Recombinant Human Papillomavirus Type 16 Regulatory Protein E2 (E2) Protein (GST)

Name: Recombinant Human Papillomavirus Type 16 Regulatory Protein E2 (E2) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09979P
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 Homo sapiens (Human) E2.

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Product Overview

Description	Recombinant Human Papillomavirus Type 16 Regulatory Protein E2 (E2) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P03120
Target Symbol	E2
Synonyms	E2; Regulatory protein E2
Species	Human papillomavirus type 16
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	METLCQRLNVCQDKILTHYENDSTDLRDHIDYWKHMRLECAIYYKAREMGFKHINHQVVPTLAVSKNKALQAIELQLTLETIYNSQYSNEKWTLQDVSLEVYLTAPTGCIKKHGYTVEVQFDGDICNTMHYTNWTHIYICEEASVTVVEGQVDYYGLYYVHEGIRTYFVQFKDDAEKYSKNKVWEVHAGGQVILCPTSVFSSNEVSSPEIIRQHLANHPAATHTKAVALGTEETQTTIQRPRSEPDTGNPCHTTKLLHRDSVDSAPILTAFNSSHKGRINCNSNTTPIVHLKGDANTLKCLRYRFKKHCTLYTAVSSTWHWTGHNVKHKSAIVTLTYDSEWQRDQFLSQVKIPKTITVSTGFMSI
Expression Range	1-365aa
Protein Length	Full Length
Mol. Weight	68.8 kDa
Research Area	Epigenetics And Nuclear Signaling
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.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
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 role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
Subcellular Location	Host nucleus.
Protein Families	Papillomaviridae E2 protein family
Database References	KEGG: vg:1489080

Gene Functions References

Anti-E2, -L1, and -p16(INK4A) antibodies in sera were determined by western blot. Among 116 samples, 69 (60%) were HPV DNA-positive. Percentages seropositive for anti-E2, -L1, and -p16(INK4A) antibodies were 39.6, 22.4, and 23.3%, respectively. PMID: 29744680
The papillomavirus E8;E2 protein shares the hinge domain with E2 and acts as a repressor of viral replication. A large fraction of HPV31 E8;E2 is phosphorylated at S78 in the hinge region, and this is important for E8;E2's repression activity. Surprisingly, phosphorylation at S78 in E8;E2 has no impact on viral replication in tissue culture but rather seems to modulate the expression of a small number of cellular genes. PMID: 29167339
The papillomavirus E2 protein has splicing-related activities. (Review) PMID: 27867028
HPV E2 protein targets Rad50-interacting protein 1 (Rint1) to facilitate virus genome replication. PMID: 28031358
the ORC2 complex with E2 restricts viral replication in the maintenance phase of the viral replication program PMID: 27701460
A mutation has been identified in HPV16 E2 that abrogates interaction with ChlR1, and it was shown that ChlR1 regulates the chromatin association of HPV16 E2 and that this virus-host interaction is essential for viral episome maintenance. PMID: 27795438
data indicate that the E2 protein links the viral replication cycle to epithelial differentiation via SRSF3, a key cellular regulator of high-risk (HR)-HPV gene expression PMID: 26962216
HPV16 E2-Brd4 interaction is more responsible for the transcriptional activation of host genes rather than repression. PMID: 26365679
E2 may be one of the drivers of genomic instability and carcinogenesis in vivo. PMID: 26474276
HPV 16 E2 can modulate ErbB-3 by interacting with Nrdp-1, which is involved in the regulation of this receptor, via ubiquitination and degradation. PMID: 26963794
mapping analysis revealed that disruption/deletion events within E2 gene occurred in high grade and cervical cancer samples while no evidence of E2 gene disruption was documented among low grade cervical intraepithelial neoplasias PMID: 25959607
study reports the detection of adenine/thymine-clustered hypermutation in the E2 gene of HPV16 isolated from clinical specimens with low- and high-grade cervical intraepithelial neoplasia lesions (CIN1/3) PMID: 25914233
This study demonstrates that E2 proteins of high risk human papillomavirus reduce STING and IFN-kappa transcription. PMID: 24614210
phosphorylation of serine 243 in the hinge region of HPV-16 E2 is essential for interaction with Brd4 and required for host chromosome binding PMID: 25340539
E2-mediated potentiation of TNF-alpha-induced NF-kappaB activation increases viability and survival in SiHa (human cervical cancer) cells. PMID: 25572145
L1 protein directly interacts with E2 and enhances E2-dependent replication and transcription activation. PMID: 25911730
HPV-16 E2 may regulate NF-kappaB and STAT3 activation in the presence of TNF-alpha with implications on the survival of HPV-infected cells. PMID: 24833467
E2 gene polymorphisms of episomal HPV16 did not affect transcriptional regulation. Nucleotide variation as well as epigenetic modification of the LCR might play a role in inducing malignant transformation of cells containing episomal HPV16. PMID: 25556457
Consistent with prior reports, TopBP1 co-localized in discrete nuclear foci and was in complex with papillomavirus E2 protein. PMID: 25666521
The results suggest that interactions between TopBP1 and E2 and between Brd4 and E2 are required to correctly initiate human papillomavirus 16 DNA replication but are not required for continuing DNA replication. PMID: 25694599
Daxx protein interacts with HPV16 E2 protein, mainly in cytoplasm. PMID: 25842852
In this study, the authors show that recruitment of positive transcription elongation factor b, a functional interaction partner of Brd4 in transcription activation, is important for E2's transcription activation activity of human papillomavirus 16. PMID: 25140737
Among the E subgroup, variation at position 3684 C>A results in the amino acid substitution T310K and was more common among the E2 undisrupted cases (7/9; 77.7%), compared to controls (2/9; 22.2%). PMID: 25032221
These data support a mechanism whereby gC1qR plays an important role in HPV-16 E2-induced human cervical squamous carcinoma cell apoptosis via a mitochondria-dependent pathway. PMID: 25288439
reveal a novel role for E2 in regulating the activities of NF-kappaB and STAT3 that may have implications in carcinogenic progression of HPV16-infected cells under conditions of stromal inflammation PMID: 25460081
CCHCR1 interacts specifically with the E2 protein of human papillomavirus type 16 on a surface overlapping BRD4 binding PMID: 24664238
This study underscores the significance of investigating alternative mechanisms of E2 expression and oncogenes E6/E7 transcripts in vivo as biomarkers for disease severity in cervical carcinomas. PMID: 24170557
These studies bring new insights for understanding Brd4-mediated stabilization of human papillomavirus 16 E2 protein, and provide an additional mechanism by which the chromatin-associated Brd4 regulates E2 functions. PMID: 24448221
E2 protein plays a pivotal role in viral transcriptional regulation, DNA replication, and modification of various cellular processes.[review] PMID: 24923176
E8;E2C repressor limits viral transcription and replication throughout the complete life cycle of HPV16. PMID: 24198405
APOBEC3 upregulated by IFN-beta induce E2 hypermutation of HPV16 in cervical keratinocytes. PMID: 24227842
HPV 16 E2 induces apoptosis by silencing the gC1qR gene or inhibiting p38 MAPK/JNK signalling in cervical squamous cell carcinoma PMID: 23651874
Transactivation by E2 proteins was less cell-type dependent but differed in an HPV-type-dependent manner. PMID: 23407419
The frequencies of E2 gene 68C and 133G variations were significantly higher in patients with CIN II-III and those with cervical cancer than in those with CIN I and those with cervical inflammation. PMID: 23076195
An interaction between human papillomavirus 16 E2 and TopBP1 is required for optimum viral DNA replication and episomal genome establishment. PMID: 22973044
The present work provides an overview of E2 biological functions across multiple HPV genotypes. PMID: 22761572
Three new sequence variations were identified at positions 2791, 2823 and 3361 in E2 of HPV16 isolated form women in Greece. PMID: 22294445
NRIP enhances HPV 16 gene expression via interaction with either GR or viral E2. PMID: 22177699
These data suggest that E2 regulatory protein of human papillomaviruses potentiates tumour necrosis factor-induced NF-kappaB signalling mediated by TRAF5 activation through direct binding. PMID: 21715600
Data indicate that the enhanced E2R showed greater repression of transcription from E2-responsive reporter plasmids in mammalian cell culture. PMID: 21482558
NRIP is a novel binding protein for human papillomavirus 16 (HPV-16) E2 protein and directly interacts with the TAD of HPV-16 E2. PMID: 21543494
HPV E2 protein binds to the regulatory region of the human IL-10 gene (-2054 nt) and induces high promoter activity in epithelial cells. PMID: 21468579
The expression of all E8wedgeE2C proteins inhibited the growth of HeLa cells. PMID: 21191025
E2 protein from HPV16 activated MMP9 promoter predominantly via the MEK1-ERK1/2-AP-1 signaling pathway. PMID: 20596661
study showed that E2 is expressed at various precursor stages of cervical carcinoma; data validate previous assumptions of the crucial role of E2 in the early steps of HPV infection and of its negative link with expression of the viral E6 and E7 oncogenes PMID: 20530671
The papillomavirus E2 proteins preferentially interacted with alpha importins 3 and 5, and showed very weak or no interaction with the other three widely expressed alpha importins (alpha1, alpha 4, and alpha 7). PMID: 20193720
Recognition of DNA by E2 regulatory protein was determined to a DNA target containing the spacer sequence TATA. PMID: 20185566
Abrogation of the interaction between P-TEFb and Brd4 thus provides a mechanism for E2-mediated repression of the viral oncogenes from the integrated viral genomes in cancer cells. PMID: 19846528
L2 selectively inhibits the transcriptional activation property of E2 and that there is a direct interaction between the two proteins PMID: 15681049
NMR structure of the HPV-16 E2 DNA binding domain PMID: 15702528

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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.

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