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This protein carries a polyhistidine tag at the C-terminus. This protein contains a furin-like convertase cleavage site, 354-RQYR-357, and will be partially processed into N and C-terminal fragment with calculated MW of 38.0 kDa and 24.4 kDa respectively. The protein migrates as 38-40 kDa and 62-100 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
>95% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
Mouse Glypican 3, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.
Emerging VoCs, Lambda, Delta, Beta, Alpha mutants and so on, including RBD, S trimer, S1, NTD, NP, etc. These mutants are of high purity and bioactivity and can be used to evaluate the efficacy of the antibodies and vaccination.
ELISA kits for neutralizing antibody titer assay, binding antibody titer assay, antibody isotype assay, antigen titer assay and inhibitor screening, etc., which can accelerate the research and development of anti-SARS-CoV-2 drugs and vaccines.
50+ targets designed for CAR detection, including PE/FITC/biotin labeled proteins. The key reagents for CD19 and BCMA were FDA DMF filed which can support your IND, NDA and BLA process.
Full length multi-pass TPs with stabilized structure and high bioactivity for immunization, antibody screening, cell based assay and CAR detection, including hot CD20, Claudin 18.2， CD133, GPRC5D，CCR8, CCR5, etc.
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