Technical Data
Papilloma Virus, Human, Type 16 Capsid L1 (hPV, HPV-16, HPV-16 Capsid, HPV16 Capsid Protein, Human Papillomavirus Type 16 L1, HPV16 L1, Human Papillomavirus Type 16 Major Capsid Protein L1, HPV16 Major Capsid Protein L1, Major Capsid Protein, Major Capsid
L1 is a major capsid protein of type 16 human papilloma virus. Infection with specific types of HPV has been associated with an increased risk of developing cervical neoplasia. HPV types 6 and 11 have been associated with relatively benign diseases such as genital warts but types 16 and 18 are strongly associated with cervical, vaginal, and vulvar malignancies.

Suitable for use in Western Blot, Immunoprecipitation and Immunohistochemistry. Other applications not tested.

Recommended Dilutions:
Immunohistochemistry: Paraffin sections
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
MabIgG2a9A275Affinity Purified
100ug-20CBlue IceMouse
Human papilloma virus type 16, major capsid protein L1.
Purified by Protein A affinity chromatography.
Supplied as a liquid in PBS.
Recognizes Papilloma Virus, Human, Type 16 Capsid L1. Reacts with a 56kD protein in cells infected with L1-vaccinia virus, the protein being present in a predominantly nuclear location. Reacts very strongly with biopsy specimens containing HPV-16 or -33.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. McLean, C.S., et al., Production characterisation of a monoclonal antibody to human papillomavirus type 16 using recombinant vaccinia virus. J. Clin. Pathol. 43: 488-492 (1990). 2. Zhang, W., et al., Expression of human papillomavirus type 16 L1 protein in Escherichia coli: denaturation, renaturation, self-assembly of virus-like particles in vitro. Virology 243: 423-431 (1998).