• Mouse PDPK1 (Phosphoinositide Dependent Protein Kinase 1) Sandwich ELISA Kit Ready-To-Use (STJE0017773)

Mouse PDPK1 (Phosphoinositide Dependent Protein Kinase 1) Sandwich ELISA Kit Ready-To-Use (STJE0017773)

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STJE0017773

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Applications: ELISA
Reactivity: Mouse
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Sensitivity: 0.055ng/mL
Detection Limit: 0.156-10ng/mL
Short Description: This PDPK1 Sandwich ELISA Kit, Ready-To-Use is an in-vitro enzyme-linked immunosorbent assay for the measurement of samples in mouse cell culture supernatant, serum and plasma (EDTA, citrate, heparin).
Storage Instruction: The whole kit may be stored at-20°C for up to 12 months from receipt. An unopened kit may be stored in the fridge at 2-8°C for up to 6 months. Once opened store individual kit contents according to components table provided with the kit.
Assay Time: 3 hrs
Gene Symbol: Pdpk1
Gene ID: 18607
Uniprot ID: PDPK1_MOUSE
Immunogen Region: Ready-To-Use
Sample Type: tissue homogenates, cell lysates or other biological fluids.
Tissue Specificity Highly expressed in heart, brain, liver and testis, also expressed in embryonic cells.
Post Translational Modifications Phosphorylation on Ser-244 in the activation loop is required for full activity. PDPK1 itself can autophosphorylate Ser-244, leading to its own activation. Autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2. Tyr-9 phosphorylation is critical for stabilization of both PDPK1 and the PDPK1/SRC complex via HSP90-mediated protection of PDPK1 degradation. Angiotensin II stimulates the tyrosine phosphorylation of PDPK1 in vascular smooth muscle in a calcium- and SRC-dependent manner. Phosphorylated on Tyr-9, Tyr-376 and Tyr-379 by INSR in response to insulin. Palmitate negatively regulates autophosphorylation at Ser-244 and palmitate-induced phosphorylation at Ser-532 and Ser-504 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylation at Thr-357 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-397 and Ser-401 by MAP3K5. Monoubiquitinated in the kinase domain, deubiquitinated by USP4.
Function Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages.
Protein Name 3-Phosphoinositide-Dependent Protein Kinase 1
Mpdk1
Database Links Reactome: R-MMU-114604
Reactome: -MMU-1257604
Reactome: -MMU-165158
Reactome: -MMU-202424
Reactome: -MMU-2730905
Reactome: -MMU-2871837
Reactome: -MMU-354192
Reactome: -MMU-389357
Reactome: -MMU-392451
Reactome: -MMU-5218920
Reactome: -MMU-5218921
Reactome: -MMU-5607764
Reactome: -MMU-5625740
Reactome: -MMU-6804757
Reactome: -MMU-9634635
Cellular Localisation Cytoplasm
Nucleus
Cell Membrane
Peripheral Membrane Protein
Cell Junction
Focal Adhesion
Tyrosine Phosphorylation Seems To Occur Only At The Cell Membrane
Translocates To The Cell Membrane Following Insulin Stimulation By A Mechanism That Involves Binding To Grb14 And Insr
Src And Hsp90 Promote Its Localization To The Cell Membrane
Its Nuclear Localization Is Dependent On Its Association With Ptpn6 And Its Phosphorylation At Ser-396
Restricted To The Nucleus In Neuronal Cells While In Non-Neuronal Cells It Is Found In The Cytoplasm
The Ser-244 Phosphorylated Form Is Distributed Along The Perinuclear Region In Neuronal Cells While In Non-Neuronal Cells It Is Found In Both The Nucleus And The Cytoplasm
Igf1 Transiently Increases Phosphorylation At Ser-241 Of Neuronal Pdpk1
Resulting In Its Translocation To Other Cellular Compartments
The Tyrosine-Phosphorylated Form Colocalizes With Ptk2b In Focal Adhesions After Angiotensin Ii Stimulation
Alternative ELISA Names 3-Phosphoinositide-Dependent Protein Kinase 1 ELISA kit
Mpdk1 ELISA kit
Pdpk1 ELISA kit
Pdk1 ELISA kit
output

Information sourced from Uniprot.org

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