Recombinant Human Papillomavirus Type 16 Probable Protein E5 (E5) Protein (His&GST)

Name: Recombinant Human Papillomavirus Type 16 Probable Protein E5 (E5) Protein (His&GST)
Brand: Beta LifeScience
SKU: BLC-06499P
Price: 2236.0 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Papillomavirus Type 16 Probable Protein E5 (E5) Protein (His&GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P06927
Target Symbol	E5
Species	Human papillomavirus type 16
Expression System	in vitro E.coli expression system
Tag	N-10His&C-GST
Target Protein Sequence	MTNLDTASTTLLACFLLCFCVLLCVCLLIRPLLLSVSTYTSLIILVLLLWITAASAFRCFIVYIIFVYIPLFLIHTHARFLIT
Expression Range	1-83aa
Protein Length	Full Length
Mol. Weight	36.4 kDa
Research Area	Others
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	Acts to keep host cells in a proliferation-competent state upon differentiation. Enhances host epidermal growth factor receptor (EGFR) activation after stimulation by EGF by inhibiting EGFR internalization. Induces a redistribution of host caveolin-1 and glycosphingolipid (ganglioside GM1) components of lipid rafts to the plasma membrane. Since GM1s inhibit cytotoxic T-lymphocytes, block immune synapse formation, and enhance proliferative signaling by the EGFR, E5 may enhance immune evasion and cell proliferation via a common mechanism. E5 also alters endosomal pH by interacting with the vacuolar H+-ATPase, which is a proton pump responsible for acidifying cellular organelles. Additionally, E5 prevents transport of the major histocompatibility class I to the cell surface and retains the complex in the Golgi apparatus.
Subcellular Location	Host membrane; Multi-pass membrane protein. Host endoplasmic reticulum membrane. Host Golgi apparatus.
Protein Families	Papillomaviridae E5 protein family
Database References	KEGG: vg:1489077

Gene Functions References

HPV16 E5 is produced from an HPV16 early mRNA spliced from SD226 to SA3358. PMID: 29155138
findings show Human papillomavirus type 16 oncogene E5 is primarily responsible for Met upregulation; E5-induced Met contributes motility of HPV-containing cells; these studies show a new role for E5 in epithelial-stromal interactions, with implications for cancer development PMID: 29609071
A transcriptional crosstalk among 16E5 and KGFR might be the crucial molecular driver of epithelial deregulation during early steps of HPV infection and transformation. PMID: 25826082
HPV16 early gene E5 specifically down-regulated miRNA196a in the cervical cancer cell lines. PMID: 25563170
Results show that HPV16 E5 down-modulates FGFR2b and induces FGFR2c expression in human keratinocytes and cervical epithelial cells through down-modulation of ESRPs. PMID: 25450802
Graphene nanoribbons elicit cell specific uptake and delivery via activation of epidermal growth factor receptor enhanced by human papillomavirus E5 protein. PMID: 24980059
Data indicate HPV16 E5 as a possible target on the therapeutic strategies about cervical cancer. PMID: 24142729
Human papillomavirus E5 oncoproteins bind the A4 in endoplasmic reticulum to regulate proliferative ability upon differentiation. PMID: 24606699
This review attempts to discuss the positive role of HPV16 E5 in the form of therapeutic target for cervical cancer. PMID: 22262402
No firm conclusion could be drawn about the correlation between the E5 expression and the disease progression in patients with squamous intra-epithelial lesions of the cervix. PMID: 21767984
Both the annexin A2 and p11 subunits of calpactin I coimmunoprecipitate with human papillomavirus type 16 E5 in COS cells and in human epithelial cell lines, and an intact E5 C terminus is required for binding. PMID: 21849434
HPV infection and subsequent transformation take place through complex regulatory patterns of gene expression in the host cells, part of which are regulated by the E5 protein PMID: 21747943
The authors show that the human papillomavirus type 16 E5 protein expression per se stimulates IFN-beta expression this stimulation is specifically mediated by the induction of interferon regulatory factor 1. PMID: 21389130
16E5 alters EGF endocytic trafficking via a pH-independent inhibition of vesicle fusion. PMID: 20686024
CD1d is downregulated by the HPV16 E5 and HPV6 E5 protein. PMID: 20810727
these data indicate that E5 represses the cellular endoplasmic reticulum stress response and suggest a potential role for E5 during productive HPV infection. PMID: 20688044
The authors show that the human papillomavirus 16 E5 protein-induced reduction of HLA-A2 has a functional impact by reducing recognition of E5 expressing cells by human papillomavirus specific CD8+ T cells. PMID: 20813390
HPV16 E5 produces polyploid cells and enlarged nucleic by endoreplication. These findings provide insight into how HPV16 E5 can contribute to cell transformation. PMID: 20605566
4075T is highly conserved in E5 of human papillomavirus type 16 isolated from Asia. PMID: 20718354
HPV-16 E5 impaired the viability of trophoblastic and cervical cell lines. E5 & E6/E7 increase chemotaxic & invasive properties of trophoblastic cells. HPV-16 E5 participated, with E6 & E7, in these changes by impairing E-cadherin expression. PMID: 19917629
HPV 16 E5 protein contributes to cervical carcinogenesis by inhibiting apoptosis of transformed cervical epithelial cells. PMID: 20015862
E5 and the EGF-receptor cooperate to enhance cell cycle entry and progression through regulating p27(Kip1) expression at protein level. PMID: 20144468
topology findings are compatible with a model of E5 being a 3-pass transmembrane protein and with studies demonstrating its C terminus interacting with cytoplasmic proteins PMID: 19955310
The first hydrophobic domain of E5 is required for invasion of cell matrix. PMID: 19812262
functions of E5 protein are not mediated by morphological alterations in the actin cytoskeleton, microtubulus network or adhesion to the extrcellular matrix; colocalization E5 with the Bcl-2 antiapoptotic protein on intracellular membranes was established PMID: 15593417
-16 E5 protein can form a complex with ErbB4 via binding to the extracellular and transmembrane domains of ErbB4 (JM-b/CYT-1). PMID: 16819515
E5 can interfere with antigen presentation by most, if not all, classical HLA I haplotypes. PMID: 16823848
Increases cell membrane expression of caveolin-1, induces a 23- to 40-fold increase in lipid raft component ganglioside GM1 at the cell membrane of E5-expressing uterine cervical cells, and mediates a dramatic increase in caveolin-1/GM1 association. PMID: 17704805
HPV-16 E5 protein binds to karyopherin beta3. PMID: 18455505
Results identify B-cell-associated protein 31 as a novel binding partner of the high-risk human papillomavirus 16 E5 proteins and provide insight into how the E5 proteins may modulate the life cycle in differentiating cells. PMID: 18684816
Using biochemical and cell biological assays to better understand HPV16 E5, the authors find that HPV16 E5 localizes to the plasma membrane with an intracellular amino terminus and an extracellular carboxyl-terminus. PMID: 19712955

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.