Recombinant Human papillomavirus type 16 Protein E7 (E7)

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Code CSB-EP365855HML
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP365855HML could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) E7.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP365855HML could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) E7.
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Product Details

Greater than 90% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Epigenetics and Nuclear Signaling
Alternative Names
E7; Protein E7
Human papillomavirus type 16
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
15.0 kDa
Protein Length
Full Length
Tag Info
N-terminal 6xHis-tagged
Liquid or 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.
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
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°C/-80°C. 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
3-7 business days
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

Protein E7 is a crucial oncoprotein found in high-risk human papillomavirus (HPV) types, such as HPV-16. E7 is a small phosphoprotein that interacts with various cellular proteins to promote cellular transformation. It shares sequence homology with adenovirus E1a protein and simian virus 40 large T antigen [1]. E7 exerts its functions by primarily interacting with the retinoblastoma protein (pRB) and other cellular targets, leading to the inactivation of Rb-related proteins p107 and p130 [2][3]. This inactivation of Rb family proteins by E7 disrupts the normal cell cycle regulation, allowing for uncontrolled cell proliferation [4].

E7 is considered the major transforming protein among HPV oncoproteins and is structurally and functionally similar to adenovirus E1A and SV40 Large T antigen [5]. It binds and destabilizes pRB, p107, and p130, inhibiting their tumor-suppressive functions and promoting cell cycle progression [6]. E7 contains conserved regions, including CR1 at the N-terminal end, CR2 with the LxCxE motif, and CR3 at the C-terminal end, which are crucial for its interactions with molecular targets [7][8].

Moreover, E7 binds to specific domains in the Rb protein, namely RbAB and RbC domains, further interfering with Rb's tumor-suppressive activities [9]. The interaction of E7 with pRB is essential for overcoming cell cycle arrest and promoting cell proliferation [6]. Additionally, E7 can induce abnormal centrosome duplication independently of Rb inactivation, further contributing to its oncogenic potential [4].

[1] N. Gammoh, H. Grm, P. Massimi, & L. Banks, "Regulation of human papillomavirus type 16 e7 activity through direct protein interaction with the e2 transcriptional activator", Journal of Virology, vol. 80, no. 4, p. 1787-1797, 2006.
[2] A. Helt and D. Galloway, "Destabilization of the retinoblastoma tumor suppressor by human papillomavirus type 16 e7 is not sufficient to overcome cell cycle arrest in human keratinocytes", Journal of Virology, vol. 75, no. 15, p. 6737-6747, 2001.
[3] A. Hall and K. Alexander, "Rna interference of human papillomavirus type 18 e6 and e7 induces senescence in hela cells", Journal of Virology, vol. 77, no. 10, p. 6066-6069, 2003.
[4] S. Duensing and K. Münger, "Human papillomavirus type 16 e7 oncoprotein can induce abnormal centrosome duplication through a mechanism independent of inactivation of retinoblastoma protein family members", Journal of Virology, vol. 77, no. 22, p. 12331-12335, 2003.
[5] T. Prathapam, C. Kühne, & L. Banks, "The hpv-16 e7 oncoprotein binds skip and suppresses its transcriptional activity", Oncogene, vol. 20, no. 52, p. 7677-7685, 2001.
[6] M. Giarrè, S. Caldeira, I. Malanchi, F. Ciccolini, M. Leão, & M. Tommasino, "Induction of prb degradation by the human papillomavirus type 16 e7 protein is essential to efficiently overcome p16 ink4a-imposed g1 cell cycle arrest", Journal of Virology, vol. 75, no. 10, p. 4705-4712, 2001.
[7] H. Yun, M. Kim, H. Lee, W. Kim, J. Shin, H. Kimet al., "Structural basis for recognition of the tumor suppressor protein ptpn14 by the oncoprotein e7 of human papillomavirus", Plos Biology, vol. 17, no. 7, p. e3000367, 2019.
[8] C. Bello-Rios, S. Montaño, O. Garibay-Cerdenares, L. Araujo-Arcos, M. Leyva-Vázquez, & B. Illades-Aguiar, "Modeling and molecular dynamics of the 3d structure of the hpv16 e7 protein and its variants",, 2020.
[9] L. Chemes, I. Sánchez, C. Smal, & G. Prat‐Gay, "Targeting mechanism of the retinoblastoma tumor suppressor by a prototypical viral oncoprotein", Febs Journal, vol. 277, no. 4, p. 973-988, 2010.

Customer Reviews and Q&A

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Would you have the recipe for the Tris buffer that you could share? If not, the recipe can you share the molarity and the pH of the Tris buffer?

Thanks for your inquiry. The buffer composition is as follows: 20mM Tris-HCl, 0.5M NaCl, pH 8.0, 50% glycerol.

I'm wondering exactly how to resuspend the protein.
You mentioned the instructions as the following:
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%.
I could use it as reference.
But I ordered 0.02mg, if I wanted to reconstitute to 1mg/mL, I would add 20ug sterile water, right?
If I plan to store the protein with 50% glycerol, would I actually resuspend with 10uL sterile water, and 10uL glycerol (for the 1mg/mL concentration?


If you want to get the protein with the final concentration of 0.1 mg/ml, you can refer to the following methods for reconstitution.
Reconstitute the protein completely with 100ul sterile water, and then add 100ul glycerol solution, with the final protein concentration of 0.1mg/ml.
The protein contains 50% glycerol and can be stored at -20℃/-80℃ for a long time.


Please address the final endotoxin level after producing. We like to know EU/ug.


We can provide free endotoxin removal service and guarantee endotoxin level within 0.1 EU/ug (1EU / ug).

Target Background

Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Plays also a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
Gene References into Functions
  1. A role for E7 protein in regulation of Langerhans cells homeostasis in the skin and in suppression of antigen specific CD8 T cell expansion. PMID: 27708419
  2. E7 oncogene alters host gene expression in the cervical stroma. PMID: 29073104
  3. direct evidence that both A3A and HPV16 E7 interact with CUL2, suggesting that the E7-CUL2 complex formed during HPV infection may regulate A3A protein levels in the cell. PMID: 29367246
  4. Results suggest that E7 recruited CUL2, driven by CUL2/E2F1/miR-424 regulatory loop, is overexpressed and accelerates HPV16-induced cervical carcinogenesis. PMID: 27153550
  5. The human papillomavirus E7 oncoprotein is a regulator of host transcription. (Review) PMID: 27818212
  6. Findings indicate the interaction network of viral oncogene HPV16 E7, miR-27b and PLK2, and support the potential strategies using antisense nucleic acid of miR-27b for therapy of cervical cancer. PMID: 26910911
  7. Based on experimental data obtained from E7 proteins from the prototypical viral types 16, 18 and 11, we identified a couple of low pKa nucleophilic cysteines that can form a disulfide bridge upon the exposure to ROS and regulate the cytoplasm to nucleus transport PMID: 27863297
  8. E7 is major transforming oncoprotein of human papillomavirus 16 and serves as paradigmatic example of intrinsically disordered proteins due to its N-terminal disordered domain. Data suggest mutation of leucines in N-terminal intrinsically disordered domain of E7 leads to pronounced increase in both alpha-helix and beta-sheet structures; thus, E7 appears to exhibit local structural elements that oppose canonical folding. PMID: 28952717
  9. Authors observed thousands of unique HPV16 genomes; very few women shared the identical HPV16 sequence, however, E7 was devoid of variants in precancers/cancers compared to higher levels in the controls; this was confirmed in cancers from around the world. Strict conservation of the 98 amino acids of E7, which disrupts Rb function, is critical for HPV16 carcinogenesis. PMID: 28886384
  10. study determined that high-risk E7 proteins target the proteolysis of the cellular protein tyrosine phosphatase PTPN14 and find that this activity is correlated with the retinoblastoma-independent transforming activity of E7 PMID: 27651363
  11. Increased phosphorylation of the N29S of E7 increases interaction with TBP and pRb and viral transforming activity. PMID: 27829177
  12. HPV16 E7 oncoprotein upregulates Oct3/4, Sox2, Nanog and Fgf4 expression to maintain the self-renewal capacity of cancer stem cells. PMID: 27693927
  13. result indicates that cervical cancers do not require the continuous expression of E7 on the Fanconi anemia pathway-deficient background PMID: 27190216
  14. the level of Cdc6 phosphorylation at serine 54 (S54P) was increased in E7-expressing cells. S54P was associated with an increase in the total amount of Cdc6 and chromatin-bound Cdc6. DNA damage-enhanced upregulation and chromatin binding of Cdc6 appeared to be due to downregulation of cyclin-dependent kinase 1 (Cdk1) as Cdk1 knockdown increased Cdc6 levels PMID: 27207654
  15. PTPN14 is classified as a potential tumor suppressor protein, and is very susceptible to HPV E7-induced proteasome-mediated degradation. PMID: 28100625
  16. study found that HPV-16 decreased the phosphorylation of AKT (pAKT) and that this is a function of E7 that is independent of the Rb degradation function PMID: 27030265
  17. These data suggest that the HPV16 E7 oncoprotein impairs the function and morphology of dendritic cells and induces the systemic accumulation of CD11b(+)Gr1(+) cells. PMID: 27478837
  18. the structural features of the flexible N-terminal region (46 residues) of E7, were investigated. PMID: 27418281
  19. The human papillomavirus type 16 oncogene E7 may affect STK31 expression through a DNA methylation-mediated mechanism. PMID: 27044426
  20. HPV16 E7 protein can up-regulate host miR-21 expression, thus elevating cervical carcinoma cell growth, proliferation and invasion. PMID: 26884851
  21. These data suggest that local expression of HPV16-E7 in keratinocytes can contribute to persisting infection with this oncogenic virus, by altering the phenotype and function of local APCs. PMID: 27031095
  22. Results found that HPV16 E7 increases RARB mRNA and protein expression both in vitro and in the cervix of young K14E7 transgenic mice suggesting that RARB overexpression is part of the early molecular events induced by the E7 oncoprotein. PMID: 26173416
  23. E7 localised to the plasma membrane in cervical cancer cells. PMID: 26131956
  24. findings suggest that increased IL-17A expression by macrophages in E7-expressing skin exposed to DNCB promotes arginase-1 induction and contributes directly to the observed hyperinflammation. PMID: 25720383
  25. the modulation of HPV-16 E6/E7 expression remarkably influenced cell proliferation, migration, and invasion, as well as the protein levels of E-cadherin and P-cadherin in cervical cell lines. PMID: 26093522
  26. The data showed that E7 induced CCNA1 methylation by forming a complex with Dnmt1 at the CCNA1 promoter, resulting in the subsequent reduction of expression in cancers. PMID: 26250467
  27. In 10 microg/ml BV-treated CaSki cells, the mRNA expression and protein levels of HPV16 E7 were significantly decreased. The mRNA and protein expression levels of HPV16 E7 were decreased by bee venom in TC-1 tumors. PMID: 25633640
  28. that mast cells, recruited towards CCL2 and CCL5 expressed by epithelium induced to proliferate by Human Papillomavirus 16 E7 protein PMID: 25340820
  29. These results point to a mutually functional interaction between p14ARF and E7 that might partly explain why the sustained p14ARF expression observed in most cervical pre-malignant lesions and malignancies may be ineffective. PMID: 24798431
  30. In genetically engineered mouse models expressing HPV16 oncogenes in stratified squamous epithelia, HPV16 E7, alone or together with E6, led to an accumulation of epithelial cells harboring gamma-H2AX nuclear foci. PMID: 25216575
  31. Data indicate that HPV16E7, CBP/p300, and retinoblastoma protein pRb interactions are potentially important for cellular transformation. PMID: 25451029
  32. Our results demonstrate that HPV16.E7 protein enhances drug associated production of arginase-1 by myeloid cells and consequent inflammatory cellular infiltration of skin. PMID: 24732401
  33. The aim of the present study was to investigate the cytotoxicity of natural killer (NK) cells to CaSki cells following knockdown of the E7 protein of the human papillomavirus type 16. PMID: 24566606
  34. Results show that E7 interacts with the B-Myb, FoxM1 and LIN9 components of this activator complex, leading to cooperative transcriptional activation of mitotic genes in primary cells and E7 recruitment to the corresponding promoters. PMID: 24141769
  35. E7 induces cancer by causing DNA damage at least in part through the inactivation of pocket proteins. PMID: 24013229
  36. E7 induces human papillomavirus-associated head and neck cancers by promoting DNA damage through the inactivation of pocket proteins. PMID: 24086435
  37. HPV16 E7 oncoprotein increases production of the IL18BP in keratinocytes. PMID: 24478434
  38. The seven cysteines in HPV16 E7 remain reduced in conditions resembling the basal reduced state of a cell. PMID: 24559112
  39. This study demonstrates that the cdk inhibitor p16INK4A is required for high-level expression of the E7 oncoproteins of HPV-16, HPV-18, and HPV-45 in cervical carcinoma cells. PMID: 24599991
  40. These data suggest that the interaction of human papillomavirus E7 with p190 dysregulates this GTPase activating protein and alters the actin cytoskeleton. PMID: 24403595
  41. Matrix metalloproteinases (MMP)--MMP-1,-2,-9 and its endogenous activity regulators in transformed by E7 oncogene HPV16 and HPV18 cervical carcinoma cell lines PMID: 24479343
  42. E7 proteins of different types of human papillomaviruses disrupted pocket protein-DREAM complexes in a similar extent. PMID: 24294959
  43. hTERT cooperates with HPV16 E7 protein in mediating bypass of the senescence blockade and effecting cell immortalization PMID: 23592995
  44. Human papillomavirus type 16 E7 expression causes increased EMI1 mRNA expression and also inhibits EMI1 degradation. PMID: 24074588
  45. that a patch of hydrophobic residues, 65LRLCV69, within the zinc-binding domain of HPV16 E7 mediates its nuclear import via hydrophobic interactions with the FG domain of the central channel nucleoporin Nup62. PMID: 24074597
  46. HPV16-induced TLR9 down-regulation affects the interferon response which negatively regulates viral infection PMID: 23752229
  47. Authors investigated the effect of E7 on the late promoter and found that E7 was able to activate the promoter. PMID: 23725693
  48. expression of a single oncoprotein in the epidermis is sufficient for lymphocyte trafficking (including immunosuppressive lymphocytes) to premalignant skin PMID: 23469070
  49. Human papillomavirus 16 E7 Adenine647Guanine can be used as a candidate marker for the progression of the cervical neoplasia. PMID: 21535311
  50. These results demonstrate an important role for Cdt1 in human papillomavirus E7-induced rereplication and shed light on mechanisms by which human papillomavirus induces genomic instability. PMID: 23152514

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Subcellular Location
Host cytoplasm. Host nucleus.
Protein Families
Papillomaviridae E7 protein family
Database Links

KEGG: vg:1489079

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