AAV8 Empty Capsids (purity> 95%)

Overview
- Purified empty adeno-associated virus 8 capsids (AAV8)
  Packaging Plasmid: pRep2-Cap8 + pHelper
  Quality check: Final titer was assigned on internal reference material using two AAV8 ELISA kits (PRAAV8 and PRAAV8XP); QC included analysis of filling grade and Endotoxin testing
  
  KEY FEATURES
  • Fully assembled, empty AAV8 capsids
  • Serotype-specific conformational epitopes
  • Reliable positive control for dot blot, western blot, ELISA
  • Quality controlled for purity, AAV titer and filling grade
  • Alignment to internal reference standard material
  
  Please contact us at for specific academic pricing.
  
  Background
  
  The AAV8 empty capsids consist of fully assembled, empty AAV8 capsids and have a titer of > 5.0E+12 capsids/ml. Final concentrations are lot-specific and can be found on the corresponding vial.
  
  The AAV8 empty capsids are provided with titers above 5.0E+12 capsids/ml in a liquid formulation. Since the buffer does not contain any stabilizing proteins or dyes, the capsids can be used in various applications, including dot blot, western blot and ELISA. The lot-specific titers were assigned using two different AAV8 ELISA (PRAAV8 and PRAAV8XP). Internal standard material calibrated with the ATCC reference standard material for AAV8 (VR-1816) was used for the final titer declaration.
  Our comprehensive quality control ensures well-characterized capsid material which can be implemented as reference material in a variety of assays to prove the validity of the corresponding assay.
  
  We also offer empty capsid material for the AAV serotypes 1, 2, 5, 6 and 9.
  
  More Details
  
  AAV Empty Capsids
Properties
- Source
  
  HEK293T cells
  
  Purification
  
  Affinity Chromatography (POROS CaptureSelect AAVX Affinity Resin, Thermo Fisher Scientific)
  Purity: > 95% by SDS-PAGE and silver stain
  
  Formulation
  
  PBS + 0.014% Tween20 + 1 mM MgCl2 + 2.5 mM KCl
  
  Storage
  
  Up to 2 weeks: 2-8°C; long term storage in aliquots at -80°C; avoid > 5 freeze/thaw cycles
  
  Note
  
  Please centrifuge before opening to ensure complete recovery of vial contents; repeated freeze/thaw cycles and aliquoting can lead to a drop in titer
  
  Concentration
  
  > 5.0E+12 capsids/ml; please find the lot-specific concentration on the CoA and on the vial
  
  Endotoxin
  
  < 5.0 EU/ml
  
  * For research use only

Applications

Application

Dot blot; ELISA; WB

Application	Dilutions
Dot Blot	Depending on primary antibody and detection method
ELISA	As a positive control in ELISA, dilute in ASSB 1x (provided with our AAV8 ELISA) and analysis at least in duplicates is recommended
Western Blot (WB)	Depending on primary antibody and detection method

Datasheet

Analytical ultracentrifugation (AUC) of the AAV8 empty capsids shows a strong peak in the 65S range typical for empty capsid with a very small peak of 80-100S corresponding to DNA containing capsids. Capsids were centrifuged at 18000 rpm with 120 scans (1/min) and detected by interference.

SDS PAGE with AAV8 empty capsids. The AAV8 VP1, VP2 and VP3 proteins were separated on a 10% SDS PAGE and visualized by Pierce Silver stain kit. Only VP1, VP2 and VP3 proteins in the correct stoichiometry of 1:1:10 are detectable indicating a purity of the AAV preparation of > 95%.

AAV8 Empty Capsids (purity> 95%)

AAV8 Empty Capsids (purity> 95%)

Background

More Details

Analytical ultracentrifugation (AUC) of the AAV8 empty capsids shows a strong peak in the 65S range typical for empty capsid with a very small peak of 80-100S corresponding to DNA containing capsids. Capsids were centrifuged at 18000 rpm with 120 scans (1/min) and detected by interference.

SDS PAGE with AAV8 empty capsids. The AAV8 VP1, VP2 and VP3 proteins were separated on a 10% SDS PAGE and visualized by Pierce Silver stain kit. Only VP1, VP2 and VP3 proteins in the correct stoichiometry of 1:1:10 are detectable indicating a purity of the AAV preparation of > 95%.

AAV8 Empty Capsids (purity> 95%)

AAV8 Empty Capsids (purity> 95%)

Background

More Details

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