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CALML5 Antibody, Mouse MAb

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Human CALML5 Antibody Product Information
Immunogen:Recombinant Human CALML5 protein (Catalog#11783-H20E)
Clone ID:2A3E2
Ig Type:Mouse IgG1
Concentration:
Formulation:0.2 μm filtered solution in PBS with 5% trehalose
Preparation:This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human CALML5 (rh CALML5; Catalog#11783-H20E; AAH39172.1; Met 1-Glu 146). The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.
Other CALML5 Antibody Products
Reactivity: Human  
Application: ELISA  IHC-P  
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11783-RP02-50
11783-RP02-200
11783-RP02-100
50 µg 
200 µg 
100 µg 
Add to Cart
Reactivity: Human  
Application: ELISA  
    11783-RP01-400
    11783-RP01-200
    11783-RP01-100
    400 µg 
    200 µg 
    100 µg 
    Add to Cart
    Reactivity: Human  
    Application: ELISA  IF  ICC/IF  
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    11783-R158-50
    11783-R158-100
    50 µg 
    100 µg 
    Add to Cart
    Reactivity: Human  
    Application: 
      11783-MM08-50
      11783-MM08-200
      11783-MM08-100
      11783-MM08-1
      50 µg 
      200 µg 
      100 µg 
      1 mg 
      Add to Cart
      Reactivity: Human  
      Application: IHC-P  
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      11783-R119-50
      11783-R119-100
      50 µg 
      100 µg 
      Add to Cart
      CALML5 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.

      Human CALML5 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.
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      Catalog: 11783-MM01-200
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      All information of our products is subject to change without notice. Please refer to COA enclosed in shipped package for the newest information.
      Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"