codon-optimized version of full-length human katanin (MorphoSys ag)
90
Structured Review
MorphoSys ag
codon-optimized version of full-length human katanin
Codon Optimized Version Of Full Length Human Katanin, supplied by MorphoSys ag, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/length+codon/codon+optimized+version+of+full+length+human+katanin/pmc03521757-62-4-10
Average 90 stars, based on 1 article reviews
Codon Optimized Version Of Full Length Human Katanin, supplied by MorphoSys ag, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/length+codon/codon+optimized+version+of+full+length+human+katanin/pmc03521757-62-4-10
Average 90 stars, based on 1 article reviews
codon-optimized version of full-length human katanin - by Bioz Stars,
2026-11
90/100 stars
Images
1) Product Images from "Spastin's Microtubule-Binding Properties and Comparison to Katanin"
Article Title: Spastin's Microtubule-Binding Properties and Comparison to Katanin
Journal: PLoS ONE
doi: 10.1371/journal.pone.0050161
Figure Legend Snippet: Movie S2 shows GFP-katanin p60 (green) moving along AlexaFluor 555 microtubules (red). The movie plays in real time, the width of the canvas is 25.1 µm.
Techniques Used:
Figure Legend Snippet: The figure shows a sequence alignment of domains of Drosophila and human spastin, as well as human katanin. The black contour highlights the position of the human spastin linker, residues with a high degree of conservation are red, residues with low degree are blue. The location of the highly basic patch in human spastin is boxed in blue. Above the alignment, the location of the sequence in the context of human spastin is indicated, below the location in human katanin. For details, see text.
Techniques Used: Sequencing
Figure Legend Snippet: Nucleotide dependence of microtubule interaction.
Techniques Used:
Figure Legend Snippet: Salt dependence of microtubule interaction.
Techniques Used:
Figure Legend Snippet: Panel A displays the constructs used for katanin binding experiments. Panel B shows a quantitative SDS-gel of supernatants (unbound) and pellets (microtubule-bound) of an in vitro binding assay of truncated katanin constructs and microtubules. Increasing microtubule concentrations (0 to 10 µM) were incubated with a fixed katanin construct concentration (1 µM). The density of the katanin construct band was plotted against the microtubule concentration and fitted to a Hill function (panel C). The half-maximal saturation was reached at 0.34 µM (Kat12) and 0.40 µM (Kat2). Only constructs containing domain 2 were able to bind to microtubules.
Techniques Used: Construct, Binding Assay, SDS-Gel, In Vitro, Incubation, Concentration Assay
Figure Legend Snippet: Binding stoichiometry.
Techniques Used: Binding Assay
Figure Legend Snippet: Panel A shows a SDS-gel of co-sedimentation assays with katanin (E309Q mutant, 1 mM ATP) and a constant concentration of microtubules (2 µM; indicated by a dotted line). With increasing katanin concentrations, an increasing amount of protein is co-sedimented with microtubules. Panel B: Plot of the densitometric analysis as in . Panel C shows the same experiment for wild type katanin.
Techniques Used: SDS-Gel, Sedimentation, Mutagenesis, Concentration Assay
Related Articles
Synthesized:Article Title: Spastin's Microtubule-Binding Properties and Comparison to Katanin Article Snippet: All mutants were generated following the QuickChange protocol (Agilent Technologies, Santa Clara, CA, U.S.A.). .. A codon-optimized version of |