Recombinant Human alpha Defensin 1/DEFA1 Protein

Beta LifeScience SKU/CAT #: BLA-12105P

Recombinant Human alpha Defensin 1/DEFA1 Protein

Beta LifeScience SKU/CAT #: BLA-12105P
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Product Overview

Host Species Human
Accession P59665
Synonym alpha 1 DEF1 DEF1_HUMAN DEFA1 DEFA1B DEFA2 Defensin Defensin 1 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
Description Recombinant Human alpha Defensin 1/DEFA1 Protein was expressed in E.coli. It is a Full length protein
Source E.coli
AA Sequence ACYCRIPACI AGERRYGTCI YQGRLWAFCC
Molecular Weight 4 kDa
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Lyophilised
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

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

Gene Functions References

  1. lower DEFA1/DEFA3 copy number (CNV < 7) is associated with higher susceptibility to hospital-acquired infections (HAIs) in critically ill patients, indicating that host genetic factors are involved in the development of HAIs PMID: 29950924
  2. Human Neutrophil Peptide 1 directly binds and neutralizes Exotoxin A of Pseudomonas aeruginosa. PMID: 29738776
  3. 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
  4. DEFA1, DEFA3, and PPBP expression was significantly increased in hyperlipidemia and coronary heart disease patients compared with controls. PMID: 28420383
  5. 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
  6. 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
  7. Increased alpha-defensin expression is associated with risk of coronary heart disease in hyperlipidemia patients. PMID: 27430968
  8. Levels in sera and CSF were elevated in Alzheimer disease patients compared with controls. PMID: 27082275
  9. 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
  10. Increased levels of neutrophil defensin 1, apolipoprotein E, clusterin, and zinc-alpha-2-glycoprotein are present in carotid atherosclerotic plaque secretomes. PMID: 26795031
  11. 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
  12. HP1 binding to the chromosomal passenger complex becomes particularly important when Aurora B phosphorylates kinetochore targets to eliminate erroneous microtubule attachments PMID: 26954544
  13. 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
  14. Results showed that NO and NaNO2 can be considered as factors regulating the chemoattractant properties of defensin HNP1 in neutrophils PMID: 25772994
  15. Overexpression of DEFA1 retained independent prognostic significance for B-ALL outcome. PMID: 25802479
  16. The expression of alpha-defensins 1, 2 and 3 is up-regulated in hypercholesteremia. PMID: 25300997
  17. Defensins promote the differentiation into activated CD91(bright) dendritic cells. PMID: 25351513
  18. Elevated DEFA1 levels in diabetes are independent of DEFA1 copy numbers. PMID: 25083086
  19. The AD-1 assay offers another test with high sensitivity and specificity for diagnosing a prosthetic joint infection. PMID: 25256621
  20. 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
  21. DEFA1 encodes an antibacterial peptide that is bacteriocidal against S. aureus, E. coli, and P. aeruginosa. PMID: 2997278
  22. Side chain hydrophobicity is the critical factor that determines HNP1 protein binding potential. PMID: 24236072
  23. 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
  24. HNP-1 enhances hepatic fibrosis in fatty liver by inducing hepatic stellate cell proliferation. PMID: 23682724
  25. -defensin 1 increases EFS-induced contractions of rat detrusor muscles PMID: 23542712
  26. sub-inhibitory doses of HNP-1 potently enhance the activity of a number of anti-gp41 antibodies and peptide inhibitors PMID: 23785290
  27. 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
  28. 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
  29. This study suggests that HNPs 1-3 promote tumor invasion and are potential indicators of disease progression in patients with bladder cancer. PMID: 23011762
  30. Invariant gly residue is important for alpha-defensin folding, dimerization PMID: 22496447
  31. 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
  32. expressional level of HNPs 1,2 and 3 were significantly higher and their distributions overlapped in cancerous tissues of gastric cancer patients PMID: 22297599
  33. Dimerization contributes to some but not all of the activities of HNP1. PMID: 22270360
  34. A high DEFA1 gene CN was significantly associated with intestinal involvement in BD patients. PMID: 22219625
  35. 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
  36. 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
  37. Human granulocyte precursors transfected with siRNA against serglycin displayed reduced capability to retain fully processed HNP-1. PMID: 21849484
  38. HNP1-3 concentrations in patients with multidrug-resistant tuberculosis were significantly lower than in drug-susceptible pulmonary TB and healthy controls PMID: 21333105
  39. 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
  40. 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
  41. 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
  42. HNP-1 (alpha), HBD-2 (beta) and RTD-1 (theta) have anti-HIV-1 activity, but different mechanisms of action PMID: 20305815
  43. 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
  44. 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
  45. 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
  46. 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
  47. 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
  48. 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
  49. HNP1 mediates host immune responses to tumors in situ through the recruitment and subsequent activation of immature dendritic cells PMID: 19861439
  50. 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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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