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DCD encodes a secreted protein that is subsequently processed into mature peptides of distinct biological activities. Additionally we are shipping Dermcidin Antibodies (63) and Dermcidin Kits (10) and many more products for this protein.
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Identification of dermcidin in human sebaceous gland cells supports the concept that sebocytes play an important role in the innate immunity of the skin through the expression of antimicrobial peptides and specific lipids.
Reduced DCD concentration in sweat in patients with inflammatory acne may permit proliferation of P. acnes in pilosebaceous units, resulting in progression of inflammatory acne.
These findings imply that DCD promotes breast tumorigenesis via modulation of ERBB (show EGFR Proteins) signaling pathways
Dermcidin binds platelets and may inhibit the therapeutic action of aspirin following acute myocardial infarction.
Data indicate that Y-P30 (show CENPV Proteins)/dermcidin expressed in placentas of first trimester pregnancies.
Increased Dermcidin was also detected with immunoblotting.
major binding partners of LEKTI were found to be the antimicrobial peptide (show cAMP Proteins) dermcidin and the serine protease (show F2 Proteins) cathepsin G (show CTSG Proteins) and no kallikreins.
Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide (show cAMP Proteins) present in human sweat.
revealed that Nck1 (show NCK1 Proteins) SH2 domain binds to the phosphotyrosine residue at position 20 (Y20) of the DCD
dermcidin was a novel platelet aggregating agent, and potentiated the ADP induced thrombosis in the animal model as well as acutely inhibited glucose induced insulin (show INS Proteins) synthesis.
This gene encodes a secreted protein that is subsequently processed into mature peptides of distinct biological activities. The C-terminal peptide is constitutively expressed in sweat and has antibacterial and antifungal activities. The N-terminal peptide, also known as diffusible survival evasion peptide, promotes neural cell survival under conditions of severe oxidative stress. A glycosylated form of the N-terminal peptide may be associated with cachexia (muscle wasting) in cancer patients.
, diffusible survival/evasion peptide
, proteolysis inducing factor
, survival promoting peptide