Protein E7, HPV16 (His)

HPV16 E7 is a viral phosphoprotein with oncogenic activity, belonging to the human papillomavirus early protein family. HPV16 E7 activates the cell cycle by releasing E2F through proteasome degradation of pRB. HPV16 E7 can cooperate with E6 to immortalize cells and neutralize the toxicity of E5, while activating the AP-1/NF-κB pathway and downregulating E-cadherin to enhance migration and invasion, making it a core target for cervical cancer. Protein E7, HPV (His) is a recombinant HPV E7 protein expressed from E. coli with an N-6*His tag.

HPV16 E7 is a multifunctional nuclear phosphoprotein and a key oncoprotein in HPV16 carcinogenesis. It belongs to the human papillomavirus early protein family. The C-terminal half of HPV16 E7 contains two conserved Cys-X-X-Cys motifs, which can reversibly bind Zn²⁺ and Cd²⁺, significantly increase the α-helical content, and stabilize the hydrophobic core of the protein. The amino terminus of HPV16 E7 has sequence similarity with the adenovirus E1A protein and functional commonality with the SV40 large T antigen.
HPV16 E7 binds to the retinoblastoma protein (pRB) with high affinity, promotes its degradation through the proteasome pathway, and releases the transcription factor E2F to activate cell cycle progression. HPV16 E7 cooperates with the Ras oncogene to transform primary rodent cells. HPV16 E7 synergizes with E6 to immortalize primary human keratinocytes and neutralizes the cytotoxic effects of E5.
HPV16 E7 downregulates E-cadherin expression and enhances cell migration and invasion by activating AP-1 and NF-κB pathways. HPV16 E7 also disrupts cell adhesion and promotes epithelial-mesenchymal transition by interfering with cell-cell junctions and cytoskeletal rearrangement. Upstream regulatory factors of HPV16 E7 include viral promoters (such as LCR); downstream targets include pRB, E2F, p16 and E-cadherin, which can affect cell cycle control and adhesion molecule expression.
HPV16 E7 can be used to study the mechanism of action of cervical cancer development. The full-length E7 protein or E7 display vector (such as Lactobacillus casei) induces specific anti-tumor immunity in animal models such as TC-1 mice, inhibits tumor growth and improves survival rate. HPV16 E7 is the main target of HPV-related cancer therapeutic vaccines.

Measured by its binding ability in a functional ELISA. Immobilized Protein E7 at 10 μg/mL (100 μL/well) can bind Biotinylated MYC. The ED₅₀ for this effect is ≤0.3071 μg/mL.

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  Measured by its binding ability in a functional ELISA. Immobilized Protein E7 at 10 μg/mL (100 μL/well) can bind Biotinylated MYC. The ED₅₀ for this effect is 0.2398 μg/mL, corresponding to a specific activity is 4.17×10³ Unit/mg.

Virus

E. coli

N-6*His

P03129 (M1-P98)

1489079  [NCBI]

Full Length

MHGDTPTLHEYMLDLQPETTDLYCYEQLNDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPICSQKP

Approximately 18-21 kDa

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  Greater than 94% as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from 0.2 μm filtered solution in 20 mM Tris-HCL, 0.5 M NaCl, 6% Trehalose, pH 8.0 or 50 mM Tris-HCL, 300 mM NaCl, pH 7.4 or PBS, 6% Trehalose, pH 7.4 or 50 mM Tris-HCL, 200 mM NaCl, pH 8.0 or 50 mM Tris-HCL, 300 mM NaCl, pH 7.4, 8% trehalose.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Pahel G, et al. Structural and functional characterization of the HPV16 E7 protein expressed in bacteria. J Biol Chem. 1993 Dec 5;268(34):26018-25.  [Content Brief]

  [2]. Boulenouar S, et al. Effects of HPV-16 E5, E6 and E7 proteins on survival, adhesion, migration and invasion of trophoblastic cells. Carcinogenesis. 2010 Mar;31(3):473-80.  [Content Brief]

  [3]. Li YL, et al. Vaccination of full-length HPV16 E6 or E7 protein inhibits the growth of HPV16 associated tumors. Oncol Rep. 2010 Nov;24(5):1323-9.  [Content Brief]

  [4]. Poo H, et al. Oral administration of human papillomavirus type 16 E7 displayed on Lactobacillus casei induces E7-specific antitumor effects in C57/BL6 mice. Int J Cancer. 2006 Oct 1;119(7):1702-9.  [Content Brief]