Recombinant Human Papillomavirus Type 16 Protein E6 (E6) Protein (His&His)

Name: Recombinant Human Papillomavirus Type 16 Protein E6 (E6) Protein (His&His)
Brand: Beta LifeScience
SKU: BLC-00940P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Featured viral antigens molecules, Hpv, Recombinant proteins, Recombinant proteins fall special offers - full-length proteins, Viral antigen

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 Human Papillomavirus Type 16 Protein E6 (E6) Protein (His&His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P03126
Target Symbol	E6
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His&C-6His
Target Protein Sequence	MHQKRTAMFQDPQERPRKLPQLCTELQTTIHDIILECVYCKQQLLRREVYDFAFRDLCIVYRDGNPYAVCDKCLKFYSKISEYRHYCYSLYGTTLEQQYNKPLCDLLIRCINCQKPLCPEEKQRHLDKKQRFHNIRGRWTGRCMSCCRSSRTRRETQL
Expression Range	1-158aa
Protein Length	Full Length
Mol. Weight	24.5 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 major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including BAK1, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway.
Subcellular Location	Host cytoplasm. Host nucleus.
Protein Families	Papillomaviridae E6 protein family
Database References	KEGG: vg:1489078

Gene Functions References

USP15 could increase the level of HPV16 E6 by inhibiting E6 degradation. PMID: 29895155
Up-regulation of miR-20a by HPV16 E6 exerted growth-promoting effects by targeting PDCD6 in cervical carcinoma cells. PMID: 29710555
The HPV16-E6 oncoprotein induces EMT in transgenic mice cataracts. The molecular mechanism may involve TGF-beta and Wnt/beta-catenin pathways, suggesting that the K14E6 transgenic mouse could be a useful model for the study or treatment of EMT-induced cataracts. PMID: 29888254
This study provides links between the DNA damage response, the regulation of E6 human papillomavirus type 16 PDZ binding motif function, and the inhibition of p53 activity and begins to explain how virus-infected cells remain within the cell cycle, despite activation of DNA damage response pathways during productive virus infections. PMID: 29848585
E6 oncogene alters host gene expression in the cervical stroma. PMID: 29073104
the K14E6 versus K14E6Delta146-151 transcriptional profile provides a source of valuable data to uncover novel E6 functions in the skin. PMID: 29130045
HPV16 E6 T178G mutation increases the disease risk of cervical intraepithelial neoplasia 2 and 3 PMID: 29787003
the network of transcriptional interactions in HPV16-infected basal-type cervical epithelium is regulated in a concentration-dependent manner by E6/E7, via a limited number of central master-regulators. PMID: 27457222
E6 association with cellular PDZ proteins promotes the nuclear localization of YAP1. PMID: 29346075
Results showed that increased expression of HPV16 E6 expression level was strongly associated with malignant transformation of the cervical epithelium and the histological progression of cervical squamous cell carcinoma. PMID: 29470526
human papillomavirus 16 E6, E7 genes and Long Control Region are expressed in cervical samples from Uruguayan women PMID: 29454092
HPV16 E6 oncoprotein promoted the bioactivities of non-small cell lung cancer (NSCLC) cells. TLR3-Src signaling pathway might be involved in this procession by up-regulation of cytokine production. The interaction between HPV16 E6 protein and TLR3 might contribute to the poor prognosis of NSCLC. PMID: 28480962
HPV16 E6-E7 promotes cancer stem-like cells phenotype in esophageal squamous cell carcinoma cells through the activation of PI3K/Akt signaling pathway PMID: 27489353
Studied role of HPV16 E6 and COX-2 in invasive ductal breast cancer using qPCR and IHC, and in vitro studies. Found HPV16 E6 promoted breast cancer proliferation; Cox-2 inhibition suppressed HPV16 E6 effects on proliferation thru NF-kappaB signaling pathway. PMID: 29250535
Findings indicate O-linked N-acetylglucosamine transferase (OGT) as a cellular factor involved in human papillomaviruses type 16/18 E6 and E7 expressions and cervical cancer tumorigenesis, suggesting that targeting OGT in cervical cancer may have potential therapeutic benefit. PMID: 27331873
IFN-beta treatment leads to p53-indipendent apoptosis in K16 cells whereas induces senescence in K16 cells if E6 is silenced and p53 expression is restored. The levels of selected miRNAs, deregulated in K16 and K38 cells, can be modulated by IFN-beta when E6 and E7 proteins of HPV-16, but not HPV-38, are expressed. PMID: 26748726
A decrease in miR-184 level by E6 oncoprotein may predict unfavorable response to cisplatin-based chemotherapy in HPV-infected non-small cell lung carcinoma patients via increasing Bcl-2 expression. PMID: 27083050
Seminal studies over the last two decades have identified the transcriptional, epigenetic, and post-transcriptional roles high-risk E6 and E7 have in TERT regulation. (Review) PMID: 27863966
Ablation of E6 by siRNA induces the tumor suppressor p53 and diminishes beta-defensin-3 (hBD3) in HPV-16 positive CaSki cervical cancer cells and UM-SCC-104 head and neck cancer cells. PMID: 27034006
This study identifies NFX1-123 as a critical host protein partner through which 16E6 is able to subvert the immune response and in turn permit a long-lived high-risk Human papillomavirus infection. PMID: 29117186
HPV E6 is capable of overriding this regulation and can promote degradation of p53 and Dlg regardless of the phosphorylation status of E6AP. PMID: 28835500
Studies indicate the accuracy of HPV16 antibodies to the oncoproteins E6. PMID: 28316084
Lactate and glucose production were enhanced in E6-transduced keratinocytes, likely due to raised levels of metabolic enzymes, but independent of(HIF-1alpha activity. PMID: 28857035
These data highlight the importance of the carboxy-terminal motif of the E6 protein and downregulation of PAR3 in tumorigenic transformation of human cervical keratinocytes. PMID: 28440909
Study presented a combined molecular dynamics/infrared spectroscopy approach to the study of ligand binding (11-residue peptide derived from the C terminus of HPV16 E6) by the PDZ1 domain of MAGI1, focusing in particular on the far-infrared region of the spectrum. PMID: 28636914
HPV16 E6/E7 oncogene expression in primary human epithelial cells alters miR expression in extracellular vesicles. PMID: 28500882
In three warty or basaloid SCSC HPV16-DNA and E6*I-mRNA were detected. LCM-PCR confirmed HPV16 was in p16(INK4a)-positive malignant cells. However, of three usual-type SCSC, all were HPV-negative and two expressed p53 protein but not p16(INK4a). PMID: 28376081
HPV-16 E6 was confirmed to regulate microRNA miR-23b indirectly through the DNA methylation of host gene C9orf3 and thus induce c-MET and inhibit apoptosis in cervical cancer cells. PMID: 28077801
Our results indicate that HPV16 E6/E7 indirectly upregulated the expression of VEGF by inhibition of liver kinase B1 expression and upregulation of hypoxia-inducible factor 2alpha expression,thus propose a human papillomavirus-liver kinase B1-hypoxia-inducible factor 2A-vascular endothelial growth factor axis for the tumorigenesis of lung cancer PMID: 28720067
HPV E6/E7 increased expression of DROSHA and DICER mRNA and protein in cervical carcinoma cells. PMID: 28448850
Data show that p63 transcription factors modulate cell migration via Src-focal adhesion kinase (FAK) signaling in foreskin keratinocytes (HFK) expressing human papilloma virus (HPV)16 E6/E7 genes. PMID: 26001294
Overall, this study supports the model that perturbation of cellular miR expression by human papillomavirus type 16 E6/E7 importantly contributes to the rewiring of cellular regulatory circuits that contributes to oncogenic transformation. PMID: 28049151
Thus, Brd4 activates human papillomavirus 16 transcription at this integration site, and strong selection for E6/E7 expression can drive the formation of a super-enhancer-like element to promote oncogenesis. PMID: 27624132
Collectively, these results indicate that human papillomavirus 16 E6 induces upregulation of APOBEC3B through increased levels of TEADs, highlighting the importance of the TEAD-APOBEC3B axis in carcinogenesis. PMID: 28077648
A transcriptomic landscape of human papillomavirus 16 E6-regulated gene expression and splicing events in cervical cancer patients has been presented. PMID: 27859058
The ubiquitylation of beta-catenin by E6AP was dependent on its E3 ubiquitin ligase activity, but it was proteasome-independent and did not require HPV16-E6. PMID: 27902311
nucleotide changes in E6 occur significantly more often in the mixed form of viral DNA and in low-grade squamous intraepithelial lesions; and the variants without additional mutations may promote integration of HPV16 genome. PMID: 27801430
We also found VPA suppressed oncogene E6 in a Notch-independent manner, and induced significant apoptosis in E6-overexpressing HPV positive CaSki cells. PMID: 27176495
Data show that alpha-linolenic acid (ALA) decreased the expression of VEGF and COX2 proteins, and reduced the expression of Human papillomavirus type 16/18 onco-proteins E6 and E7, resulting into restoration of expression of tumor suppressor proteins, p53 and Rb in cervical cancer cell lines. PMID: 26440049
Expression changes of E6 and E7 significantly promoted the protein expression of HIF-1alpha, the expression of both protein and mRNA of GLUT1, but had no effect on the expression of HIF-1alpha mRNA in lung cancer cells. PMID: 26508030
our results suggest that ERK1/2 signaling pathway is involved in HPV-16 E6 but not E7 oncoprotein-induced HIF-1a, VEGF, and IL-8 expression in NSCLC cells, leading to the enhanced angiogenesis in vitro. PMID: 26931433
Our data suggest that the use of HPV 16 spliced transcripts may help to predict for poorer outcomes in patients with HPV positive oropharyngeal cancer PMID: 26575468
Within the limitations of this study, the immunoexpression of HPV 16/18 E6 and E7 oncoproteins may have prognostic value regarding cervical squamous intraepithelial lesions persistence in HIV-positive women. PMID: 26909984
HPV16 E6/E7 Oncoproteins Alter the In Vitro Growth of CD44+NGFR+ Human Tonsillar Epithelial Cells. PMID: 26527383
Human papillomavirus type 16 E6 protein, a major etiological molecule of cervical cancer, maintains high YAP protein levels in cervical cancer cells by preventing proteasome-dependent YAP degradation to drive cervical cancer cell proliferation. PMID: 26417066
E6 and E7 have roles in methylation of tumor suppressor genes and inducing phenotype transformation of human cervical carcinoma cells PMID: 26329329
Here we demonstrate that E7, and to a lesser extend E6, strongly reduce NFkappaB activation in response to the inflammatory mediator imiquimod. Moreover, we establish that undifferentiated keratinocytes do not express the putative receptor for imiquimod, TLR7 PMID: 26268216
The data indicate for the first time that increased cytoplasmic human papillomavirus type 16 E6 levels associated with malignant progression alter Cx43 trafficking and recycling to the membrane and the E6/human Dlg interaction may be involved. PMID: 26445057
High-risk HPV-type lesions might inhibit the chemokine CCL20 on Langerhans cells through E6 and E7 to escape the immune response. PMID: 26400278
E6 protein functioning as a host miRna modulator and play a role of HPV induced carcinogenesis in patient diagnosed with cervical cancer. PMID: 26384051

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.