly specific markers in the analysis of mast cell heterogeneity, differentiation and function.

Background References

1. De Martin S et al. Expression and distribution of the adrenomedullin system in newborn human thymus. PLoS One 9:e97592 (2014).

2. Edmunds MC et al. Paradoxical effects of heme arginate on survival of myocutaneous flaps. Am J Physiol Regul Integr Comp Physiol 306:R10-22 (2014).

Sequence Similarity

Belongs to the peptidase S1 family. Tryptase subfamily.

Tissue Specificity

Isoform 1 and isoform 2 are expressed in lung, stomach, spleen, heart and skin; in these tissues, isoform 1 is predominant. Isoform 2 is expressed in aorta, spleen, and breast tumor, with highest levels in the endothelial cells of some blood vessels surrounding the aorta, as well as those surrounding the tumor and low levels, if any, in mast cells (at protein level).

Subcellular Location

Secreted.

UNIPROT

SwissProt: Q15661 Human

Synonyms