Recombinant Epstein-Barr Virus Lytic Switch Protein Bzlf1 (BZLF1) Protein (His-SUMO)

Name: Recombinant Epstein-Barr Virus Lytic Switch Protein Bzlf1 (BZLF1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04468P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) BZLF1.

Collections: All products, High-quality recombinant proteins, Other 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

Description	Recombinant Epstein-Barr Virus Lytic Switch Protein Bzlf1 (BZLF1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P03206
Target Symbol	BZLF1
Synonyms	BZLF1; Trans-activator protein BZLF1; EB1; Zebra
Species	Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MMDPNSTSEDVKFTPDPYQVPFVQAFDQATRVYQDLGGPSQAPLPCVLWPVLPEPLPQGQLTAYHVSTAPTGSWFSAPQPAPENAYQAYAAPQLFPVSDITQNQQTNQAGGEAPQPGDNSTVQTAAAVVFACPGANQGQQLADIGVPQPAPVAAPARRTRKPQQPESLEECDSELEIKRYKNRVASRKCRAKFKQLLQHYREVAAAKSSENDRLRLLLKQMCPSLDVDSIIPRTPDVLHEDLLNF
Expression Range	1-245aa
Protein Length	Full Length
Mol. Weight	42.9kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Plays a key role in the switch from latent infection to lytic cycle producing new virions. Acts as a transcription factor, inducing early lytic cycle genes, and as a origin binding protein for genome replication. BZLF1 activates the promoter of another EBV gene (BSLF2+BMLF1).
Subcellular Location	Host nucleus.
Protein Families	BZIP family
Database References	KEGG: vg:3783744

Gene Functions References

position C189 in Zta impacts sequence-specific binding to DNA containing modified and unmodified cytosine. PMID: 29772230
ERK/c-Jun recruits Tet1 to Induce Zta expression and Epstein-Barr virus reactivation through DNA demethylation. PMID: 27708396
HIF-1alpha directly bound the promoter of the EBV primary latent-lytic switch BZLF1 gene, Zp, activating transcription via a consensus hypoxia-response element (HRE) located at nt -83 through -76 relative to the transcription initiation site. PMID: 28617871
By CRISPR/Cas9-induced inactivation of TLR9, MyD88, IRAK4 and IRAK1 we confirm that BZLF1 repression is dependent on functional TLR9 and MyD88 signaling, and identify IRAK4 as an essential element for TLR9-induced repression of BZLF1 expression upon BCR cross-linking PMID: 29088270
Comparison of how AP-1 (Jun/Jun dimer) and Epstein-Barr virus Zta recognize methyl groups within their cognate response elements PMID: 28158710
Binding of PARP1 at the BZLF1 lytic switch promoter restricts Epstein Barr Virus reactivation. PMID: 28456021
These results suggest that lytic Epstein-Barr virus infection attenuates the transmission of inflammatory paracrine senescence through BZLF1 downregulation of TNF-alpha secretion and alters the inflammatory microenvironment to allow virus propagation and persistence. PMID: 27334596
The dimerization region of Epstein-Barr virus Zta is not required to mediate host CIITA repression. PMID: 26653871
These results suggest that Epstein-Barr Virus BZLF1 attenuates the proinflammatory responses to facilitate viral replication. PMID: 26537683
Presented is a model of DNA damage responses activation during the EBV lytic cycle in which ZEBRA induces ATM kinase phosphorylation, in a DNA binding dependent manner, to modulate gene expression. PMID: 25950714
RanBPM was found to enhance Zta-dependent transcriptional activity via the inhibition of Zta sumoylation. PMID: 25900136
Studied the effects of BZLF1 on cellular response to DNA damage in nasopharyngeal carcinoma cells. PMID: 26006018
This is the first report to characterize BZLF1 gene polymorphisms in paediatric patients from our geographical region and to suggest the association of these polymorphisms with malignant lymphomas. PMID: 24666405
ZEBRA and BGLF5 each function as viral host shutoff factors. PMID: 24705134
these results indicate a critical role for MCAF1 in AP-1-dependent Rta activation of BZLF1 transcription. PMID: 24598729
Performed the recombinant production of a biologically active Epstein-Barr virus BZLF1 trans-activator, i.e., Z-encoded broadly reactive activator (ZEBRA), that recognized specific DNA motifs. PMID: 24291446
B-cell specific transcription factor, Oct-2, inhibits the function of the viral immediate-early protein, BZLF1, and prevents lytic viral reactivation. PMID: 22346751
the genetic characteristics of BZLF1 gene and its promoter Zp of the epidemic strains in children with primary Epstein-Barr virus (EBV)-associated diseases PMID: 24772891
TAF-Ibeta promotes BZLF1 expression and subsequent lytic infection by affecting chromatin at the BZLF1 promoter PMID: 23691099
Mutation of MEF2 sites severely impaired both spontaneous and induced expression of not only BZLF1, but also BRLF1 in comparison to wild-type or revertant virus cases. PMID: 23843637
The B-cell-specific transcription factor and master regulator Pax5 promotes Epstein-Barr virus latency by negatively regulating the viral immediate early protein BZLF1. PMID: 23678172
Zta drives cell migration and invasion through MMPs PMID: 23409137
BZLF1 is a pioneer factor that reverses epigenetic silencing of viral DNA to allow escape from latency. PMID: 22969425
Genome-wide analyses of Zta binding to the Epstein-Barr virus genome reveals interactions in both early and late lytic cycles and an epigenetic switch leading to an altered binding profile. PMID: 23015699
The mechanism of p53-mediated Epstein-Barr viral Zta protein activation requires the cooperative action of another cellular factor, Sp1. PMID: 22711357
Herpes simplex virus type 1 induces the reactivation of latent EBV by triggering BZLF1 expression. PMID: 22188237
Epigenetic modification of the BZLF1 promoter in latent Raji cells by histone H3 lysine 27 trimethylation (H3K27me3), H3K9me2/me3, and H4K20me3. PMID: 22357272
The authors show that expression of the Epstein-Barr virus immediate-early protein BZLF1 is restricted to Blimp1-positive epithelial cells in oral hairy leukoplakia. PMID: 22278826
The abundance of Zta protein coupled with the methylation status of the Epstein-Barr virus (EBV) genome act together to co-ordinate the expression of lytic cycle genes at the majority of EBV promoters. PMID: 22022468
conclude that TGF-beta induces EBV lytic reactivation via the canonical Smad pathway by activating BZLF1 gene expression through multiple SBEs acting in concert PMID: 21593157
study reports that specific single missense mutations within the basic domain of ZEBRA induce the formation of nuclear aggresomes, which strongly sequester the mutant protein PMID: 21233201
The authors conclude that the ZIIR element is a potent silencing element in the BZLF1 promoter Zp and plays a key role in establishment and maintenance of virus latency by inhibiting activation of Zp through the PKC signal transduction pathway. PMID: 21389123
This study also reveals that the interaction between Zta and Ku80 involves the C-terminal region of Zta and the 425 aa N-terminal region of Ku80. PMID: 21123545
Data show that Daudi cells express glucocorticoid receptors that mediate Dex-dependent up-regulation of BZLF1 mRNA levels. PMID: 20466055
By a chromatin immunoprecipitation (ChIP) assay, the authors show that Ubn-1 blocks EB1-human herpesvirus 4 DNA interaction. PMID: 21084479
These observations indicate that the EBV lytic transactivator protein Zta displays activity consistent with a pathogenic role in pulmonary fibrosis associated with herpesvirus infection. PMID: 20817778
Results strongly suggest that oxidative stress contributes to the reactivation of EBV lytic cycle, through induction of BZLF-1 gene expression. PMID: 19898754
Enhanced binding of ZEBRA to the origin of lytic DNA replication is crucial for lytic viral DNA replication. PMID: 20808903
Data propose that EBV protein Zta activates SOCS3 protein as an immune escape mechanism that both suppresses optimal IFNalpha secretion by human monocytes and favors a state of type I IFN irresponsiveness in these cells. PMID: 20689596
sumoylation of BZLF1 regulates its transcriptional activity through histone modification during Epstein-Barr virus productive replication PMID: 20516063
Study renders ZEBRA-MD a promising candidate for therapeutic protein delivery applications. PMID: 20385549
These data suggest that Zta acts by inducing and/or stabilizing a DNA hairpin structure during productive infection. PMID: 20444899
viral BZLF1 protein is crucial both to establish latency and to escape from it; Epstein Barr virus has evolved to its host mode of dna methylation. PMID: 20080764
Our work implies that the balance of promyelocytic leukemia protein and BZLF1 levels in cells may affect how each protein functions. PMID: 16307818
there are three phosphorylation sites on the Epstein-Barr virus ZEBRA protein PMID: 16321978
Results describe the crystal structure of ZEBRA's DNA binding domain bound to an Epstein-Barr virus lytic gene promoter element. PMID: 16483937
Comparison among viral orthologues of Zta suggest that a conserved N-terminal extension of the consensus B-ZIP domain is required for this multivalent DNA recognition capacity of Zta and is essential for viral reactivation.[Zta] PMID: 16971443
BZLF1 is expressed as an immediate-early gene following primary EBV infection of B lymphocytes. PMID: 17079287
We report that the plasma cell differentiation factor, XBP-1s, activates the expression of the master regulator of EBV lytic activation, BZLF1. PMID: 17898050
HHV8-RTA and EBV-BZLF1 are co-localized and physically interact with each other in dually-infected PELs, required for the mutual inhibition of the two molecules PMID: 18253508

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.