Recombinant HPV16 L1/Major capsid protein L1 Protein, N-GST & C-His

Reference: YVV08802
Product nameRecombinant HPV16 L1/Major capsid protein L1 Protein, N-GST & C-His
Origin speciesHuman papillomavirus type 16
Expression systemEukaryotic expression
Molecular weight76.45 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeConfidential
Aliases /SynonymsMajor capsid protein L1, L1, Human papillomavirus type 16, HPV16
ReferenceYVV08802
NoteFor research use only.

Description of Recombinant HPV16 L1/Major capsid protein L1 Protein, N-GST & C-His

Introduction Recombinant HPV16 L1/Major capsid protein L1 is a protein that plays a crucial role in the structure and activity of the human papillomavirus (HPV). This protein is a major component of the viral capsid, which is the outer shell of the virus that protects its genetic material. Recombinant HPV16 L1/Major capsid protein L1 is produced through recombinant DNA technology, making it a valuable tool in research and medical applications. Structure of Recombinant HPV16 L1/Major capsid protein L1 Recombinant HPV16 L1/Major capsid protein L1 is a large protein with a molecular weight of approximately 55 kDa. It is composed of 495 amino acids and has a complex three-dimensional structure. The protein is made up of five structural domains, including the N-terminal arm, the L1 head domain, the L1 tail domain, the L1 helical domain, and the C-terminal arm. The N-terminal arm is responsible for the attachment of the protein to the viral DNA. The L1 head domain is the largest domain and contains the majority of the antigenic sites that are recognized by the immune system. The L1 tail domain is involved in the assembly of the viral capsid. The L1 helical domain is responsible for the structural stability of the capsid. The C-terminal arm is involved in the binding of the virus to host cells. Activity of Recombinant HPV16 L1/Major capsid protein L1 The main function of Recombinant HPV16 L1/Major capsid protein L1 is to form the viral capsid, which is essential for the survival and replication of the virus. The protein self-assembles into pentamers, which then form the icosahedral capsid structure of the virus. These capsids are highly stable and can withstand harsh environmental conditions, allowing the virus to remain infectious for extended periods. In addition to its structural role, Recombinant HPV16 L1/Major capsid protein L1 also plays an important role in the immune response to HPV infection. The protein contains numerous antigenic sites that are recognized by the host immune system. These sites elicit a strong immune response, leading to the production of antibodies that can neutralize the virus and prevent infection. Application of Recombinant HPV16 L1/Major capsid protein L1 Recombinant HPV16 L1/Major capsid protein L1 has several important applications in the field of research and medicine. One of the most significant applications is in the development of vaccines against HPV infection. The recombinant protein is used as an antigen in HPV vaccines, which stimulate the production of antibodies that can protect against infection. These vaccines have been shown to be highly effective in preventing HPV-related diseases, including cervical cancer. Recombinant HPV16 L1/Major capsid protein L1 is also used in diagnostic tests for HPV infection. The protein can be detected in blood or tissue samples, indicating the presence of the virus. This is particularly useful in screening for HPV infection in high-risk populations, such as sexually active individuals. In addition, Recombinant HPV16 L1/Major capsid protein L1 is a valuable tool in research on HPV and related diseases. Its structural and immunological properties make it an ideal candidate for studying the mechanisms of HPV infection and the development of new treatments and vaccines. Conclusion Recombinant HPV16 L1/Major capsid protein L1 is a crucial component of the human papillomavirus, playing a vital role in the structure, activity, and immune response to the virus. Its use in vaccines and diagnostic tests has greatly contributed to the prevention and detection of HPV-related diseases. Furthermore, its unique properties make it a valuable tool in research on HPV and the development of new treatments.

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