Recombinant Human Neutrophil Defensin 1 (DEFA1) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-02835P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Neutrophil Defensin 1 (DEFA1) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-02835P
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Product Overview

Description Recombinant Human Neutrophil Defensin 1 (DEFA1) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P59665
Target Symbol DEFA1
Synonyms alpha 1; DEF1; DEF1_HUMAN; DEFA1; DEFA1B; DEFA2; Defensin 1; Defensin; Defensin; alpha 1; Defensin; alpha 1; myeloid related sequence; Defensin; alpha 2; HNP-1; HNP-2; HNP1; HP-1; HP-2; HP1; HP2; MRS; Myeloid related sequence; Neutrophil defensin 1; Neutrophil defensin 2
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence DIPEVVVSLAWDESLAPKHPGSRKNMACYCRIPACIAGERRYGTCIYQGRLWAFCC
Expression Range 1-94aa
Protein Length Full Length
Mol. Weight 37.2 kDa
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.
Subcellular Location Secreted.
Protein Families Alpha-defensin family
Database References

HGNC: 2761

OMIM: 125220

KEGG: hsa:1667

STRING: 9606.ENSP00000372136

UniGene: PMID: 29950924

  • Human Neutrophil Peptide 1 directly binds and neutralizes Exotoxin A of Pseudomonas aeruginosa. PMID: 29738776
  • Pretreatment of component b with human alpha-defensin-1 prior to addition of component a of Clostridium perfringens iota toxin prevented intoxication implicating that alpha-defensin-1 interacts with the toxin b component to prevent the formation of biologically active iota toxin on cells. PMID: 29635426
  • DEFA1, DEFA3, and PPBP expression was significantly increased in hyperlipidemia and coronary heart disease patients compared with controls. PMID: 28420383
  • HNP1 upregulation of cytokine expression in pDCs was inhibited by blockade of NF-kappaB activation or knockdown of IRF1, demonstrating the importance of these two signaling events in HNP1-induced pDC activation. PMID: 27031443
  • these results demonstrate that HNPs1-3 may be potent inhibitors of ADAMTS13 activity, likely by binding to the central A2 domain of VWF and physically blocking ADAMTS13 binding. PMID: 27207796
  • Increased alpha-defensin expression is associated with risk of coronary heart disease in hyperlipidemia patients. PMID: 27430968
  • Levels in sera and CSF were elevated in Alzheimer disease patients compared with controls. PMID: 27082275
  • the decreased HNP-1 production in the polymorphonuclear phagocytes form elderly individuals might have an important participation in the increased susceptibility to infectious diseases. PMID: 26323500
  • Increased levels of neutrophil defensin 1, apolipoprotein E, clusterin, and zinc-alpha-2-glycoprotein are present in carotid atherosclerotic plaque secretomes. PMID: 26795031
  • HNP1 functions as a "molecular brake" on macrophage-driven inflammation, ensuring both pathogen clearance and the resolution of inflammation with minimal bystander tissue damage. PMID: 27044108
  • HP1 binding to the chromosomal passenger complex becomes particularly important when Aurora B phosphorylates kinetochore targets to eliminate erroneous microtubule attachments PMID: 26954544
  • data demonstrate that HNP-1 induces IL-8 production not only through P2Y6, but also through additional P2 receptors via an ERK1/2-dependent mechanism in intestinal epithelial cells. PMID: 25816245
  • Results showed that NO and NaNO2 can be considered as factors regulating the chemoattractant properties of defensin HNP1 in neutrophils PMID: 25772994
  • Overexpression of DEFA1 retained independent prognostic significance for B-ALL outcome. PMID: 25802479
  • The expression of alpha-defensins 1, 2 and 3 is up-regulated in hypercholesteremia. PMID: 25300997
  • Defensins promote the differentiation into activated CD91(bright) dendritic cells. PMID: 25351513
  • Elevated DEFA1 levels in diabetes are independent of DEFA1 copy numbers. PMID: 25083086
  • The AD-1 assay offers another test with high sensitivity and specificity for diagnosing a prosthetic joint infection. PMID: 25256621
  • The concentrations of LL37, alpha-1, beta-1 and beta-2 defensins were determined by ELISA. Serum AMPs did not change during attacks and did not correlate with acute phase reactants. PMID: 24747281
  • DEFA1 encodes an antibacterial peptide that is bacteriocidal against S. aureus, E. coli, and P. aeruginosa. PMID: 2997278
  • Side chain hydrophobicity is the critical factor that determines HNP1 protein binding potential. PMID: 24236072
  • A decrease in salivary HNP 1-3 levels might be a biological factor for predisposition to oral ulcers in patients with Behcet disease and oral infection in healthy patients. PMID: 22861387
  • HNP-1 enhances hepatic fibrosis in fatty liver by inducing hepatic stellate cell proliferation. PMID: 23682724
  • -defensin 1 increases EFS-induced contractions of rat detrusor muscles PMID: 23542712
  • sub-inhibitory doses of HNP-1 potently enhance the activity of a number of anti-gp41 antibodies and peptide inhibitors PMID: 23785290
  • Human defensin alpha-1 is an innate immune molecule that is secreted by HCT116 cells in response to Trypanosoma cruzi infection, inhibits Trypanosoma cruzi motility, and plays an important role in reducing cellular infection. PMID: 23980110
  • 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. PMID: 23050799
  • This study suggests that HNPs 1-3 promote tumor invasion and are potential indicators of disease progression in patients with bladder cancer. PMID: 23011762
  • Invariant gly residue is important for alpha-defensin folding, dimerization PMID: 22496447
  • alpha-Defensin (DEFA1) was the most differentially overexpressed gene in this sample and may be related to the onset of Bell's palsy and Ramsay Hunt Syndrome. PMID: 22737966
  • expressional level of HNPs 1,2 and 3 were significantly higher and their distributions overlapped in cancerous tissues of gastric cancer patients PMID: 22297599
  • Dimerization contributes to some but not all of the activities of HNP1. PMID: 22270360
  • A high DEFA1 gene CN was significantly associated with intestinal involvement in BD patients. PMID: 22219625
  • Directly isolated dendritic cells secrete alpha-defensins 1-3; E2 inhibits this secretion. Same trend is observed in myeloid dendritic cells isolated from pregnant women in their first trimester (low plasma E2) and third trimester (high plasma E2). PMID: 21861873
  • Increased levels of human neutrophil peptides 1, 2, and 3 in peritoneal fluid of patients with endometriosis: association with neutrophils, T cells and IL-8. PMID: 21831449
  • Human granulocyte precursors transfected with siRNA against serglycin displayed reduced capability to retain fully processed HNP-1. PMID: 21849484
  • HNP1-3 concentrations in patients with multidrug-resistant tuberculosis were significantly lower than in drug-susceptible pulmonary TB and healthy controls PMID: 21333105
  • Changes in the expression pattern of DEFA 1/3 seem to be involved in the development of gingival irritation fibromas, whereas chronic inflammation might be of less importance. PMID: 21187770
  • alpha-defensins 1-3 in T cells from patients with SJS/TEN may be involved in the etiopathology of these life-threatening diseases induced by medications. PMID: 20880148
  • defensin-alpha(1)is a biologically active peptide exhibiting a dose-dependent trypanocidal effect in vitro against trypomastigotes and amastigotes of Trypanosoma cruzi line Tulahuen PMID: 21165432
  • HNP-1 (alpha), HBD-2 (beta) and RTD-1 (theta) have anti-HIV-1 activity, but different mechanisms of action PMID: 20305815
  • HNP-1 mainly enhanced the expression of IL-8 in epithelial cells, whereas it enhanced transforming growth factor-beta and vascular endothelial growth factor expressions in lung fibroblasts. PMID: 20715983
  • Our report of DEFA1-3 expression by human omental adipocytes adds to the role of adipocytes in the primary defense against bacterial infection. PMID: 20424487
  • Data show that high production of alpha-defensins1-3 by immature DCs appears as a host protective factor against progression of HIV-1 infection, suggesting potential diagnostic, therapeutic and preventive implications. PMID: 20195543
  • The total amount of gingival crevicular fluid human neutrophil peptides 1 and 2 were not different among periodontitis, gingivitis, and health control groups; there was no correlation with clinical periodontal parameters. PMID: 20151808
  • HNP1 binds to the cell wall precursor lipid II and reduction of lipid II levels in the bacterial membrane significantly reduces bacterial killing. PMID: 20214904
  • Combining the distance constraints from the 3d experiment and the chemical-shift-derived torsion angles, we obtained a de novo high-resolution NMR structure of HNP-1 PMID: 19963419
  • HNP1 mediates host immune responses to tumors in situ through the recruitment and subsequent activation of immature dendritic cells PMID: 19861439
  • The solid-state NMR structure of HNP-1 has close similarity to the crystal structures of the HNP family, with the exception of the loop region between the first and second beta-strands. PMID: 20097206
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