Recombinant Human Beta-Defensin 3 / DEFB103A Protein

Name: Recombinant Human Beta-Defensin 3 / DEFB103A Protein
Brand: Beta LifeScience
SKU: BL-1235SG
Availability: InStock

Collections: Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	P81534
Synonym	Beta-defensin 3, BD-3, DEFB-3, HBD3, hBD-3, Defensin, beta 103, Defensin-like protein, BD3, DEFB103, DEFB3.
Background	Defensins are a large family of peptides of which two groups exist in mammals: alpha defensins and beta defensins - which are distinguishable by the spacing and connectivity of the conserved cysteine residues within the mature peptides. It is thought that the function of defensins in the eradication of pathogens from the host system is to insert themselves into the bacterial membrane under the influence of membrane potential, in doing so form channels which lead to leakage of cytoplasmic molecules and cell death. Unlike hBD-1, this second peptide, human beta-defensin-2 (hBD-2), is regulated at a transcriptional level in response to contact with microorganisms, and is highly effective in killing the gram negative bacteria Its expression is also upregulated by the cytokine tumor necrosis factor-alpha.
Description	Recombinant Human Beta-Defensin 3 (DEFB103A) was produced in E. coli. This protein is purified with our unique purification methods.
Source	E.coli
Molecular Weight	5.4 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human Beta-Defensin 3 / DEFB103A Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Exhibits antimicrobial activity against Gram-positive bacteria S.aureus and S.pyogenes, Gram-negative bacteria P.aeruginosa and E.coli and the yeast C.albicans. Kills multiresistant S.aureus and vancomycin-resistant E.faecium. No significant hemolytic activity was observed.
Subcellular Location	Secreted.
Protein Families	Beta-defensin family
Database References	HGNC: 15967 OMIM: 606611 KEGG: hsa:414325 STRING: 9606.ENSP00000324633 UniGene: Hs.283082
Tissue Specificity	Highly expressed in skin and tonsils, and to a lesser extent in trachea, uterus, kidney, thymus, adenoid, pharynx and tongue. Low expression in salivary gland, bone marrow, colon, stomach, polyp and larynx. No expression in small intestine.

Gene Functions References

this study shows that hBD3 amplifies the response to bacterial DNA in both mouse and human immune cells in a TLR9-dependent manner PMID: 28102569
the role of DEFB103 gene copy number variation (CNV) in ankylosing spondylitis (AS) susceptibility, was investigated. PMID: 26224324
It may be concluded hepatitis B virus up-regulates HBD-3 and A3G expression in vivo and in vitro in placental trophoblast and lack of this up-regulation is possibly associated with intrauterine transmission of hepatitis B. PMID: 25196417
The encoded peptide displays antimicrobial activity against S. aureus and E. faecium. PMID: 11085990
these observations suggest that there may be an interracial difference in DEFB4/103A copy numbers between admixed populations and a relationship between DEFB1 single nucleotide polymorphisms and DEFB4/103A copy number variation PMID: 23194186
Human beta-defensin 3 peptide is increased and redistributed in Crohn's ileitis PMID: 23511030
study demonstrates that HBD2 and 3 activate plasmacytoid dendritic cells by enhancing the intracellular uptake of CpG and self DNA and promote DNA-induced IFN-alpha production in a TLR9-dependent manner PMID: 23776172
Mapping of key residues in the interaction between human Beta-defensin 3 and CXCR4 reveals key defensin motifs involved in protein binding. PMID: 23659571
These results suggest an important role for hBD3 in inducing dendritic cell activation, migration, and polarization. PMID: 22951718
Using a large, unique cohort of pediatric CA-SAB, this study found no significant association between DEFB1 genetic variation or DEFB4/DEFB103 gene copy number and susceptibility for Staphylococcus aureus bacteremia PMID: 22384213
Human beta-defensin 3 exhibits further functions than antimicrobial peptide activity in cultured bone cells, including stimulation of proliferation and differentiation. PMID: 21520074
Data show that high-glucose conditions inhibited the BD3 expression of epidermal keratinocytes. PMID: 21442129
hBD-1 might function as a tumor suppressor gene in oral squamous cell carcinoma, while hBD-2 and -3 might be protooncogenes. PMID: 21280982
extraplacental membranes can react differentialy to the arrival of E. coli, secreting HBD2 and HBD3 mainly in the choriodecidua region. PMID: 21122132
PPARgamma regulates the 1,25D-induced hBD-3 and cathelicidin expression in keratinocytes through the regulation of AP-1 and p38 activity. PMID: 20970965
hBD3 represents a novel NF-kappaB-regulated mediator of CCR7 expression and anti-apoptotic pathways. PMID: 21071608
Inducibility of HBD3 influences the severity of Gram-positive skin infection in humans in vivo. PMID: 20404083
Data show that beta-defensin cluster (DEFB4, DEFB103 and DEFB104) varied between 2 and 9 copies per genome, and high copy numbers (>4) were underrepresented among patients, suggesting that increased copy numbers could protect from CD. PMID: 20483368
Human pulmonary cells produce hBD-3 upon L. pneumophila infection via a TLR-JNK-AP-1-dependent pathway which may contribute to an efficient innate immune defense. PMID: 20615218
The beta-defensin antimicrobial peptides hBD1, hBD2 and hBD3 were expressed by immature dendritic cells as well as gingival epithelial cells. PMID: 20618959

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.