Active Recombinant Human DEFB4 protein(1-50aa)

Cat.No. : DEFB4-18H
Product Overview : Recombinant Human DEFB4 protein(Q8WTQ1)(50aa) was expressed in E.coli.
Availability June 27, 2025
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Species : Human
Source : E.coli
Tag : Non
Protein Length : 1-50aa
Form : Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 130 mM NaCl.
Bio-activity : Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration range of 0.1-100.0 ng/ml.
Molecular Mass : Approximately 6.0 kDa, a single non-glycosylated polypeptide chain containing 50 amino acids.
AA Sequence : EFELDRICGY GTARCRKKCR SQEYRIGRCP NTYACCLRKW DESLLNRTKP
Endotoxin : Less than 1 EU/μg of rHuBD-4 as determined by LAL method.
Purity : > 98 % by SDS-PAGE and HPLC analyses.
Storage : Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Reconstitution : We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
Gene Name DEFB104A defensin beta 104A [ Homo sapiens (human) ]
Official Symbol DEFB104A
Synonyms BD-4; DEFB4; hBD-4; DEFB-4; DEFB104
Gene ID 140596
mRNA Refseq NM_080389
Protein Refseq NP_525128
UniProt ID Q496I2

Antimicrobial Peptide Resistance Mechanism Contributes to Staphylococcus aureus Infection

Journal: The Journal of Infectious Diseases    PubMed ID: 29351622    Data: 2018/4/1

Authors: Gordon Y C Cheung, Emilie L Fisher, Michael Otto

Article Snippet:LL-37 was purchased from Invivogen, and human beta defensin 3 ([hBD3] DEFB103A) was purchased from Creative BioMart.. The hBD3 was resuspended in water, LL-37 in 0.01% acetic acid.The hBD3 was resuspended in water, LL-37 in 0.01% acetic acid.

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. *, P < .05; **, P < .01; ***, P < .001 (two-way analysis of variance [ANOVA] with Tukey’s posttest). Error bars show the mean ± standard deviation (SD). (C and D) The LAC ?αβhld?pmt strain was complemented with plasmids harboring wild-type or ATP-binding motif (Walker A, Walker B) mutated pmt genes. Killing assays, LL-37, 180 μg/mL; human beta defensin 3 (hBD3), 75 μg/mL. *, P < .05; ***, P < .001; ****, P < .0001 (n = 5/group; one-way ANOVA with Dunnett’s posttest versus values in the pmt mutant). Error bars show the mean ± SD. Abbreviations: CFU, colony-forming units.

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. *, P < .05; **, P < .01; ***, P < .001 (two-way analysis of variance [ANOVA] with Tukey’s posttest). Error bars show the mean ± standard deviation (SD). (C and D) The LAC ?αβhld?pmt strain was complemented with plasmids harboring wild-type or ATP-binding motif (Walker A, Walker B) mutated pmt genes. Killing assays, LL-37, 180 μg/mL; human beta defensin 3 (hBD3), 75 μg/mL. *, P < .05; ***, P < .001; ****, P < .0001 (n = 5/group; one-way ANOVA with Dunnett’s posttest versus values in the pmt mutant). Error bars show the mean ± SD. Abbreviations: CFU, colony-forming units.

Structures of antimicrobial peptides (AMPs) used in this study. Structures of phenol-soluble modulin (PSM)α3 (Protein Data Bank indentification [PDB ID] 5KGY) and PSMβ2 (PDB ID 5KGZ) as examples of α- and β-type PSMs, respectively, and of LL-37 (PDB ID 2K6O) and human beta defensin 3 ([hBD3] PDB ID 1KJ6). N termini are placed at the (bottom) left. Structures were obtained from the structural data bank at the National Center for Biotechnology Information. α-helices and β-sheets are shown as ribbons. Red and blue colors represent positive and negative charges, and yellow color represents sulfur atoms. Note that these are solution structures (except for LL-37, obtained in lipid micelles), whereas the confirmation during membrane insertion may be considerably different.

Structures of antimicrobial peptides (AMPs) used in this study. Structures of phenol-soluble modulin (PSM)α3 (Protein Data Bank indentification [PDB ID] 5KGY) and PSMβ2 (PDB ID 5KGZ) as examples of α- and β-type PSMs, respectively, and of LL-37 (PDB ID 2K6O) and human beta defensin 3 ([hBD3] PDB ID 1KJ6). N termini are placed at the (bottom) left. Structures were obtained from the structural data bank at the National Center for Biotechnology Information. α-helices and β-sheets are shown as ribbons. Red and blue colors represent positive and negative charges, and yellow color represents sulfur atoms. Note that these are solution structures (except for LL-37, obtained in lipid micelles), whereas the confirmation during membrane insertion may be considerably different.

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