research use only

CDK5 Antibody [H9D2]

Cat.No.: F5053

    Application: Reactivity:

    Usage Information

    Dilution
    1:1000
    1:50
    1:200 - 1:400
    Application
    WB, IP, IF
    Reactivity
    Human, Mouse, Rat, Monkey
    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
    30 kDa
    Positive Control HeLa cells; Mouse retina; Mouse cortex; Mouse cerebellum
    Negative Control

    Datasheet & SDS

    Biological Description

    Specificity
    CDK5 (D1F7M) Rabbit mAb detects endogenous levels of total CDK5 protein.
    Clone
    H9D2
    Synonym(s)
    Cyclin-dependent kinase 5; Cell division protein kinase 5; Tau protein kinase II catalytic subunit; TPKII catalytic subunit; CDK5; CDKN5; PSSALRE
    Background
    CDK5 is a proline‑directed serine/threonine kinase of the cyclin‑dependent kinase (CDK) family that uniquely functions primarily in post‑mitotic neurons rather than in cell cycle progression. It is activated by binding neuron‑specific, non‑cyclin cofactors p35 or p39, which induce conformational changes that expose the ATP‑binding cleft and key catalytic residues such as Lys33, Glu240, and Asp145 that are essential for phosphotransfer. CDK5 adopts the canonical bilobal kinase fold, with a conserved glycine‑rich loop (G‑loop) that positions the nucleotide, an activation loop containing atypical Thr14/Tyr15 phosphorylation sites for CDKs, and binding pockets for p35/p39 that sterically displace CDK5’s autoinhibitory helix αH. CDK5–p35/p39 activity regulates neuronal migration via N‑cadherin and microtubule dynamics (for example, by phosphorylating DCX), synaptic plastic Mans‑related plasticity and LTD via AMPA receptor trafficking. calpain‑mediated cleavage of p35 to p25 deregulates CDK5, causing hyperphosphorylation of tau (at sites such as Ser202/Thr205/Ser396), APP (Thr668), and neurofilaments. This promotes neurofibrillary tangle formation, Aβ‑42 production, synaptic loss, mitochondrial dysfunction, and apoptosis in Alzheimer’s disease (AD), while also contributing to α‑synuclein aggregation in Parkinson’s disease, huntingtin‑associated pathology in Huntington’s disease, and TDP‑43 mislocalization in amyotrophic lateral sclerosis (ALS).
    References
    • https://pubmed.ncbi.nlm.nih.gov/24879856/
    • https://pubmed.ncbi.nlm.nih.gov/16407256/

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