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BD-4, human recombinant protein
DEFB104A; DEFB4; BD-4; DEFB-4; DEFB104; MGC118942; MGC118944; MGC118945; hBD-4
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q8WTQ1 |
|---|---|
| Calculated MW | ~6.0 kDa |
| Gene ID | 140596 |
|---|---|
| Gene Symbol | DEFB4 |
| Other Names | Beta-defensin 3, Defensin, beta 103, Defensin-like protein, DEFB103A, BD3, DEFB103, DEFB3, DEFB103B |
| Gene Source | Human |
| Source | E. coli |
| Assay&Purity | SDS-PAGE; ≥98% |
| Assay2&Purity2 | HPLC; ≥98% |
| Recombinant | Yes |
| Target/Specificity | BD-4 |
| Application Notes | Centrifuge the vial prior to opening. Reconstitute in sterile dd H₂O to a concentration ≥ 100 µg/ml. This solution can then be diluted into other aqueous buffers and stored at 4 °C for 2-7 days and at -20 °C for future use. |
| Format | Lyophilized protein |
| Storage | -20°C; Sterile filtered and lyophilized from 20 mM PBS, pH 7.4 and 130 mM NaCl. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Defensins are cationic peptides with a large spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The Alpha defensins are differentiated from the Beta-defensins by the pairing of their 3 disulfide bonds. Four human Beta-defensins have been identified to date; BD-1, BD-2, BD-3 and BD-4. Beta-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. Beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence (for BD-1 a propeptide region). Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta Defensin-4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 50 amino acids. The BD-4 is purified by proprietary chromatographic techniques.
References
Conejo-Garcia J.-R.,et al.FASEB J. 15:1819-1821(2001).
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