69037 Factor Xa Cleavage Capture Kit

69037
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      Description
      Overview

      The Factor Xa Cleavage Capture Kit is designed for highly specific cleavage of fusion proteins followed by convenient affinity-based capture and removal of Factor Xa. After cleavage of the target protein, Factor Xa is removed with greater than 99% efficiency from the reaction by affinity capture on Xarrest™ Agarose. Following capture of Factor Xa, the agarose is removed by spin-filtration. No buffer changes are necessary because the same buffer conditions are used for both cleavage and capture. The kit includes a Cleavage Control Protein for conducting control digests in parallel with experimental samples, or to test cleavage under customized buffer conditions. The 49 kDa Xa Cleavage Control Protein is cleaved into two proteolytic fragments of 32 kDa and 17 kDa, which are easily visualized by standard SDS-PAGE followed by Coomassie blue staining. The Xa Cleavage Control Protein also features an amino terminal S•Tag™ sequence enabling sensitive detection of the 17 kDa proteolytic product with Western Blot reagents..

      Specific Activity: ≥150 IU/ug

      One IU is defined as the amount of enzyme that will release 1 µmole of p-nitroaniline per minute using methanesulfonyl-D-leucyl-glycyl-arginyl-paranitroanilide at 37°C, pH 8.4.

      One µg of enzyme cleaves 50 µg Cleavage Control Protein to >95% completion in 16 hr at 25°C in a buffer containing 50 mM Tris-HCl pH 8.0, 100 mM NaCl, and 5 mM CaCl2.

      Catalogue Number69037
      Brand Family Novagen®
      References
      Product Information
      100 µgRestriction Grade Factor Xa
      2 mlFactor Xa Dilution/Storage Buffer
      5 ml10X Factor Xa Cleavage/Capture Buffer
      2 × 2.5 mlXarrest™ Agarose
      10 µgXa Cleavage Control Protein
      pkg/10Spin Filters, 2 ml capacity
      Applications
      Biological Information
      Biological activityOne microgram of enzyme cleaves 50 µg Xa Cleavage Control Protein to >95% completion in 16 hours at 25°C in a buffer containing 50 mM Tris-HCl pH 8.0, 100 mM NaCl, and 5 mM CaCl₂.
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Blue Ice Only
      Toxicity Multiple Toxicity Values, refer to MSDS
      Storage -20°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      Factor Xa Cleavage Capture Kit Certificates of Analysis

      TitleLot Number
      69037

      Citations

      Title
    • Hongjun Jin, et al. (2007) The human CC chemokine MIP-1 dimer is not competent to bind to the CCR5 receptor. Journal of Biological Chemistry 282, 27976-27983.
    • Masanobu Chinami, et al. (2005) Binding of HTm4 to cyclin-dependent kinase (Cdk)-associated phosphatase (KAP)·Cdk2·cyclin A complex enhances the phosphatase activity of KAP, dissociates cyclin A, and facilitates KAP dephosphorylation of Cdk2. Journal of Biological Chemistry 280, 17235-17242.
    • Gianguido Coffa, et al. (2005) On the relationships of substrate orientation, hydrogen abstraction, and product stereochemistry in single and double dioxygenations by soybean lipoxygenase-1 and its Ala542Gly mutant. Journal of Biological Chemistry 280, 38756-38766.
    • Koji Ohira, et al. (2005) A truncated tropo-myosine-related kinase B receptor, T1, regulates glial cell morphology via rho GDP dissociation inhibitor 1. Journal of Neuroscience 25, 1343-1353.
    • Irene Soderhall, et al. (2005) An ancient role for a prokineticin domain in invertebrate hematopoiesis. journal of Immunology 174, 6153-6160.
    • Domenico Sanfelice, et al. (2004) Letter to the editor: resonance assignment and secondary structire of the La motif. Journal of Biomolecular NMR 29, 449-450.
    • User Protocols

      Title
      TB205 Factor Xa Kits Rev. G 0413JN