DEFB103A
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Official Full Name
defensin, beta 103A -
Overview
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 103B, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense. -
Synonyms
DEFB103A;defensin, beta 103A;DEFB3, DEFB103, defensin, beta 3;beta-defensin 103;DEFB 3;HBD 3;HBD3;HBP 3;HBP3;beta-defensin 3;defensin, beta 3;defensin, beta 103;defensin-like protein;BD-3;DEFB3;HBP-3;hBD-3;DEFB-3;DEFB103
Recombinant Proteins
- Human
- E.coli
- Wheat Germ
- In Vitro Cell Free System
- Non
- GST
- His
Cat.# | Product name | Source (Host) | Species | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
DEFB103A-84H | Recombinant Human DEFB103A protein | E.coli | Human | Non | 45 | |
DEFB103A-2522H | Recombinant Human DEFB103A Protein, GST-tagged | Wheat Germ | Human | GST | ||
DEFB103A-7304H | Recombinant Human DEFB103A protein, His-tagged | E.coli | Human | His | Gly23-Lys67 | |
DEFB103A-85H | Recombinant Human DEFB103A protein, His-tagged | E.coli | Human | His | Gly 23-Lys 67 | |
DEFB103A-464HCL | Recombinant Human DEFB103A cell lysate | Human | Non | |||
DEFB103A-2431HF | Recombinant Full Length Human DEFB103A Protein, GST-tagged | In Vitro Cell Free System | Human | GST | Full L. 67 amino acids | |
DEFB103A-301628H | Recombinant Human DEFB103A protein, GST-tagged | E.coli | Human | GST | Met23-Lys67 | |
DEFB103A-541H | Active Recombinant Human DEFB103A Protein | E.coli | Human | Non | ||
DEFB103A-69H | Recombinant Human DEFB103A Protein | E.coli | Human |
Background
What is defb103a protein?
Defb103a is a protein that belongs to the beta-defensin family.Beta-defensins are small cationic peptides with antimicrobial properties. They help defend against pathogens.Defb103a, also known as intelectin-1, is specifically expressed in the mammalian intestine and pancreas.It binds to galactofuranose on the surface of some gut bacteria and fungi in a calcium-dependent manner. This promotes microbial clearance.
Defb103a plays a role in maintaining gut microbiome homeostasis by selectively targeting certain microbes for clearance via direct antimicrobial activity.It facilitates nutrient absorption by binding bile salts and fatty acids after microbial lysis. This aids fat digestion.Defb103a knockout mice studies show impaired growth, dysbiosis and increased susceptibility to enteric infections.
Genetic variants in DEFB103A are linked to inflammatory bowel diseases like Crohn's disease in humans.It has lectin properties and helps mediate interactions between gut microbes and epithelial cells.Defb103a is an intestinal antimicrobial peptide crucial for gut immunity, digestion, microbiota balance and protecting against enteric infections.
What is the function of defb103a protein?
Antimicrobial activity: Defb103a exhibits direct microbicidal action against certain gut bacteria and fungi. It binds to galactofuranose on microbial cell surface in a calcium-dependent manner. This binding enables clearance of target microbes from the intestine via microbial lysis.
Regulation of gut microbiota: By selectively clearing certain microbes, Defb103a helps maintain homeostasis of gut microbial communities. This prevents overgrowth of potential pathogenic microbes in the intestine.
Fat digestion and nutrient absorption: After microbial lysis, Defb103a binds bile salts and fatty acids to facilitate their absorption. This aids in optimal digestion and absorption of dietary fats in the small intestine.
Intestinal immunity: Defb103a acts as an antimicrobial peptide to protect the gut from infections. It also mediates interactions between gut bacteria and intestinal epithelial cells.
Defb103a related signaling pathway
Microbial recognition and binding: Defb103a recognizes and binds to galactofuranose residues on microbial cell surfaces in a calcium-dependent manner via its lectin domain.
Microbial clearance: Binding triggers direct antimicrobial activity of Defb103a through membrane disruption, resulting in lysis of target microbes.
Intestinal epithelial signaling: Microbial lysis/binding releases microbial ligands that activate epithelial TLR/NOD signaling like TLR2/4. This triggers inflammatory/repair responses.
Defb103a Related Diseases
- Inflammatory bowel disease (IBD): Polymorphisms and decreased expression of Defb103a associated with IBD like Crohn's disease. Suggests its protective role.
- Obesity: Defb103a deficient mice exhibit increased body weight and adiposity. It regulates fatty acid absorption and metabolism.
- Necrotizing enterocolitis: Defb103a protects premature infants from fatal NEC by maintaining intestinal integrity and microbiota balance.
- Probiotic development: Bacteria overexpressing Defb103a could promote gut health by competing with pathogens.
- Biomarker for gut disease: Stool/serum Defb103a levels can indicate IBD, dysbiosis, infections, malabsorption.
Biomedical Application of defb103a Protein
- Probiotic development: Bacteria overexpressing Defb103a could promote gut health by competing with pathogens.
- Antimicrobial drug target: Defb103a mimicking peptides may treat gastrointestinal infections by microbiota modulation.
- Diagnostic for malnutrition: Defb103a expression analysis complements techniques to identify environmental enteric dysfunction.
- Diagnostic for malnutrition: Defb103a expression analysis complements techniques to identify environmental enteric dysfunction.
Case Study
(Gordon Y C Cheung, 2018)
Fig2. Export by Pmt provides resistance to human antimicrobial peptides (AMPs). (A and B) Killing assays were performed in triplicate in phenol-soluble modulin (PSM)-deficient (∆αβhld), PSM/Pmt-deficient (∆αβhld∆pmt), and PSM/Pmt Walker site-mutated (∆αβhld/pmtWalker) isogenic strains in the LAC (USA300) background.
(Sabine Nuding, 2013)
Fig3. HBD3 immunostaining in H. pylori negative and positive mucosal antrum.
HBD3 immunohistochemistry shows no or only a marginal staining in both, H. pylori negative (A) and positive antrum (B). In contrast, HBD3 is clearly found in the cytoplasm of the epithelium in Crohn's colitis (C) and unspecific bronchiolitis (D).
Quality Guarantee
High Purity
Fig1. SDS-PAGE (DEFB103A-84H).Fully biologically active when compared to standard. The ED50 as determined by anti-microbial activity against E. coli. is less than 30 μg/mL, corresponding to a specific activity of > 33.3 IU/mg.
Involved Pathway
DEFB103A involved in several pathways and played different roles in them. We selected most pathways DEFB103A participated on our site, such as Beta defensins,Defensins,Immune System, which may be useful for your reference. Also, other proteins which involved in the same pathway with DEFB103A were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
---|---|
Beta defensins | DEFB125,DEFB104A,DEFB116,DEFB129,DEFB4A,DEFB119,CCR6,DEFB106A,DEFB1,DEFB4B |
Immune System | IFIT11,TRIM69,HAVCR2,TPP2,DEFB125,WWP1,MB21D1,RAPGEF3,FCN2,CYBB |
Defensins | DEFB4B,DEFB1,DEFB116,DEFB121,ART1,DEFB125,DEFA1,DEFB4A,DEFA5,DEFB106A |
Innate Immune System | TANK,BAIAP2,CNPY3,ABI1B,DUSP3B,CLEC6A,DEFA5,SIGIRR,DEFB125,DEFB1 |
Protein Function
DEFB103A has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by DEFB103A itself. We selected most functions DEFB103A had, and list some proteins which have the same functions with DEFB103A. You can find most of the proteins on our site.
Function | Related Protein |
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Interacting Protein
DEFB103A has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with DEFB103A here. Most of them are supplied by our site. Hope this information will be useful for your research of DEFB103A.
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References
- Nuding, S; Gersemann, M; et al. Gastric Antimicrobial Peptides Fail to Eradicate Helicobacter pylori Infection Due to Selective Induction and Resistance. PLOS ONE 8:-(2013).
- Mehlotra, RK; Zimmerman, PA; et al. Variation in human -defensin genes: new insights from a multi-population study. INTERNATIONAL JOURNAL OF IMMUNOGENETICS 40:261-269(2013).