Anti-CALML5 antibody

Cat.#: 106145

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Product Information

  • Product Name
    Anti-CALML5 antibody
  • Documents
  • Description
    Rabbit monoclonal to CALML5
  • Tested applications
    IHC-P
  • Species reactivity
    Human CALML5
  • Alternative names
    CALML5 antibody; CLSP antibody
  • Immunogen
  • Isotype
    Rabbit IgG
  • Preparation
    This antibody was obtained from a rabbit immunized with purified, recombinant Human CALML5 (rh CALML5; AAH39172.1; Met1-Glu146).
  • Clonality
    Monoclonal
  • Formulation
    0.2 μm filtered solution in PBS with 5% trehalose
  • Storage instructions
    This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free.
    Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
  • Applications

    IHC-P: 0.5-5 μg/mL

  • Validations

    CALML5 Antibody, Rabbit MAb, Immunohistochemistry

    CALML5 Antibody, Rabbit MAb, Immunohistochemistry

    Immunochemical staining of human CALML5 in human skin with rabbit monoclonal antibody (5 µg/mL, formalin-fixed paraffin embedded sections). Positive staining was localized to epithelium.

  • Background
    Calmodulin-like protein 5, also known as Calmodulin-like skin protein, CALML5 and CLSP, is a protein which contains four EF-hand domains. CALML5 / CLSP is particularly abundant in the epidermis where its expression is directly related to keratinocyte differentiation.The expression is very low in lung. CALML5 / CLSP binds calcium. It may be involved in terminal differentiation of keratinocytes. Coxsackievirus and adenovirus receptor (CAR) is a member of the immunoglobulin (Ig) superfamily and a component of epithelial tight junction. CAR functions as a primary receptor for coxsackievirus B and adenovirus (Ad) infection. CALML5 / CLSP is closely related to CAR. The structure and dynamics of human calmodulin-like skin protein CALML5 / CLSP have been characterized by NMR spectroscopy. The mobility of CALML5 / CLSP has been found to be different for the N-terminal and C-terminal domains. The N-terminal domain is characterized by four stable helices, which experience large fluctuations. This is shown to be due to mutations in the hydrophobic core. The overall N-terminal domain behavior is similar both in the full-length protein and in the isolated domain.
  • References
    • Mehul B., et al., 2000, J. Biol. Chem. 275:12841-12847.
    • Babini E., et al., 2006, Structure 14:1029-1038.
    • Kawabata,K. et al., 2007, Gene Ther. 14 (16):1199-207.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"