DEFA5 Antibody

Code CSB-PA034616
Size US$166
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Image
  • The image on the left is immunohistochemistry of paraffin-embedded Human liver cancer tissue using CSB-PA034616(DEFA5 Antibody) at dilution 1/15, on the right is treated with synthetic peptide. (Original magnification: ×200)
  • The image on the left is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using CSB-PA034616(DEFA5 Antibody) at dilution 1/15, on the right is treated with synthetic peptide. (Original magnification: ×200)
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Product Details

Uniprot No.
Target Names
DEFA5
Alternative Names
alpha 5 antibody; DEF5 antibody; DEF5_HUMAN antibody; Defa antibody; Defa29 antibody; DEFA5 antibody; Defcr29 antibody; Defcr5 antibody; Defensin 5 antibody; Defensin alpha 5 antibody; Defensin alpha 5 Paneth cell specific antibody; Defensin alpha 5 preproprotein antibody; Defensin antibody; Enteric defensin antibody; HD 5 antibody; HD5 antibody; HD5(20-94) antibody; HD5(63-94) antibody; MGC129728 antibody; RD 5 antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Synthetic peptide of Human DEFA5
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Isotype
IgG
Purification Method
Antigen affinity purification
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
-20°C, pH7.4 PBS, 0.05% NaN3, 40% Glycerol
Form
Liquid
Tested Applications
ELISA,IHC
Recommended Dilution
Application Recommended Dilution
ELISA 1:1000-1:2000
IHC 1:25-1:100
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing.
Gene References into Functions
  1. The binding mechanisms of HD5 on lipopolysaccharide in comparison to a bare DMPC lipid membrane was studied using molecular dynamics (MD) simulations. PMID: 30187138
  2. Bifidobacterium infantis NLS super strain decreases Paneth cell counts and expression of alpha-defensin-5 in celiac disease. PMID: 27636409
  3. Human alpha-Defensin-5 is a potential candidate biomarker to molecularly differentiate Crohn's colitis from ulcerative colitis, to our knowledge. These data give us both a potential diagnostic marker in Human alpha-Defensin-5 and insight to develop future mechanistic studies to better understand crypt biology in Crohn's colitis. PMID: 28817680
  4. Different dynamics and pathway of disulfide bonds reduction has been demonstrated for two human defensins, HD5 and HBD-3. PMID: 28106297
  5. These data support capsid stabilization and redirection to the lysosome during infection as a general antiviral mechanism of alpha-defensins against nonenveloped viruses. PMID: 28119475
  6. Human adenovirus 3 produces large amounts of penton-dodecahedra (PtDd), virus-like particles, during replication, which also function in blocking of HD5. PMID: 28077642
  7. no biologic differences between wild-type HD5 and its variants were observed on HD5 antibacterial activity against Escherichia coli PMID: 27160989
  8. a moderately active linear peptide derived from the alpha-defensin HD5 can be engineered to enhance antimicrobial activity almost comparable to the native peptide. PMID: 26206286
  9. The study used ion mobility coupled to mass spectrometry to track the structural changes in HD-5 upon disulfide bond reduction. PMID: 25970658
  10. The study reports the screening of human defensin 5 against the Keio Collection of E. coli strains and shows how this important hostdefense peptide kills bacteria and how bacteria protect themselves against the attack from the human host. PMID: 25430675
  11. Authors show that although NOD2 by itself can slightly up-regulate expression of HD5 and HD6, it can strongly down-regulates their expression during differentiation of the Paneth cell lineage mainly by inhibiting activation of the MAPK pathway. PMID: 25433720
  12. HD5ox, at least in part, exerts its antibacterial activity against E. coli and other Gram-negative microbes in the cytoplasm. PMID: 25664683
  13. These data support a model in which HD5 prevents furin from accessing human papillomavirus 16 L2 by occluding the furin cleavage site via direct binding to the viral capsid. PMID: 25540379
  14. Enteric alpha-defensin HD5 and beta-defensin hBD2 shared similar toxin-unfolding effects with HNP1, albeit to different degrees. PMID: 25517613
  15. our results highlight the potential contribution of altered alpha-defensin HD-5 expression in the formation of a viral/tumour-permissive environment in high-risk HPV infection and progression to cancer of the uterine cervix PMID: 25196670
  16. DEFA5 displays antimicrobial activity against E. coli, E. aerogenes, B. cereus, and S. aureus. PMID: 15616305
  17. Data indicate that cellular effects of defensin 5 involve interactions with the extra-cellular domain of tumor necrosis Factor 1. PMID: 24681099
  18. Anti-HIV activity of human defensin 5 in primary CD4+ T cells under serum-deprived conditions is a consequence of defensin-mediated cytotoxicity. PMID: 24086683
  19. This study considers the redox properties of HD-5 and reports that the reduced form, HD-5 red, is a zinc-ion chelator. PMID: 23841778
  20. HD5 neutralizes JC polyomavirus infection by stabilizing the viral capsid and disrupting virus trafficking. PMID: 24198413
  21. human alpha defensin 5 increases LGR stem cell migration into wound beds, leading to enhanced healing, bacterial reduction, and hair production through the augmentation of key Wnt and wound healing transcripts. PMID: 24165598
  22. E-cadherin expression in squamous cells is reduced by HD-5 PMID: 23958301
  23. Subnanometer resolution cryo-electron microscopy structures of HD5 complexed with both neutralization-sensitive and -resistant human adenovirus chimeras, were determined. PMID: 23620768
  24. study demonstrate that binding of integrin alphavbeta5 and alpha defensin 5 have opposite effects on the elastic response of adenovirus type 35, revealing a direct link between virus-host interactions and the mechanical properties of the capsid PMID: 23269786
  25. structural analysis of human enteric alpha-defensin HD5 shows a crucial role for hydrophobicity at the dimer interface PMID: 22573326
  26. Several arginine residues and tyrosine 27 are important for HD-5 antibacterial activity. PMID: 22354633
  27. Defensins 5 and 6 enhance HIV-1 infectivity through promoting HIV attachment. PMID: 21672195
  28. The hydrophobicity of regions 2, 9 & 10 was higher than in other regions. It was difficult for the HD molecule to have many conformations because of its 3 S-S bridges; however, it responds to various external factors by restricting conformation. PMID: 21873175
  29. The concentrations of human defensin 5, HBD1, and HBD2 in vulvovaginal candidiasis patients were higher than in controls. PMID: 19080508
  30. Statistical analysis of gene expression showed a distinction between regions 1 and 2 of the small intestin for HD5. PMID: 21125297
  31. HalphaD-5 and HbetaD-2 may protect fallopian tubes during microbial infection. PMID: 20629326
  32. To respond to LPS stimulation, human primary endocervical epithelial cells may function in the mucosal immune defense through TLR4 activation and HD5 secretion. PMID: 20819643
  33. This study demonstrated the multifunctional roles of the activation process in human defensin-5. PMID: 20375624
  34. The authors provide direct evidence that human alpha-defensins block adenovirus infection by preventing uncoating during cell entry. PMID: 20130047
  35. Data show that DEFA5-expressing mice had striking losses of segmented filamentous bacteria and fewer interleukin 17 (IL-17)-producing lamina propria T cells. PMID: 19855381
  36. By acting as a prodefensin convertase in human Paneth cells, trypsin is involved in the regulation of innate immunity in the small intestine. PMID: 12021776
  37. Defensin 5 transgenic mice were resistant to oral challenge with virulent Salmonella typhimurium; support for a critical in vivo role of epithelial-derived defensins in mammalian host defence PMID: 12660734
  38. Crystal structure of HD-5. PMID: 17088326
  39. HD-5 binds to the cell membrane of intestinal epithelial cells and induces secretion of the chemokine interleukin (IL)-8 PMID: 17250830
  40. The persistence of HD5-chymotrypsinogen-trypsin complex in Crohn disease may be attributable to increased luminal levels of proteinase inhibitors such as alpha1-anti-trypsin. PMID: 18258845
  41. Single nucleotide polymorphism in defensin alpha 5 Paneth cell associated with inflammatory bowel diseases in caucasoid population. PMID: 18394979
  42. Clostridium difficile toxin B interacts with high affinity with HD5 which may provide a defense mechanism against clostridial glucosylating cytotoxins. PMID: 18435932
  43. the primary function of the conserved salt bridge in HD5 is to ensure correct processing of proHD5 and subsequent stabilization of mature alpha-defensin in vivo PMID: 18499668
  44. HBD-2 and HD-5 may be involved in defending against invasion by BV-related microorganisms and the decrease in IL-4 concentration may increase susceptibility to bacterial vaginosis PMID: 18635180
  45. Human enteric defensin (HD)-5 and HD-6 were detected in Paneth cells, which are observed in the gastric metaplastic mucosa as well as small intestinal epithelia. Less H. pylori was observed in the intestinal metaplasia with HD-5 expressing Paneth cells. PMID: 19250512
  46. Self-association and multivalent binding may play integral roles in the ability of alpha-defensin 5 (HD5) to protect against infections caused by viruses and other infectious agents. PMID: 19542459
  47. Results report on the antibacterial properties and cellular interaction of Human Defensin 5 as a function of its positive charge and hydrophobicity. PMID: 19589339

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Subcellular Location
Secreted. Cytoplasmic vesicle, secretory vesicle. Note=Peptides HD5(20-94), HD5(23-94) and HD5(29-94) are found within tissues, HD5(20-94) being the predominant intracellular form. Peptides HD5(56-94) and HD5(63-94) are found in the extracellular milieu, HD5(63-94) being the most abundant form.
Protein Families
Alpha-defensin family
Tissue Specificity
Paneth cells of the small intestine (at protein level).
Database Links

HGNC: 2764

OMIM: 600472

KEGG: hsa:1670

STRING: 9606.ENSP00000329890

UniGene: Hs.655233

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