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Defensins are a family of microbicidal and cytotoxic peptides thought to be involved in host defense. Additionally we are shipping Defensin, alpha 4, Corticostatin Kits (8) and Defensin, alpha 4, Corticostatin Proteins (3) and many more products for this protein.
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DEFA4 displays antimicrobial activity against E. coli, S. faecalis, and C. albicans.
Results indicate that the gene expression of DEFA 1/3 and 4 was significantly increased in all tumours - except for a significant decrease of DEFA 4 gene expression in pleomorphic adenomas.
DEFA1-3 and DEFA4 mRNA level in peripheral blood cells can be used to identify chronic myeloid leukaemia patients who are at risk of being imatinib-resistant, before initiation of the therapy.
The combination of an increased expression of the antimicrobial peptide DEFA-4, the oncogene S100-A7, epidermal growth factor, and tenascin-c, and a decreased Doc-1 expression in oral leukoplakia might characterize its potency of malignant transformation.
Crystal structure of HNP-4.
DEFA4 was upregulated in IPF patients with acute exacerbation
Lys-for-Arg substitutions in rhesus myeloid alpha-defensin improved microbicidal activity against certain bacteria
Depleting CRP4 is incompatible with a proper cardiac development and function. CRP4 is a novel antiremodeling factor regulated, at least to some extent, by cardiac cGMP.
Backbone cyclization provides a means for engineeringalpha-defensins to improve their biological activity while providing excellent stability to serum degradation and highlighting the potential of peptide scaffolds for development of novel compounds.
bactericidal activity predominantly affects noncommensal bacteria
MMP-7-dependent procryptdin activation in vivo provides mouse Paneth cells with functional peptides for apical secretion into the small intestine lumen
the prosegment of Crp4 inhibits Crp4 bactericidal activity by blocking peptide-mediated perturbation of target cell membranes
Crp4 disulfide arrangement confers essential protection from degradation by this critical activating proteinase, allowing antibacterial action.
cryptdin-1 and cryptdin-4 exhibit circadian oscillation
function of the conserved salt bridge in Crp4 is not linked to bactericidal activity or proteolytic stability of the mature peptide.
CRP4 mediates cGMP/PKG stimulation of SM-specific gene expression, and PKG plays an important role in regulating the phenotype of VSMCs
Kinetics of Crp4 translocation coupled with peptide-induced vesicle leakage are reported.
Beta-sheet-containing Crp4 induces membrane permeabilization more effectively than disulfide-null Crp4 by translocating and forming transient membrane defects.
Lys-for-Arg replacements in cryptdin 4 attenuated bactericidal activity
Defensins are a family of microbicidal and cytotoxic peptides thought to be involved in host defense. They are abundant in the granules of neutrophils and also found in the epithelia of mucosal surfaces such as those of the intestine, respiratory tract, urinary tract, and vagina. Members of the defensin family are highly similar in protein sequence and distinguished by a conserved cysteine motif. Several alpha defensin genes are clustered on chromosome 8. This gene differs from other genes of this family by an extra 83-base segment that is apparently the result of a recent duplication within the coding region. The protein encoded by this gene, defensin, alpha 4, is found in the neutrophils\; it exhibits corticostatic activity and inhibits corticotropin stimulated corticosterone production.
, defensin, alpha 4, preproprotein
, neutrophil defensin 4
, alpha-defensin 4, corticostatin
, Paneth cell-specific alpha-defensin 4
, alpha-defensin 4
, alpha-defensin, 28
, defensin related cryptdin 4
, defensin, alpha, 28
, defensin-related cryptdin-4