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Render Timestamp: 2024-10-04T09:37:37.245Z
Commit: f04ddd7fea9fb3592f59f61482fcb94610d25cbe
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

CFTR (D6W6L) Rabbit mAb (BSA and Azide Free) #30167

Filter:
  • WB
  • IF

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 150-220
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    This product is the carrier free version of product #78335. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.

    This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.

    BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.

    Formulation

    Supplied in 1X PBS (10 mM Na2HPO4, 3 mM KCl, 2 mM KH2PO4, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.

    For standard formulation of this product see product #78335

    Storage

    Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.

    Specificity / Sensitivity

    CFTR (D6W6L) Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of total CFTR protein. This antibody also detects a 60 kDa band of unknown origin in some cell lines.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with recombinant protein fragment of human CFTR protein. The epitope corresponds to a region surrounding Arg735 of human CFTR.

    Background

    CFTR (ABC35, ABCC7, CBAVD, CF, dj760C5.1, MRP7, TNR-CFTR) is a member of the ATP-binding cassette (ABC) transporter superfamily. Mutations in ABC genes have been linked to many diseases. CFTR is a plasma membrane cyclic AMP activated chloride channel that is expressed in the epithelial cells of the lung and several other organs (1,2). It mediates the secretion of Cl- and also regulates several channels including the epithelial sodium channel (ENaC), K+ channels , ATP release mechanisms, anion exchangers, sodium bicarbonate transporters and aquaporin water channels (3,4,5,6,7,8 9,10). Mutations in the CFTR gene cause cystic fibrosis, a disease that is characterized by exocrine pancreatic insufficiency, increase in sweat gland NaCl, male infertility and airway disease (1,2,11). Intracellular trafficking regulates the number of CFTR molecules at the cell surface, which in part regulates Cl- secretion. Deletion of phenylalanine 508 (deltaF508) is the most common mutation in CF patients. This mutation results in retention in the ER, where ER quality control mechanisms target the deltaF508 mutant to the proteosome for degradation (12-14). Therefore, disruption of CFTR trafficking leads to disregulation of Cl- secretion at the plasma membrane of epithelial cells.
    1. Bradbury, N.A. et al. (1999) Am. J. Physiol. 276, L659-L668.
    2. Bertrand, C.A. and Frizzell, R.A. (2003) Am. J. Physiol. Cell Physiol. 285, C1-C18.
    3. Ko, S.B. et al. (2004) Nat. Cell Biol. 6, 343-350.
    4. Ji, H.L. et al. (2000) J. Biol. Chem. 275, 27947-27956.
    5. Jiang, Q. et al. (2000) J. Biol. Chem. 275, 13266-13274.
    6. Stutts, M.J. et al. (1997) J. Biol. Chem. 272, 14037-14040.
    7. Cheung, K.H. et al. (2003) Biol. Reprod. 68, 1505-15010.
    8. Shumaker, H. et al. (1999) Am. J. Physiol. 276, C16-C25.
    9. Schwiebert, E.M. et al. (1999) Physiol. Rev. 79, S145-S166.
    10. Yoo, D. et al. (2004) J. Biol. Chem. 279, 6863-6873.
    11. Cohn, J.A. et al. (2005) Hum. Mutat. 26, 303-307.
    12. Gibson, R.L. et al. (2003) Am. J. Respir. Crit. Care Med. 168, 918-951.
    13. Boucher, R.C. (2004) Eur. Respir. J. 23, 146-158.
    14. Riordan, J.R. (2005) Annu. Rev. Physiol. 67, 701-718.
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