208670 Calmodulin, His•Tag® Human, Recombinant

208670
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      Overview

      Replacement Information

      Pricing & Availability

      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      208670-50UG
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      Stocked 
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          Plastic ampoule 50 μg
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          Description
          OverviewFull-length, recombinant human calmodulin fused to a HisTag® sequence at the N-terminus. Contains four functional Ca2+-binding sites (aa 20-31; aa 56-67; aa 93-104; aa 129-140) with EF-hands (aa 7-42; aa 43-78; aa 80-115; aa 116-148); and a ubiquitination site at Lys21. This preparation is qualified for use as a substrate for protein tyrosine kinases in in vitro assays. Through its interaction with Ca2+, calmodulin mediates the control of a large number of enzymes, including protein kinases and phosphatases. It is expected to be phosphorylated at Thr44 by CaMK4. In addition, it serves as a substrate for various protein tyrosine kinases.
          Catalogue Number208670
          Brand Family Calbiochem®
          SynonymsCalmodulin, Human, Recombinant
          Application Data
          References
          ReferencesChou, J.J., et al. 2001.Nat. Struct. Biol.8, 990.
          Lennon, G., et al. 1996.Genomics33, 151.
          Product Information
          FormLiquid
          FormulationIn PBS, 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 Standard Handling
          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

          Documentation

          SDS

          Title

          Safety Data Sheet (SDS) 

          Certificates of Analysis

          TitleLot Number
          208670

          References

          Reference overview
          Chou, J.J., et al. 2001.Nat. Struct. Biol.8, 990.
          Lennon, G., et al. 1996.Genomics33, 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.

          Revision28-May-2008 RFH
          SynonymsCalmodulin, Human, Recombinant
          Application Data
          DescriptionFull-length, recombinant human calmodulin fused to a HisTag® sequence at the N-terminus. Contains four functional Ca2+-binding sites (aa 20-31; aa 56-67; aa 93-104; aa 129-140) with EF-hands (aa 7-42; aa 43-78; aa 80-115; aa 116-148); and a ubiquitination site at Lys21. This preparation is qualified for use as a substrate for protein tyrosine kinases in in vitro assays. Through its interaction with Ca2+, calmodulin mediates the control of a large number of enzymes, including protein kinases and phosphatases. It is expected to be phosphorylated at Thr44 by CaMK4. In addition, it serves as a substrate for various protein tyrosine kinases.
          FormLiquid
          FormulationIn PBS, 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 ≤ -70°C
          Avoid freeze/thaw
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
          Toxicity Standard Handling
          ReferencesChou, J.J., et al. 2001.Nat. Struct. Biol.8, 990.
          Lennon, G., et al. 1996.Genomics33, 151.