Recombinant human alpha Defensin 1 protein
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Recombinant human alpha Defensin 1 protein is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, FuncS.
View Alternative Names
DEF1, DEFA2, MRS, DEFA1B, DEFA1, Neutrophil defensin 1, HNP-1, HP-1, HP1
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The alpha defensin 1 peptide disrupts the integrity of microbial membranes by inserting into microbial lipid bilayers leading to membrane permeabilization and lysis. This activity is not limited to bacteria; it also affects fungi and some viruses. The peptide is not part of a complex but it acts as a standalone antimicrobial agent. Besides its antimicrobial role alpha defensin 1 can modulate inflammatory responses and influence wound healing. It interacts with chemokines and cytokines affecting immune modulation.
Pathways
Alpha defensin 1 is integral to the antimicrobial response pathway and innate immunity processes. In the antimicrobial defense pathway it collaborates with other defensins and lysozymes to ensure pathogen elimination. In the innate immunity processes it works in conjunction with cytokines such as IL-8 which recruits more neutrophils to infection sites. Both pathways highlight alpha defensin 1's importance in both direct defense mechanisms and immune signaling.
Specifications
Form
Lyophilized
General info
Function
Effector molecule of the innate immune system that acts via antibiotic-like properties against a broad array of infectious agents including bacteria, fungi, and viruses or by promoting the activation and maturation of some APCs (PubMed : 15616305, PubMed : 17142766, PubMed : 20220136, PubMed : 24236072). Interacts with the essential precursor of cell wall synthesis lipid II to inhibit bacterial cell wall synthesis (PubMed : 20214904). Inhibits adenovirus infection via inhibition of viral disassembly at the vertex region, thereby restricting the release of internal capsid protein pVI, which is required for endosomal membrane penetration during cell entry (PubMed : 18191790). In addition, interaction with adenovirus capsid leads to the redirection of viral particles to TLR4 thereby promoting a NLRP3-mediated inflammasome response and interleukin 1-beta (IL-1beta) release (PubMed : 35080426). Induces the production of proinflammatory cytokines including type I interferon (IFN) in plasmacytoid dendritic cells (pDCs) by triggering the degradation of NFKBIA and nuclear translocation of IRF1, both of which are required for activation of pDCs (PubMed : 27031443).
Sequence similarities
Belongs to the alpha-defensin family.
Post-translational modifications
ADP-ribosylation drastically reduces cytotoxic and antibacterial activities, and enhances IL8 production.. Phosphorylation at Tyr-85 has been found in some cancer cell lines, and interferes with ADP-ribosylation.
Target data
Product promise
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