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Immunoprecipitation/ IP Kit- Anti-HPV-L1 Immunomagnetic Beads 1mL

价:
1900.00
价:
¥1710.00

号:MB68009-MM01

牌:义翘神州

账期 货到付款

EA (预计5-7工作日到货)

工作时间

周一至周五:9:00-18:00

咨询电话

0771-3293894

在线咨询

客服 郭恒 蔡玉坤 曾宪飞 技术咨询

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Anti-HPV capsid L1 Magnetic Beads-IP Kit Product Components

Components Storage
Anti-HPV capsid L1 Magnetic Beads1,3 2-8℃ for 12 months
NP40 Cell Lysis Buffer2 -20℃ for 12 months
5×TBST(pH7.4)  
1×TBST(pH7.4)  
ddH2O  
CD166 Positive Cell Lysate -20℃ for 12 months
Alkaline Elution Buffer 2-8℃ for 12 months
Acidity Elution Buffer 2-8℃ for 12 months
Neutralization Buffer 2-8℃ for 12 months

[1] The IP KIT contains anti-HPV capsid L1 magnetic Beads (2 mg/mL) in phosphate buffered saline (PBS, pH 7.4) with sodium azide (0.1%).

[2] Using NP-40 cell lysate buffer in the kit is required,otherwise,the magnetic beads may be precipitated.

[3] Shipping: Magnetic Beads kits are shipped at ambient temperature in which magnetic beads are provided in liquid buffer.

Anti-HPV capsid L1 Magnetic Beads-IP Kit Product Description

The Anti-HPV capsid L1 magnetic Beads, conjugated with Anti-HPV capsid L1 antibody, are used for immuneprecipitation (IP) of HPV capsid L1 proteins which expressed in vitro expression systems. For IP, the beads are added to a sample containing HPV capsid L1 proteins to form a bead-protein complex. The complex is removed from the solution manually using a magnetic separator. The bound HPV capsid L1 proteins are dissociated from the magnetic beads using an elution buffer.

Anti-HPV capsid L1 Magnetic Beads-IP Kit Antibody Information

Antibody
HPV16 L1 Antibody (Conformational Antibody), Mouse MAb( 68009-MM01)
Immunogen
Recombinant HPV16 L1 virus like particle
Species Reactivity
Human Papillomavirus (HPV)
Source
Monoclonal HPV16 Mouse IgG1
Preparation
This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant HPV16 L1 virus like particle. The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.
Applications
Immunoprecipitation (IP), Minimum Protein Purification

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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