Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 1, an antimicrobial peptide implicated in the resistance of epithelial surfaces to microbial colonization. This gene maps in close proximity to defensin family member, defensin, alpha 1 and has been implicated in the pathogenesis of cystic fibrosis. The mature form of Beta-defensin 1 is 36 amino acids. Beta-defensins (also designated BD, and hBD in human) are small cationic peptides with broad-spectrum antimicrobial activity. Produced in mucosal epithelia and neutrophils of several species, Beta-defensins are developmentally regulated. Research indicates that human Beta-defensin 1 may contribute to the antimicrobial activity of airway surface fluid and may play a role in the mucosal defenses of the lung. Human β-defensin 1 shares homology with other Beta-defensins from human blood filtrate and is also

Calretinin Polyclonal

Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesothe liomas and some pulmonary adenocarcinomas.

Calretinin Polyclonal