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Render Timestamp: 2024-12-20T11:00:54.785Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:59:42.040
Product last modified at: 2024-09-30T08:00:24.926Z
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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.

STAU1 (E5Z1N) Rabbit mAb #89056

Filter:
  • WB

    Supporting Data

    REACTIVITY H Mk
    SENSITIVITY Endogenous
    MW (kDa) 63, 55
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Simple Western™ 1:50 - 1:250

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    STAU1 (E5Z1N) Rabbit mAb recognizes endogenous levels of total STAU1 protein. This antibody recognizes both the 63 kDa (Uniprot #O95793-1) and 55 kDa (Uniprot #O95793-2) isoforms of STAU1. This antibody does not cross-react with STAU2 protein.

    Species Reactivity:

    Human, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu486 of human STAU1 protein.

    Background

    Staufen is a multifunctional double-stranded RNA (dsRNA)-binding protein that was first described as a key regulator of development in early Drosophila oocytes (1). Two Staufen orthologues are expressed in mammals, Staufen1 (STAU1) and Staufen2 (STAU2). Although both proteins share some sequence similarity, they have largely distinct spatiotemporal expression patterns and cellular functions (2). 

    STAU1 is encoded by the STAU1 gene and is ubiquitously expressed in most cell and tissue types. Multiple isoforms of STAU1 have been identified due to alternative splicing, with the two predominant isoforms being STAU155 and STAU163 (3,4). STAU1 plays a key role in multiple RNA processes, including splicing, translation, targeted mRNA decay (referred to as Staufen-mediated mRNA decay or SMD), and the transport of mRNA to subcellular regions during embryonic development and differentiation (1,5-10). STAU1 also transports mRNA along neuronal dendrites, contributing to localized protein synthesis and synaptic plasticity (11,12). Indeed, STAU1-deficient mice display reduced dendritic protrusions and impaired dendritic outgrowth, resulting in fewer synapses (13). STAU1 can undergo liquid-liquid phase separation and is frequently recruited to cytoplasmic foci known as stress granules (SGs), which are ribonucleoprotein (RNP) granules formed at sites of stalled mRNA translation (14,15). STAU1 has also been found to interact with ataxin-2, another SG-associated protein that is the primary cause of spinocerebellar ataxia type 2 (SCA2) when mutated (16). Cells derived from SCA2 patients display elevated levels of STAU1 protein and colocalization between STAU1 and ataxin-2 in SG-like aggregates (16). Recruitment of STAU1 to pathological protein aggregates has also been observed in other neurological disorders, such as amyotrophic lateral sclerosis (ALS) (17). STAU1 function has additionally been implicated in several types of cancer, including prostate, colorectal, and glioma (18-20).   
    1. St Johnston, D. et al. (1991) Cell 66, 51-63.
    2. Almasi, S. and Jasmin, B.J. (2021) Cell Mol Life Sci 78, 7145-7160.
    3. Wickham, L. et al. (1999) Mol Cell Biol 19, 2220-30.
    4. Bondy-Chorney, E. et al. (2016) Rare Dis 4, e1225644.
    5. Ravel-Chapuis, A. et al. (2012) J Cell Biol 196, 699-712.
    6. Dugré-Brisson, S. et al. (2005) Nucleic Acids Res 33, 4797-812.
    7. Kim, Y.K. et al. (2005) Cell 120, 195-208.
    8. Park, E. and Maquat, L.E. (2013) Wiley Interdiscip Rev RNA 4, 423-35.
    9. Broadus, J. et al. (1998) Nature 391, 792-5.
    10. Gautrey, H. et al. (2008) Biochim Biophys Acta 1783, 1935-42.
    11. Lebeau, G. et al. (2008) Mol Cell Biol 28, 2896-907.
    12. Heraud-Farlow, J.E. and Kiebler, M.A. (2014) Trends Neurosci 37, 470-9.
    13. Vessey, J.P. et al. (2008) Proc Natl Acad Sci USA 105, 16374-9.
    14. Thomas, M.G. et al. (2005) Mol Biol Cell 16, 405-20.
    15. Thomas, M.G. et al. (2009) J Cell Sci 122, 563-73.
    16. Paul, S. et al. (2018) Nat Commun 9, 3648.
    17. Paul, S. et al. (2021) Ann Neurol 89, 1114-1128.
    18. Marcellus, K.A. et al. (2021) BMC Cancer 21, 120.
    19. Damas, N.D. et al. (2016) Nat Commun 7, 13875.
    20. Jing, F. et al. (2020) Mol Ther Oncolytics 17, 216-231.
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