C-type lectin domain-containing protein.

Peptidase S1 domain-containing protein; Belongs to the peptidase S1 family.

C-type lectin domain-containing protein.

Similar to Anionic trypsin II precursor (Pretrypsinogen II); Belongs to the peptidase S1 family.

C-type lectin domain-containing protein.

Anionic trypsin-1; Belongs to the peptidase S1 family.

C-type lectin domain-containing protein.

Anionic trypsin-2; Belongs to the peptidase S1 family.

C-type lectin domain-containing protein.

Regenerating islet-derived protein 3-alpha 16.5 kDa form; Bactericidal C-type lectin. Regulates keratinocyte proliferation and differentiation after skin injury via activation of EXTL3-PI3K-AKT signaling pathway (By similarity).

C-type lectin domain-containing protein.

Regenerating islet-derived protein 3-beta 16.5 kDa form; Bactericidal C-type lectin which acts against several intestinal Gram-positive bacteria and Gram-negative bacteria. Lacks antibacterial activity against S.typhimurium. May play a role in protection against infection with S.enteritidis by inhibiting its translocation from the gut lumen into intestinal tissues and further extraintestinal tissues (By similarity).

C-type lectin domain-containing protein.

Regenerating islet-derived protein 3-gamma 16.5 kDa form; Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Restricts bacterial colonization of the intestinal epithelial surface and consequently limits activation of adaptive immune responses by the microbiota. The uncleaved form has bacteriostatic activity, whereas the cleaved form has bactericidal activity against L.monocytogenes and methicillin-resistant S.aureus. Regulates keratinocyte proliferation and [...]

C-type lectin domain-containing protein.

Trypsin 10; Belongs to the peptidase S1 family.

C-type lectin domain-containing protein.

Serine protease 3; Belongs to the peptidase S1 family.

C-type lectin domain-containing protein.

Trypsin 5; Belongs to the peptidase S1 family.

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.

Cathepsin G.

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.

Elastase 2, neutrophil (Predicted); Belongs to the peptidase S1 family.

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.

Lipopolysaccharide-binding protein; Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. Acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the release of cytokines in response to bacterial lipopolysaccharide; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.

Lactotransferrin (Predicted); Belongs to the transferrin family.

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.

Myeloperoxidase.

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.

Peptidoglycan recognition protein 1; Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria. Involved in innate immunity. Is microbicidal for Gram-positive and Gram-negative bacteria and yeast. May function in intracellular killing of bacteria (By similarity); Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.

Proteinase 3 (Predicted); Belongs to the peptidase S1 family.

Cathelicidin antimicrobial peptide.

Cathepsin G.

Cathelicidin antimicrobial peptide.

Defensin alpha 11.

Cathelicidin antimicrobial peptide.

Neutrophil antibiotic peptide NP-2; Active in vitro against S.aureus, fungi, Gram-positive and Gram-negative bacteria and to a lesser extent against an enveloped virus.