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AB54409

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

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Active

Accession

P59665

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in water

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"ACYCRIPACIAGERRYGTCIYQGRLWAFCC","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P59665","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
A few weeks
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Alpha defensin 1 also known as human defensin 1 or neutrophil defensin 1 is a small cationic peptide with a mass of approximately 3-4 kDa. This protein is mainly expressed in neutrophils where it plays an essential role in the body's innate immune system. Additional sites of expression include Paneth cells in the intestines where alpha defensins contribute to mucosal immunity. Its structure consists of three intramolecular disulfide bonds that confer stability and enable its antimicrobial properties.
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.

Alpha defensin 1 is linked to inflammatory conditions and autoimmune diseases such as Crohn’s disease and ulcerative colitis. In Crohn's disease altered levels of alpha defensin 1 relate to intestinal inflammation and microbial imbalance. It is also connected to rheumatoid arthritis where its role in inflammation may exacerbate disease activity. In these conditions alpha defensin 1 interacts with other proteins including TNF-alpha an important cytokine involved in inflammatory pathways.

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.

Product protocols

Target data

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).
See full target information DEFA1

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