Recombinant Human BD3 Protein (His Tag)

Name: Recombinant Human BD3 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-0389
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	His
Host Species	Human
Accession	P81534
Synonym	BD-3, DEFB-3, DEFB103, DEFB3, hBD-3, HBD3, HBP-3, HBP3
Background	Beta-defensin 3 is a member of the defensin family. Defensin family is comprised by microbicidal and cytotoxic peptides made by neutrophils. Members of the beta-defensin 3 family are highly similar in protein sequence. Beta-defensin 3 shows antimicrobial activity against Gram-positive bacteria S.aureus and S.pyogenes, Gram-negative bacteria P.aeruginosa and E.coli and the yeast C.albicans. Beta-defensin 3 is abundantly expressed in skin and tonsils, and to a lesser extent in trachea, uterus, kidney, thymus, adenoid, pharynx and tongue. It is also expressed in salivary gland, bone marrow, colon, stomach, polyp and larynx. However, in small intestine, it cannot be detected. Defensin has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense. Beta-defensin 3 kills multiresistant S.aureus and vancomycin-resistent E.faecium. It has no significant hemolytic activity.
Description	A DNA sequence encoding the mature form of human DEFB103A (P81534) (Gly 23-Lys 67) was expressed, with a His tag at the N-terminus.
Source	E.coli
Predicted N Terminal	Met
AA Sequence	Gly 23-Lys 67
Molecular Weight	The recombinant human DEFB103A consists of 61 a.a. and predicts a molecular mass of 7.3 KDa. It migrates as an approximately 12 KDa band in SDS-PAGE under reducing conditions.
Purity	>99% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 50mM Tris, 0.3% Ttiton X-100, 0.3% SKL, pH 8.5.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°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

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.