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654163 Tubulin-γ-1, His•Tag® Fusion

654163
  
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Přehled

Replacement Information
Description
Overview

This product has been discontinued.





Full-length, recombinant, human tubulin-γ-1 (GCP-1, γ-1 tubulin) fused to His•Tag® and S•Tag™ sequences at the N-terminus and expressed in E. coli. This preparation is qualified for use as a substrate for protein tyrosine kinases in in vitro assays. Tubulin-γ-1 is a major constituent of microtubules and is found at microtubule organizing centers (MTOC) such as the spindle poles and the centrosome. It is phosphorylated by the serine-threonine polo-like kinase (Plk) and it has been reported that the 55 kDa regulatory subunit of PI 3-kinase interacts with tubulin-γ in response to insulin. Moreover, tubulin-γ is tyrosine phosphorylated by Src family kinases (Fyn, Lyn, Src). Studies have shown that tubulin-γ binds to GST-Fyn-SH2 and GST-Src-SH2 fusion proteins, but not to their SH3 analogs. In budding yeast, Tyr445 is phosphorylated (this residue is invariant all γ-tubulins and corresponds to Tyr443 in the human sequence). Mutation of this residue changes microtubule dynamics. Phosphorylation is expected at Tyr92 by InsR, Tyr435 and Tyr443 by Src, and at Thr191, Thr241, and Thr443 by PKC.
Catalogue Number654163
Brand Family Calbiochem®
SynonymsTubulin-γ-1, Human, Recombinant
Application Data
References
ReferencesKukharskyy, V., et al. 2004. Exp. Cell Res. 298, 218.
Lennon, G., et al. 1996. Genomics 33, 151.
Product Information
FormLiquid
FormulationIn PBS, 4 M Urea, 0.2% Protease Inhibitor Cocktail Set VII (Cat. No. 539138).
Applications
Biological Information
Purity≥90% by SDS-PAGE
Concentration Label Please refer to vial label for lot-specific concentration
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Dry Ice Only
Toxicity Irritant
Storage ≤ -70°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Katalogové číslo GTIN
654163 0

Documentation

Tubulin-γ-1, His•Tag® Fusion Certificates of Analysis

TitleLot Number
654163

References

Přehled odkazů
Kukharskyy, V., et al. 2004. Exp. Cell Res. 298, 218.
Lennon, G., et al. 1996. Genomics 33, 151.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision15-September-2008 RFH
SynonymsTubulin-γ-1, Human, Recombinant
Application Data
DescriptionFull-length, recombinant, human tubulin-γ-1 (GCP-1, γ-1 tubulin) expressed in E. coli with N-terminal His•Tag® and S•Tag™ sequences. This preparation is qualified for use as a substrate for protein tyrosine kinases in in vitro assays. Tubulin-γ-1 is a major constituent of microtubules and is found at microtubule organizing centers (MTOC) such as the spindle poles and the centrosome. It is phosphorylated by the serine-threonine polo-like kinase (Plk) and it has been reported that the 55 kDa regulatory subunit of PI 3-kinase interacts with tubulin-γ in response to insulin. Moreover, tubulin-γ is tyrosine phosphorylated by Src family kinases (Fyn, Lyn, Src). Studies have shown that tubulin-γ binds to GST-Fyn-SH2 and GST-Src-SH2 fusion proteins, but not to their SH3 analogs. In budding yeast, Tyr445 is phosphorylated (this residue is invariant all γ-tubulins and corresponds to Tyr443 in the human sequence). Mutation of this residue changes microtubule dynamics. Phosphorylation is expected at Tyr92 by InsR, Tyr435 and Tyr443 by Src, and at Thr191, Thr241, and Thr443 by PKC.
FormLiquid
FormulationIn PBS, 4 M Urea, 0.2% Protease Inhibitor Cocktail Set VII (Cat. No. 539138).
Concentration Label Please refer to vial label for lot-specific concentration
Purity≥90% by SDS-PAGE
Storage Avoid freeze/thaw
≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Toxicity Irritant
ReferencesKukharskyy, V., et al. 2004. Exp. Cell Res. 298, 218.
Lennon, G., et al. 1996. Genomics 33, 151.