Recombinant Human papillomavirus type 16 Regulatory protein E2 (E2)

Code CSB-YP365852HML
MSDS
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Source Yeast
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Code CSB-EP365852HML-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP365852HML
MSDS
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Source Baculovirus
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Code CSB-MP365852HML
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
E2
Uniprot No.
Alternative Names
E2; Regulatory protein E2
Species
Human papillomavirus type 16
Expression Region
1-365
Target Protein Sequence
METLCQRLNV CQDKILTHYE NDSTDLRDHI DYWKHMRLEC AIYYKAREMG FKHINHQVVP TLAVSKNKAL QAIELQLTLE TIYNSQYSNE KWTLQDVSLE VYLTAPTGCI KKHGYTVEVQ FDGDICNTMH YTNWTHIYIC EEASVTVVEG QVDYYGLYYV HEGIRTYFVQ FKDDAEKYSK NKVWEVHAGG QVILCPTSVF SSNEVSSPEI IRQHLANHPA ATHTKAVALG TEETQTTIQR PRSEPDTGNP CHTTKLLHRD SVDSAPILTA FNSSHKGRIN CNSNTTPIVH LKGDANTLKC LRYRFKKHCT LYTAVSSTWH WTGHNVKHKS AIVTLTYDSE WQRDQFLSQV KIPKTITVST GFMSI
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

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.
Gene References into Functions
  1. 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
  2. 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
  3. The papillomavirus E2 protein has splicing-related activities. (Review) PMID: 27867028
  4. HPV E2 protein targets Rad50-interacting protein 1 (Rint1) to facilitate virus genome replication. PMID: 28031358
  5. the ORC2 complex with E2 restricts viral replication in the maintenance phase of the viral replication program PMID: 27701460
  6. 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
  7. 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
  8. HPV16 E2-Brd4 interaction is more responsible for the transcriptional activation of host genes rather than repression. PMID: 26365679
  9. E2 may be one of the drivers of genomic instability and carcinogenesis in vivo. PMID: 26474276
  10. 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
  11. 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
  12. 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
  13. This study demonstrates that E2 proteins of high risk human papillomavirus reduce STING and IFN-kappa transcription. PMID: 24614210
  14. 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
  15. E2-mediated potentiation of TNF-alpha-induced NF-kappaB activation increases viability and survival in SiHa (human cervical cancer) cells. PMID: 25572145
  16. L1 protein directly interacts with E2 and enhances E2-dependent replication and transcription activation. PMID: 25911730
  17. 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
  18. 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
  19. Consistent with prior reports, TopBP1 co-localized in discrete nuclear foci and was in complex with papillomavirus E2 protein. PMID: 25666521
  20. 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
  21. Daxx protein interacts with HPV16 E2 protein, mainly in cytoplasm. PMID: 25842852
  22. 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
  23. 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
  24. 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
  25. 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
  26. CCHCR1 interacts specifically with the E2 protein of human papillomavirus type 16 on a surface overlapping BRD4 binding PMID: 24664238
  27. 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
  28. 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
  29. E2 protein plays a pivotal role in viral transcriptional regulation, DNA replication, and modification of various cellular processes.[review] PMID: 24923176
  30. E8;E2C repressor limits viral transcription and replication throughout the complete life cycle of HPV16. PMID: 24198405
  31. APOBEC3 upregulated by IFN-beta induce E2 hypermutation of HPV16 in cervical keratinocytes. PMID: 24227842
  32. HPV 16 E2 induces apoptosis by silencing the gC1qR gene or inhibiting p38 MAPK/JNK signalling in cervical squamous cell carcinoma PMID: 23651874
  33. Transactivation by E2 proteins was less cell-type dependent but differed in an HPV-type-dependent manner. PMID: 23407419
  34. 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
  35. An interaction between human papillomavirus 16 E2 and TopBP1 is required for optimum viral DNA replication and episomal genome establishment. PMID: 22973044
  36. The present work provides an overview of E2 biological functions across multiple HPV genotypes. PMID: 22761572
  37. Three new sequence variations were identified at positions 2791, 2823 and 3361 in E2 of HPV16 isolated form women in Greece. PMID: 22294445
  38. NRIP enhances HPV 16 gene expression via interaction with either GR or viral E2. PMID: 22177699
  39. 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
  40. Data indicate that the enhanced E2R showed greater repression of transcription from E2-responsive reporter plasmids in mammalian cell culture. PMID: 21482558
  41. 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
  42. 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
  43. The expression of all E8wedgeE2C proteins inhibited the growth of HeLa cells. PMID: 21191025
  44. E2 protein from HPV16 activated MMP9 promoter predominantly via the MEK1-ERK1/2-AP-1 signaling pathway. PMID: 20596661
  45. 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
  46. 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
  47. Recognition of DNA by E2 regulatory protein was determined to a DNA target containing the spacer sequence TATA. PMID: 20185566
  48. 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
  49. L2 selectively inhibits the transcriptional activation property of E2 and that there is a direct interaction between the two proteins PMID: 15681049
  50. NMR structure of the HPV-16 E2 DNA binding domain PMID: 15702528

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Subcellular Location
Host nucleus.
Protein Families
Papillomaviridae E2 protein family
Database Links

KEGG: vg:1489080

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