Peptidases are enzymes that are responsible for hydrolyzing peptide bonds of polypeptide chains during protein catabolism. Protease inhibitors are important peptidase regulators which halt enzymatic function. The WAP (whey acidic protein) domain, also referred to as the WAP-type four-disulfide core domain, is a signature protein motif that contains eight cysteine residues which form disulfide bonds and may exhibit protease inhibitor activity. WAP domain-containing proteins are thought to function in the immune defense by cleaving microbial proteolytic enzymes in order to prevent tissue penetration and infection. WFDC8 (WAP four-disulfide core domain protein 8), also known as WAP8, is a 241 amino acid secreted protein that contains three WAP domains and one BPTI/Kunitz inhibitor domain. WFDC8 is ubiquitously expressed, however highest levels are found in trachea and testis. A cluster of WAP genes, including WFDC8, exist on chromosome 20, suggesting they evolved by repeated duplications.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of WFDC8 of human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope mapping within an internal region of WFDC8 of human origin
Tissue Specificity
epitope mapping within an internal region of WFDC8 of human origin