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654163 Tubulin-γ-1, His•Tag® Fusion

Tubulin-γ-1, His•Tag® Fusion MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Tubulin-γ-1, Human, Recombinant

654163
  
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      Overview

      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
      Catalogue Number GTIN
      654163 0

      Documentation

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

      TitleLot Number
      654163

      References

      Reference overview
      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.