rab8a cdna Search Results


expression plasmids for 92 rab8a variants  (GenScript corporation)
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GenScript corporation expression plasmids for 92 rab8a variants
A . Principle of the dynamic scanning fluorimetry (DSF) assay. The temperature of the samples is gradually increased resulting in protein destabilization. Fluorescence is monitored to measure protein unfolding. B . Apo <t>Rab8A</t> unfolded at 51° C . The addition of GDP and GTP stabilized Rab8A by 15 and 21 K, respectively. C. All Rabs from the panel were stable in presence of GDP and GTP with melting temperatures between 45 and 78°C.
Expression Plasmids For 92 Rab8a Variants, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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A . Principle of the dynamic scanning fluorimetry (DSF) assay. The temperature of the samples is gradually increased resulting in protein destabilization. Fluorescence is monitored to measure protein unfolding. B . Apo Rab8A unfolded at 51° C . The addition of GDP and GTP stabilized Rab8A by 15 and 21 K, respectively. C. All Rabs from the panel were stable in presence of GDP and GTP with melting temperatures between 45 and 78°C.

Journal: bioRxiv

Article Title: Selectivity profiles and substrate recognition of Rab phosphorylating kinases

doi: 10.1101/2025.04.09.647999

Figure Lengend Snippet: A . Principle of the dynamic scanning fluorimetry (DSF) assay. The temperature of the samples is gradually increased resulting in protein destabilization. Fluorescence is monitored to measure protein unfolding. B . Apo Rab8A unfolded at 51° C . The addition of GDP and GTP stabilized Rab8A by 15 and 21 K, respectively. C. All Rabs from the panel were stable in presence of GDP and GTP with melting temperatures between 45 and 78°C.

Article Snippet: Expression plasmids for 92 Rab8A variants were obtained from Genscript ( Table S3 ).

Techniques: Fluorescence

A . Selected Rab:GDP and Rab:GTP complexes were subjected to LRRK1 and LRRK2 phosphorylation. In contrast to LRRK1, LRRK2 preferred Rab:GDP complexes as substrates. B . Structure models of Rab8A:GDP and Rab8A:GTP highlighting the impact of the GTP γ phosphate on Rab8A substrate properties. Blue indicates low B-factors, while red indicates high B-factors. C . pRabs were tested as PPM1H phosphatase substrates by incubating the pRabs in presence of PPM1H followed by MS evaluation of the phosphogrades. The pRabs labelled with blue diamonds were completely dephosphorylated, while the pRabs labelled with grey diamonds were not dephosphorylated by PPM1H.

Journal: bioRxiv

Article Title: Selectivity profiles and substrate recognition of Rab phosphorylating kinases

doi: 10.1101/2025.04.09.647999

Figure Lengend Snippet: A . Selected Rab:GDP and Rab:GTP complexes were subjected to LRRK1 and LRRK2 phosphorylation. In contrast to LRRK1, LRRK2 preferred Rab:GDP complexes as substrates. B . Structure models of Rab8A:GDP and Rab8A:GTP highlighting the impact of the GTP γ phosphate on Rab8A substrate properties. Blue indicates low B-factors, while red indicates high B-factors. C . pRabs were tested as PPM1H phosphatase substrates by incubating the pRabs in presence of PPM1H followed by MS evaluation of the phosphogrades. The pRabs labelled with blue diamonds were completely dephosphorylated, while the pRabs labelled with grey diamonds were not dephosphorylated by PPM1H.

Article Snippet: Expression plasmids for 92 Rab8A variants were obtained from Genscript ( Table S3 ).

Techniques: Phospho-proteomics

A . 92 Rab8A variants were tested as LRRK2 substrates. Several variants were poor substrates in comparison to wild-type Rab8A. Other variants boosted the LRRK2 kinase activity nearly 100-fold. B . Recombinant LRRK2 and eGFP-Rab8A variants were expressed in 293T cells and the Rab8A phosphogrades were assessed by Western blotting. The phosphogrades of the Rab8A variants R79A and R104A were reduced, and the phosphogrades of the variants E68R and E108R increased. The results of at least three independent measurements are shown as mean ± SD, *** indicates P <0.001. C . Rab8A:GDP structure model (from PDB ID 4LHY) with the T72 phosphoacceptor residue and residues that modulate the substrate properties for the LRRK2 kinase. Our mutational analysis suggests that the LRRK2 docking interface is in the C-terminus of the α3 helix.

Journal: bioRxiv

Article Title: Selectivity profiles and substrate recognition of Rab phosphorylating kinases

doi: 10.1101/2025.04.09.647999

Figure Lengend Snippet: A . 92 Rab8A variants were tested as LRRK2 substrates. Several variants were poor substrates in comparison to wild-type Rab8A. Other variants boosted the LRRK2 kinase activity nearly 100-fold. B . Recombinant LRRK2 and eGFP-Rab8A variants were expressed in 293T cells and the Rab8A phosphogrades were assessed by Western blotting. The phosphogrades of the Rab8A variants R79A and R104A were reduced, and the phosphogrades of the variants E68R and E108R increased. The results of at least three independent measurements are shown as mean ± SD, *** indicates P <0.001. C . Rab8A:GDP structure model (from PDB ID 4LHY) with the T72 phosphoacceptor residue and residues that modulate the substrate properties for the LRRK2 kinase. Our mutational analysis suggests that the LRRK2 docking interface is in the C-terminus of the α3 helix.

Article Snippet: Expression plasmids for 92 Rab8A variants were obtained from Genscript ( Table S3 ).

Techniques: Comparison, Activity Assay, Recombinant, Western Blot, Residue