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 |
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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.](productimages/extendimages/pmc05939666__jiy02401.jpg)
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
![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.](productimages/extendimages/pmc05939666__jiy02402.jpg)
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
Not For Human Consumption!
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