Beta-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensin 2 or DEFB2 is a cystein-rich cationic 41 amino acid antimicrobial peptide of 4-5 kDa. Human DEFB2 is produced by epithelial cells upon stimulus by lipopolysaccharides and proinflammatory cytokines TNFalpha and IL1beta. Contact of keratinocytes with gram-negative bacteria results in rapid induction of DEFB2 protein. DEFB2 has been described as a dynamic component of the local epithelial defense system of the skin, intestinal and respiratory tract, where it functions by protecting surfaces from infection. Its local expression has been associated with skin lesions like psoriasis as well as infected lung epithelia of patients with cystic fibrosis.
Clone
Polyclonal
Isotype
IgG
Host species
Rabbit
Species Reactivity
Human
Cellular Localization
Secreted
Positive Control
Tonsil, kidney, stomach, colon and pancreas cancer
Applications
IHC, ELISA, IF, WB
Intended Use
Research Use Only