research use only
Cat.No.: F5053
| Dilution |
|---|
|
| 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 |
| 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 |
|---|
|
Tel: +1-832-582-8158 Ext:3
If you have any other enquiries, please leave a message.