Recombinant Human Beta Defensin-4

SKU:BHP11000370
Suppliers
ProSpec-Tany TechnoGene Ltd
ProSpec-Tany TechnoGene Ltd
Details Products
Overview
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RUO recombinant Beta Defensin-4 (Human) protein for mechanistic studies and assay development. Supplied as a traceable protein input (E. coli; >98% (SDS-PAGE) purity; lyophilized; MW 5 kDa) for reproducible assay inputs.
Target DEFB104B
Species Human
Options selector
Catalog no. Size
cyt-599-5UG 5 ug
cyt-599-20UG 20 ug
cyt-599-1MG 1 mg
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size (3) — 5 ug, 20 ug, 1 mg
  • Lead time: options listed as “in stock at manufacturer” typically ship in 5–7 business days; other statuses may take longer.
  • Storage: Lyophilized Beta Defensin-4 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at the recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No cyt-599
Alternative Names HBD-4, DEFB-4, HBD4, DEFB104B, Beta-defensin 4, BD-4.
Biological Activity Determined by its ability to chemoattract human monocytes using a concentration range of 0.1-50 ng/ml, corresponding to a specific activity of 20,000-10,000,000 units/mg.
Concentration 1 mg/ml
Expression System
  • E. coli
Form Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation The DEFB4 (1mg/ml) was lyophilized with 20mM sodium Phosphate buffer pH-7.4 and 130mM NaCl.
Product Type
  • Proteins & Peptides
  • Cytokines and Growth Factors
  • Other Protein
Protein Length 50
Protein Size 5 kDa
Purity Greater than 98.0% as determined by:<br>(a) Analysis by RP-HPLC.<br>(b) Analysis by SDS-PAGE.
Solubility It is recommended to reconstitute the lyophilized Beta Defensin-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Source Escherichia Coli.
Species Human
Storage Lyophilized Beta Defensin-4 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Target DEFB104B

Recombinant Human Beta Defensin-4 is supplied as a recombinant protein for in vitro research use.

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. 4 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. The beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.

Beta Defensin-4 Human Recombinant: Exploring the Potential of a Novel Antimicrobial Peptide Abstract: Beta Defensin-4 (hBD-4) human recombinant is a promising antimicrobial peptide with unique properties and potential therapeutic applications. This research paper provides an in-depth analysis of hBD-4, including its characteristics, mode of action, and potential uses. Furthermore, novel methodologies for the production and optimization of hBD-4 human recombinant are proposed, shedding light on its future implications in the field of infectious disease management. Introduction: In the face of increasing drug-resistant infections, alternative therapeutic strategies are crucial. Antimicrobial peptides, such as hBD-4, have gained attention due to their broad-spectrum activity against pathogens. This paper aims to explore the distinctive features of hBD-4 and propose innovative approaches for its production and optimization. Characteristics and Mode of Action: hBD-4 is a cationic peptide comprising 50 amino acids and is characterized by a unique structure that contributes to its antimicrobial properties. The mechanism of action involves the disruption of microbial membranes and subsequent cell death. Additionally, hBD-4 exhibits immunomodulatory effects, including the stimulation of chemotaxis and modulation of the inflammatory response. Production of hBD-4 Human Recombinant: Efficient production methodologies for hBD-4 human recombinant are essential for its therapeutic applications. Various expression systems, such as bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents advantages and challenges, necessitating careful selection for high yields and protein quality. Optimization strategies, including codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as chromatography and ultrafiltration, have been optimized to isolate high-quality hBD-4 recombinant. Potential Applications: hBD-4 human recombinant demonstrates potential therapeutic applications in combating drug-resistant pathogens. Its broad-spectrum antimicrobial activity against bacteria, viruses, and fungi positions it as a promising candidate for infectious disease management. Moreover, hBD-4 shows promise in wound healing and tissue regeneration due to its ability to promote angiogenesis and stimulate cell migration. Exploring its potential in combination with drug delivery systems for targeted therapy is an exciting avenue for future research. Conclusion: hBD-4 human recombinant represents a novel antimicrobial peptide with diverse potential applications. Optimizing production methodologies and elucidating its mechanisms of action will further enhance its clinical utility. With its broad-spectrum antimicrobial activity and potential implications in wound healing and targeted therapy, hBD-4 human recombinant holds promise as an innovative therapeutic agent.

Product format

Provided as a recombinant protein suitable for in vitro workflows such as binding studies, screening, and assay development. Refer to the specifications table for expression format and molecular properties.

What is the purity of Recombinant Human Beta Defensin-4 (Human)?
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE. BioHippo includes a Certificate of Analysis (CoA) confirming purity per lot with every order.
What buffer / formulation is this protein supplied in?
Supplied as: The DEFB4 (1mg/ml) was lyophilized with 20mM sodium Phosphate buffer pH-7.4 and 130mM NaCl. Reconstitute lyophilized material in sterile ultrapure water or the recommended buffer per the datasheet prior to use.
How should Recombinant Human Beta Defensin-4 (Human) be stored?
Lyophilized Beta Defensin-4 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles. Prepare single-use aliquots after reconstitution to avoid repeated freeze–thaw cycles.
What expression system was used to produce this protein?
This recombinant protein was expressed in E. coli. The system was selected to achieve high yield, correct folding, and appropriate post-translational modifications.
Is this protein biologically active?
Determined by its ability to chemoattract human monocytes using a concentration range of 0.1-50 ng/ml, corresponding to a specific activity of 20,000-10,000,000 units/mg. Refer to the product datasheet for recommended assay conditions and controls.
Is this protein approved for clinical or in vitro diagnostic use?
No. Supplied for Research Use Only (RUO) — not intended for therapeutic applications or in vitro diagnostic procedures.
Can I request a custom size, tag variant, or formulation?
Yes. BioHippo can accommodate custom requests including alternative sizes, His/GST/Fc tag variants, bulk quantities, and custom formulations. See the Customization & Add-ons tab or email support@biohippo.com.

Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.

Bibliography: Semple F, Dorin JR. Beta-defensins: multifunctional modulators of infection, inflammation and more? J Innate Immun. 2012;4(4):337-348. Rodríguez-Jiménez FJ, Krause A, Schulz S, Forssmann U, Conejo-García JR, Schreeb R. Distribution of new human beta-defensin genes clustered on chromosome 20 in functionally different segments of epididymis. Genomics. 2003;81(2):175-183. Harder J, Bartels J, Christophers E, Schroder JM. Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic. J Biol Chem. 2001;276(8):5707-5713. Schibli DJ, Hunter HN, Aseyev V, et al. The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. J Biol Chem. 2002;277(10):8279-8289. Wu Z, Hoover DM, Yang D, Boulegue C, Santamaria F, Oppenheim JJ, Lubkowski J, Lu W. Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human β-defensin 3. Proc Natl Acad Sci U S A. 2003;100(15):8880-8885.
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