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Dynein intermediate chain 1/DNAI1 Antibody [E1A7]

Cat.No.: F3995

    Application: Reactivity:
    • F3995-wb
      Lane 1: Human testis, Lane 2: Rat testis, Lane 3: Mouse testis

    Usage Information

    Dilution
    1:2000
    1:50 - 1:100
    Application
    WB, IF
    Reactivity
    Mouse, Rat, Human
    Source
    Rabbit Monoclonal Antibody
    Storage Buffer
    PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3
    Storage (from the date of receipt)
    -20°C (avoid freeze-thaw cycles), 2 years
    Predicted MW Observed MW
    79 kDa 79 kDa
    *Why do the predicted and actual molecular weights differ?
    The following reasons may explain differences between the predicted and actual protein molecular weight.
    Positive Control Human testis tissue; Rat testis tissue; Mouse testis tissue; Jurkat cells; F9 cells
    Negative Control

    Datasheet & SDS

    Biological Description

    Specificity
    Dynein intermediate chain 1/DNAI1 Antibody [E1A7] detects endogenous levels of total Dynein intermediate chain 1/DNAI1 protein.
    Clone
    E1A7
    Synonym(s)
    Dynein axonemal intermediate chain 1; Axonemal dynein intermediate chain 1; DNAI1
    Background
    Dynein intermediate chain 1 (DNAI1) is a WD-repeat protein that forms the structural base of outer dynein arms (ODAs) in motile cilia axonemes, assembling with heavy chains like DNAH5 and DNAH11 and various light chains. It features seven conserved WD40 propeller blades that undergo helical folding upon binding LC8 light chains, supporting microtubule attachment, while its flexible N-terminal domain coordinates cargo adaptor recruitment necessary for force generation during ATP-driven sliding between A/B tubule doublets. DNAI1 anchors ODAs at specific intervals along the axoneme perimeter, enabling coordinated power and recovery strokes required for mucociliary clearance in respiratory epithelia and for sperm flagellar propulsion. ODA assembly is mediated by intraflagellar transport, and DNAI1 mutations can disrupt ODA docking, resulting in static or immotile cilia with normal ultrastructure except for missing ODAs. Through DNAI1-LC8 interactions, conformational changes are transmitted from heavy chain AAA+ rings to microtubule-binding domains, regulating sliding velocity and displacement and preventing axonemal collapse. Disease-associated truncations that destabilize the WD40 propeller structure lead to primary ciliary dyskinesia (PCD), including Kartagener syndrome, which is characterized by situs inversus, neonatal respiratory distress, chronic rhinosinusitis, bronchiectasis, and male infertility due to impaired sperm motility.
    References
    • https://pubmed.ncbi.nlm.nih.gov/33957056/
    • https://pubmed.ncbi.nlm.nih.gov/11231901/

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