Specifications
Antibody Isotype
IgG2a, κ
Immunogen
Recombinant adeno-associated virus type 6 (AAV6)
Applications
Application Notes
Dot Blot assay dependent (non-denaturing conditions)
ELISA assay dependent
Immunocytochemistry (ICC)/ Immunofluorescence (IF) assay dependent
Immunohistochemistry (IHC) - frozen ready-to-use
Immunohistochemistry (IHC) - paraffin ready-to-use (microwave treatment recommended)
Images
Indirect ELISA using Mouse anti-AAV6 particle monoclonal antibody (CABT-B9064) as detection antibody
CABT-B9064 and CABT-B9065 bind to multiple serotypes, indicating that these antibodies may target the core structure of the AAV capsid and exhibit broad-spectrum affinity for AAV.
Target
Alternative Names
AAV6; AAV 6; Adeno-associated virus; Adeno-associated virus 6; Adeno-associated virus type 6
Custom Antibody Labeling
We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody.
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Citations
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Adeno-associated virus 6 (AAV6) is a member of the Adeno-associated virus (AAV) family, which are small, non-enveloping viruses that have gained significant attention in the field of gene therapy. AAV6 has a single-stranded DNA genome approximately 4.7 kilobases in size. The genome contains two open reading frames (ORFs), rep and cap, which encode proteins responsible for viral replication and capsid formation, respectively. Its broad tropism, low immunogenicity, and potential for tissue-specific targeting make it an attractive candidate for various therapeutic applications. Ongoing research and clinical trials continue to explore the full potential of AAV6-based gene therapies, paving the way for the development of novel treatments for a range of diseases.
Figure 1. AAV6 structure.
(Source: Ng, R. et al., 2010)
The anti-AAV6 (intact particle) monoclonal antibody (CABT-B9064) is a valuable tool for characterizing different stages of AAV6 infection and analyzing the AAV assembly process. It specifically targets intact AAV6 particles, including both empty and full capsids. One key feature of this monoclonal antibody is its recognition of a conformational epitope found on assembled capsids. This epitope is not present in denatured capsid proteins or native but unassembled capsid proteins. This means that the antibody selectively binds to AAV6 particles that have undergone the proper assembly process, providing a reliable marker for fully assembled and functional capsids.
Significantly, its application is not suitable for immunoblotting due to the antibody's recognition of conformational epitopes. Alternative methods such as immunofluorescence or ELISA are more appropriate for the detection and analysis of intact AAV6 particles using this antibody. By using Anti-AAV6 (intact particle) Monoclonal Antibody, researchers can gain insights into AAV6 assembly kinetics, monitor the presence of intact AAV6 particles during infection, and assess the efficiency of AAV6-mediated gene transfer in different cell types or animal models.
Alternative Names
Anti-AAV6 (intact particle) monoclonal antibody
Anti-Adeno-associated virus type 6 (intact particle) monoclonal antibody
Anti-Adeno-associated virus 6 (intact particle) monoclonal antibody
References
1. Ng R, et al. Structural characterization of the dual glycan binding adeno-associated virus serotype 6. Journal of Virology. 2010, 84(24): 12945-12957.
Q & A
Q: Can this clone distinguish full and empty particles?
A: Clone BEL7 (Cat. No. CABT-B9064) detects assembled/intact particles. It doesn’t distinguish between full and empty particles. The antibody binds both empty and full particles.
To determine the full/empty ratio an ELISA for total capsid titer can be combined with an PCR for genomic titer. To detect assembled/intact capsids an anti-intact particle antibody like the BEL7 is required.
Our anti-intact particle antibodies measure the total capsid titer of intact/assembled particles. They bind to the conformational epitope.Whereas, our anti-capsid protein antibodies bind the denatured capsid proteins, only disassembled capsids.
Customer Reviews
Comparative evaluation of viral, nonviral and physical methods of gene delivery to normal and transformed lung epithelial cells
ANTI-CANCER DRUGS
Authors: Gilbert, Jennifer L.; Purcell, James; Strappe, Padraig; McCabe, Matthew; O'Brien, Timothy; O'Dea, Shirley
Abstract
Few studies have directly compared the efficiencies of gene delivery methods that target normal lung cells versus lung tumor cells. We report the first study directly comparing the efficiency and toxicity of viral [adeno-associated virus (AAV2, 5, 6) and lentivirus], nonviral (Effectene, SuperFect and Lipofectamine 2000) and physical [particle-mediated gene transfer (PMGT)] methods of gene delivery in normal mouse lung cells and in mouse adenocarcinoma cells. Lentivirus pseudotyped with the vesicular stomatitis virus glycoprotein was the most efficient gene transfer method for normal mouse airway epithelial cells [25.95 (+/- 3.57) %] whereas AAV6 was most efficient for MLE-12 adenocarcinoma cells [68.2 (+/- 3.2) %]. PMGT was more efficient in normal mouse airway epithelial cells than AAV5, Lipofectamine 2000 and SuperFect. AAV5 displayed the lowest transfection efficiency at less than 10% in both cell types. PMGT was the only method that resulted in significant toxicity. In summary, for all of the gene delivery methods examined here, lung tumor cells were transfected more easily than normal lung cells. Lipofectamine 2000 is potentially highly selective for lung tumor cells whereas AAV6 and lentivirus vesicular stomatitis virus glycoprotein may be useful for gene delivery strategies that require targeting of both normal and tumor cells.
Optimization of adeno-associated virus vector-mediated gene transfer to the respiratory tract
GENE THERAPY
Authors: Kurosaki, F.; Uchibori, R.; Mato, N.; Sehara, Y.; Saga, Y.; Urabe, M.; Mizukami, H.; Sugiyama, Y.; Kume, A.
Abstract
An efficient adeno-associated virus (AAV) vector was constructed for the treatment of respiratory diseases. AAV serotypes, promoters and routes of administration potentially influencing the efficiency of gene transfer to airway cells were examined in the present study. Among the nine AAV serotypes (AAV1-9) screened in vitro and four serotypes (AAV1, 2, 6, 9) evaluated in vivo, AAV6 showed the strongest transgene expression. As for promoters, the cytomegalovirus (CMV) early enhancer/chicken beta-actin (CAG) promoter resulted in more robust transduction than the CMV promoter. Regarding delivery routes, intratracheal administration resulted in strong transgene expression in the lung, whereas the intravenous and intranasal administration routes yielded negligible expression. The combination of the AAV6 capsid and CAG promoter resulted in sustained expression, and the intratracheally administered AAV6-CAG vector transduced bronchial cells and pericytes in the lung. These results suggest that AAV6-CAG vectors are more promising than the previously preferred AAV2 vectors for airway transduction, particularly when administered into the trachea. The present study offers an optimized strategy for AAV-mediated gene therapy for lung diseases, such as cystic fibrosis and pulmonary fibrosis.
Anti-AAV Antibodies in AAV Gene Therapy: Current Challenges and Possible Solutions
Frontiers in Immunology
Authors: Weber T.
Abstract
Adeno-associated virus (AAV) vector-based gene therapy is currently the only in vivo gene therapy approved in the US and Europe. The recent tragic death of three children in a clinical trial to treat X-Linked Myotubular Myopathy by delivering myotubularin with an AAV8 vector notwithstanding, AAV remains a highly promising therapeutic gene delivery platform. But the successful use of AAV vectors to treat an increasing number of diseases also makes establishing protocols to determine therapeutically relevant titers of pre-existing anti-AAV antibodies and approaches to deplete those antibodies more urgent than ever. In this mini review, I will briefly discuss (i) our knowledge regarding the prevalence of anti-AAV antibodies, (ii) the challenges to measure those antibodies by methods that are most predictive of their influence on therapeutic efficacy of AAV gene transfer, and (iii) approaches to overcome the formidable hurdle that anti-AAV antibodies pose to the successful clinical use of AAV gene therapy.
Development of novel AAV serotype 6 based vectors with selective tropism for human cancer cells
Gene Therapy
Authors: Sayroo R, Nolasco D, Yin Z, et al.
Abstract
Viral vectors-based gene therapy is an attractive alternative to common anti-cancer treatments. In the present studies, AAV serotype 6 vectors were identified to be particularly effective in the transduction of human prostate (PC3), breast (T47D) and liver (Huh7) cancer cells. Next, we developed chimeric AAV vectors with Arg-Gly-Asp (RGD) peptide incorporated into the viral capsid to enable specific targeting of integrin-overexpressing malignant cells. These AAV6-RGD vectors improved transduction efficiency approximately 3-fold compared with wild-type AAV6 vectors by enhancing the viral entry into the cells. We also observed that transduction efficiency significantly improved, up to approximately 5-fold, by the mutagenesis of surface-exposed tyrosine and threonine residues involved in the intracellular trafficking of AAV vectors. Therefore, in our study, the AAV6-Y705-731F+T492V vector was identified as the most efficient. The combination of RGD peptide, tyrosine and threonine mutations on the same AAV6 capsid further increased the transduction efficiency, approximately 8-fold in vitro. In addition, we mutated lysine (K531E) to impair the affinity of AAV6 vectors to heparan sulfate proteoglycan. Finally, we showed a significant increase in both specificity and efficiency of AAV6-RGD-Y705-731F+T492V+K531E vectors in a xenograft animal model in vivo. In summary, the approach described here can lead to the development of AAV vectors with selective tropism to human cancer cells.
AAV titration ELISA
Certificate of Analysis
