Recombinant Human STEP / PTPN5 protein is a Human Full Length protein, in the 1 to 565 aa range, expressed in Wheat germ and suitable for SDS-PAGE, ELISA, WB.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
May regulate the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs, Src family kinases and NMDA receptors.
Tyrosine-protein phosphatase non-receptor type 5, Neural-specific protein-tyrosine phosphatase, Striatum-enriched protein-tyrosine phosphatase, STEP, PTPN5
Recombinant Human STEP / PTPN5 protein is a Human Full Length protein, in the 1 to 565 aa range, expressed in Wheat germ and suitable for SDS-PAGE, ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
May regulate the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs, Src family kinases and NMDA receptors.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily.
Phosphorylation at Ser-245 by PKA deactivates PTPN5. Phosphorylation at Thr-255 and Ser-268 by MAPKs stabilizes the phosphatase, dephosphorylation of these sites results in ubiquitin-mediated degradation of the active phosphatase.
STEP also known as PTPN5 is a protein tyrosine phosphatase with a molecular mass approximately 69-80 kDa. It regulates the activity of key signaling proteins by dephosphorylation. Expression of STEP occurs mainly in the central nervous system particularly in the striatum hippocampus and cortex regions of the brain. These areas of expression suggest its significant role in neuronal signaling and function. STEP exists in multiple isoforms which allow it to participate in various signaling pathways by altering substrate specificity.
STEP plays a significant role in modulating synaptic strength and plasticity acting as a negative regulator of synaptic signaling. Its main function involves dephosphorylating several kinase substrates like ERK1/2 and Fyn kinase thereby reducing their activity. This action controls synaptic sensitivity to neurotransmitters and impacts long-term potentiation a process essential for learning and memory. STEP does not form part of a large complex but interacts with other proteins through transient associations based on cellular needs.
STEP contributes significantly to the glutamatergic and dopaminergic signaling pathways. Within these pathways STEP dephosphorylates and inactivates specific receptors and kinases to maintain homeostasis in neuronal signaling. For example in the glutamatergic pathway STEP deactivates NMDA receptors affecting calcium influx and signaling cascades that rely on it. Its interactions with other proteins like ERK which is part of the MAPK pathway illustrate its integrated role in signal transduction cascades that influence cellular responses to neurotransmitters.
STEP has a relationship with neurodegenerative diseases such as Alzheimer's disease and schizophrenia. Increased activity of STEP leads to excessive dephosphorylation of proteins necessary for synaptic function contributing to the cognitive deficits observed in these disorders. In Alzheimer's disease for instance hyperactive STEP decreases the phosphorylation of the NMDA receptor and disrupts synaptic transmission. Additionally STEP's influence extends to dynamin-related protein 1 (Drp1) in neurodegenerative pathways indicating how altered STEP activity can escalate mitochondrial dysfunction commonly seen in Alzheimer's pathology.
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12.5% SDS-PAGE analysis of ab132095 stained with Coomassie Blue.
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