Human Papilloma Virus type 33 (HPV 33) L1 protein (VLP)

Human Papilloma Virus type 33 (HPV 33) L1 protein (VLP): Product Information

Purity
> 95 % as determined by SDS-PAGE.
Endotoxin
< 0.01 EU per μg of the protein as determined by the LAL method
Activity
Testing in progress
Expressed Host
Baculovirus-Insect Cells
Species
HPV
Molecule Mass
The recombinant HPV 33 L1 consists of 499 amino acids and predicts a molecular mass of 56 kDa.
Formulation
Sterile 20 mM His, 0.5 M NaCl, pH 6.2, formaldehyde (≤ 40 μg/mL).
Please contact us for any concerns or special requirements.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

Human Papilloma Virus type 33 (HPV 33) L1 protein (VLP): Images

SDS-PAGE before formaldehyde cross-linking

HPV capsid L1 Background Information

Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminata to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so called capsomeres, to form particles which are immunologically indistinguishable from native virions. Experimentally induced VLP antisera have been shown to be mostly typespecific with respect to neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hyper variable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hyper variable loops of the major capsid protein L1.
References
  • Zur Hausen, H., 1989, Cancer Res. 49: 4677-4691.
  • Chan, SY, et al., 1995, J. Virol. 69: 3074-3083.
  • Lorincz AT, et al., 1992, Obstet Gynecol. 79: 328-337.
  • Munoz N, et al., 2003, N Engl J Med. 348: 518-527.
  • Pastrana DV, et al., 2004, Virology. 321: 205-216.
  • Christensen ND, et al., 1996, Virology. 224: 477-486.
  • Combita AL, et al., 2002, J Virol. 76: 6480-6486.
  • Christensen ND, et al., 2001, Virology. 291:324-334.
  • Fleury MJ, et al., Arch Virol. 2006, 151: 1511-1523.
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