Alpha-2-macroglobulin-like protein 1; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and [...]

Calpain-14; Calcium-regulated non-lysosomal thiol-protease.

Alpha-2-macroglobulin-like protein 1; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and [...]

Kallikrein-6; Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neu [...]

Alpha-2-macroglobulin-like protein 1; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and [...]

Kallikrein-7; May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines.

Alpha-2-macroglobulin-like protein 1; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and [...]

Keratinocyte differentiation-associated protein; May act as a soluble regulator of keratinocyte differentiation. May play an important role in embryonic skin morphogenesis.

Alpha-2-macroglobulin-like protein 1; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and [...]

Serine protease inhibitor Kazal-type 5; Serine protease inhibitor, probably important for the anti- inflammatory and/or antimicrobial protection of mucous epithelia. Contribute to the integrity and protective barrier function of the skin by regulating the activity of defense-activating and desquamation- involved proteases. Inhibits KLK5, it's major target, in a pH-dependent manner. Inhibits KLK7, KLK14 CASP14, and trypsin.

Alpha-2-macroglobulin-like protein 1; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and [...]

Serine protease inhibitor Kazal-type 7; Probable serine protease inhibitor.

Alpha-2-macroglobulin-like protein 1; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and [...]

Transmembrane protease serine 11B; Serine protease.

Uncharacterized protein C1orf43; Chromosome 1 open reading frame 43.

Cysteine rich C-terminal 1.

Calpain-14; Calcium-regulated non-lysosomal thiol-protease.

Alpha-2-macroglobulin-like protein 1; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and [...]

Calpain-14; Calcium-regulated non-lysosomal thiol-protease.

Cornulin; Promotes cell proliferation, G1/S cell cycle progression and induces expression of the cell cycle regulator CCND1. Regulates proliferation induced by proinflammatory cytokine response via activation of NFKB1 and PI3K/AKT signaling pathways ; Belongs to the S100-fused protein family.

Calpain-14; Calcium-regulated non-lysosomal thiol-protease.

Serine protease inhibitor Kazal-type 5; Serine protease inhibitor, probably important for the anti- inflammatory and/or antimicrobial protection of mucous epithelia. Contribute to the integrity and protective barrier function of the skin by regulating the activity of defense-activating and desquamation- involved proteases. Inhibits KLK5, it's major target, in a pH-dependent manner. Inhibits KLK7, KLK14 CASP14, and trypsin.

Calpain-14; Calcium-regulated non-lysosomal thiol-protease.

Serine protease inhibitor Kazal-type 7; Probable serine protease inhibitor.

Calpain-14; Calcium-regulated non-lysosomal thiol-protease.

Transmembrane protease serine 11B; Serine protease.

Cornifelin; Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia; Belongs to the cornifelin family.

Cysteine rich C-terminal 1.

Cornifelin; Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia; Belongs to the cornifelin family.

Cornulin; Promotes cell proliferation, G1/S cell cycle progression and induces expression of the cell cycle regulator CCND1. Regulates proliferation induced by proinflammatory cytokine response via activation of NFKB1 and PI3K/AKT signaling pathways ; Belongs to the S100-fused protein family.

Cornifelin; Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia; Belongs to the cornifelin family.

Cysteine rich tail 1.

Cornifelin; Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia; Belongs to the cornifelin family.

Dermokine; May act as a soluble regulator of keratinocyte differentiation.

Cornifelin; Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia; Belongs to the cornifelin family.

Kallikrein-13; Kallikrein related peptidase 13.

Cornifelin; Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia; Belongs to the cornifelin family.

Keratin, type II cytoskeletal 78; Keratin 78; Belongs to the intermediate filament family.

Cornifelin; Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia; Belongs to the cornifelin family.

Keratinocyte differentiation-associated protein; May act as a soluble regulator of keratinocyte differentiation. May play an important role in embryonic skin morphogenesis.