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CAG-FLEX-NES-jRCaMP1a AAV (Serotype 9)

For research use only. Not intended for any clinical use.

Cat. No. :   AAB0045

Serotype :   AAV Serotype 9 Storage :   -80 ℃

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Virus Particles Information

Quality Control

Cat. No. AAB0045
Description Premade AAV particles in serotype 9 containing Cre-dependent jRCaMP1a under the control of a CAG promoter. The nuclear export signal (NES) directs export of proteins from the nucleus to the cytoplasm.
Product Type Adeno-associated virus particles
Tag jRCaMP1a
Serotype AAV Serotype 9
Biosensor jRCaMP1a-Red, improved SNR, slower kinetics, bright
Titer Varies lot by lot, typically ≥1x10^12 GC/mL
Size Varies lot by lot, for example, 30 μL, 100 μL, 500 μL etc.
Storage Store at -80℃. Avoid multiple freeze/thaw cycles.
Shipping Frozen on dry ice
Summary Creative Biogene ensures high-quality AAV particles by optimizing and standardizing production protocols and performing stringent quality control (QC). The specific QC experiments performed vary between AAV particle lots.
Endotoxin Endotoxins, primarily derived from Gram-negative bacteria, can trigger adverse immune responses. Endotoxin contamination is a significant concern in the production of AAV, especially for applications in animal studies and gene therapy. Effective endotoxin quality control is essential in the development and manufacturing of AAV particles. Creative Biogene utilizes rigorous endotoxin detection methods to monitor the endotoxin level in our produced AAV particles to ensure regulatory compliance.
Purity AAV purity is critical for ensuring the safety and efficacy of AAV-based applications.AAV capsids are composed of three main protein components, known as viral proteins: VP1, VP2, and VP3. These proteins play a critical role in the structure and functionality of the AAV capsid. Monitoring the VP1, VP2, and VP3 content in AAV preparations is essential for quality control in AAV production. Our AAV particles are tested for showing three clear bands of VP1, VP2 VP3 by SDS-PAGE.
Sterility The AAV virus samples are inoculated into the cell culture medium for about 5 days to detect bacterial and fungal growth.
Transducibility Upon requirement, Creative Biogene can perform in vitro or in vivo transduction assays to evaluate the ability of AAV to deliver genetic material into target cells or tissues, and assess gene expression and functional activities.
Empty vs. Full Capsids Based-on our proprietary AAV production and purification technology, Creative Biogene can always offer AAV particles with high ratio of full capsids. If required, we can also assess the ratio for a specifc lot of AAV particles by transmission electron microscopy (TEM) or other methods.
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Adeno-associated virus (AAV) is a small, non-pathogenic virus found in many mammals, including humans. AAV has a simple structure consisting of an icosahedral capsid with a diameter of approximately 26 nm and a single-stranded DNA genome of approximately 4.7 kb. Recombinant AAV (rAAV) has attracted great interest as a gene delivery vector due to its excellent in vivo tissue tropism for both dividing and non-dividing cells, especially in the field of gene therapy. The development of rAAV has been greatly facilitated by the large number of AAV capsid serotypes and variants found from human and non-human primate (NHP) tissues, which together provide a toolbox for targeting various tissues and cell types.

In addition to packaging, protecting, and delivering the viral genome, the AAV capsid also serves as an attachment surface for viral host cell receptors, which in part determines the cell and tissue tropism of AAV. Studies have shown that many AAV serotypes can interact with glycosylated cell surface proteins for viral uptake, suggesting that cell surface glycans are the first contact receptors for the capsid. Although most AAVs are heparan sulfate proteoglycan binders (e.g., AAV2, AAV3, and AAV13), sialic acid binders (e.g., AAV1, AAV4, and AAV5), or both (e.g., AAV6), AAV9 has been shown to be a unique terminal galactose binder and has also been described to transduce cells in the presence of the 37- to 67-kDa laminin receptor.

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Using jRCaMP1a has significantly improved the sensitivity of our calcium imaging experiments, leading to better data quality and interpretation.

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