You Searched For: Phosphoryl+tribromide

Catalog Number: (10373-542)

Supplier: Bioss

Description: Pin1 is a Peptidyl-prolyl isomerases (PPIase). Peptidyl-prolyl isomerases (PPIase) facilitate the cis-trans interconversion of the peptidyl-prolyl bond thereby affecting protein folding. Pin1 is a PPIase which specifically recognizes phosphorylated S/T-P bonds. Pin1 has been implicated in tau pathologies that underlie Alzheimer's Disease. Pin1 binds to tau phosphorylated specifically on the Thr231-Pro site and induces conformational changes in tau. Such conformational changes can directly restore the ability of phosphorylated Tau to bind microtubules and promote microtubule assembly and/or facilitate tau dephosphorylation. Pin1 expression inversely correlates with the predicted neuronal vulnerability in normally aged brain and also with actual neurofibrillary degeneration in AD brain. Pin1 could be pivotal for maintainance of normal neuronal function and preventing age-dependent neurodegeneration.

Catalog Number: (CA80016-822)

Supplier: MilliporeSigma

Description: Rabbit polyclonal antibody adsorbed against non-phosphopeptide corresponding to the immunogen phosphorylation site and a generic phosphotyrosine-containing peptide, followed by immunoaffinity chromatography. Recognizes the ~125 kDa FAK protein phosphorylated at Tyr⁸⁶¹.

Catalog Number: (10370-886)

Supplier: Bioss

Description: WNK1 controls sodium and chloride ion transport by inhibiting the activity of WNK4, potentially by either phosphorylating the kinase or via an interaction between WNK4 and the autoinhibitory domain of WNK1. WNK4 regulates the activity of the thiazide sensitive Na/Cl cotransporter, SLC12A3, by phosphorylation. WNK1 may also play a role in actin cytoskeletal reorganization.

Catalog Number: (10342-378)

Supplier: Bioss

Description: Feedback inhibitor of fibroblast growth factor mediated Ras-MAPK signaling and ERK activation. May inhibit FGF-induced FGFR1 tyrosine phosphorylation. Regulates the nuclear ERK signaling pathway by spatially blocking nuclear translocation of activated ERK without inhibiting cytoplasmic phosphorylation of ERK. Mediates JNK activation and may be involved in apoptosis.

Catalog Number: (10229-792)

Supplier: Bioss

Description: Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters. Transcription activation is enhanced by the TORC coactivators which act independently of Ser-133 phosphorylation. Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells.

Catalog Number: (10342-382)

Supplier: Bioss

Description: Feedback inhibitor of fibroblast growth factor mediated Ras-MAPK signaling and ERK activation. May inhibit FGF-induced FGFR1 tyrosine phosphorylation. Regulates the nuclear ERK signaling pathway by spatially blocking nuclear translocation of activated ERK without inhibiting cytoplasmic phosphorylation of ERK. Mediates JNK activation and may be involved in apoptosis.

Catalog Number: (76080-392)

Supplier: Bioss

Description: IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Catalog Number: (76100-796)

Supplier: Bioss

Description: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation.

Catalog Number: (10070-202)

Supplier: Prosci

Description: Signal transducer and activator of transcription that mediates signaling by interferons (IFNs). Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state.

Catalog Number: (76080-478)

Supplier: Bioss

Description: MEK5 is a dual specificity protein kinase belonging to thr Ser/Thr protein kinase family, (MAP kinase kinase family). It is activated by phosphorylation on Ser/Thr by MAP kinase kinases and interacts specifically with ERK5, and not with another MAP kinase like P38. This kinase specifically interacts with and activates MAPK7/ERK5. This kinase itself can be phosphorylated and activated by MAP3K3/MEKK3, as well as by atypical protein kinase C isoforms (aPKCs). It is not phosphorylated by RAFA, RAFB or RAFC and it may interact with GTPases such as CDC42. The signal cascade mediated by this kinase is involved in growth factor stimulated cell proliferation and muscle cell differentiation. MEK5 is expressed in many adult tissues and is most abundant in heart and skeletal muscle.

Catalog Number: (76080-474)

Supplier: Bioss

Description: MEK5 is a dual specificity protein kinase belonging to thr Ser/Thr protein kinase family, (MAP kinase kinase family). It is activated by phosphorylation on Ser/Thr by MAP kinase kinases and interacts specifically with ERK5, and not with another MAP kinase like P38. This kinase specifically interacts with and activates MAPK7/ERK5. This kinase itself can be phosphorylated and activated by MAP3K3/MEKK3, as well as by atypical protein kinase C isoforms (aPKCs). It is not phosphorylated by RAFA, RAFB or RAFC and it may interact with GTPases such as CDC42. The signal cascade mediated by this kinase is involved in growth factor stimulated cell proliferation and muscle cell differentiation. MEK5 is expressed in many adult tissues and is most abundant in heart and skeletal muscle.

Catalog Number: (89362-920)

Supplier: Genetex

Description: Tyrosine phosphorylation plays a critical role in many physiological processes. There is a fine balance between phosphorylation caused by protein tyrosine kinases and actions of protein tyrosine phosphatases, that regulates these physiological processes. Striatal enriched phosphatase (STEP) is part of a family of protein tyrosine phosphatases enriched within the CNS and is a component of the NMDAR complex. It is expressed within dopaminoceptive neurons in the CNS and particularly enriched within the basal ganglia and related structures.

Catalog Number: (10401-800)

Supplier: Bioss

Description: The Sarco(endo)plasmic-reticulum (SER) regulatory protein, Phospholamban (PLB), is a small, plasma membrane-associated protein found in the SER of cardiac, smooth and slow-twitch muscle. Believed to assemble into a pentamer, PLB regulates cardiac contractility and Ca2+ affinity for cardiac SER Ca2+ ATPase (SERCA2a). Non-phosphorylated PLB associates with SERCA2a, and inhibits Ca2+ reuptake into the SER. PLB activation occurs when key Serine/Threonine residues in PLB (Ser-10, Ser-16, Thr-17) are phosphorylated by numerous effectors, which include PKC, PKA, PKG, and CaM kinase. Phosphorylation of PLB causes dissociation from SERCA2a and a subsequent increase in the rate of Ca2+ reuptake into the SER, which accelerates ventricular relaxation.

Catalog Number: (CAPIPA5-12621)

Supplier: Thermo Scientific

Description: The protein encoded by this gene is a member of the serine/threonine kinase family. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. In vitro, this kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites.

Catalog Number: (76077-836)

Supplier: Bioss

Description: The protein encoded by this gene belongs to the protein phosphatase 1 (PP1) inhibitor family. This protein is an inhibitor of smooth muscle myosin phosphatase, and has higher inhibitory activity when phosphorylated. Inhibition of myosin phosphatase leads to increased myosin phosphorylation and enhanced smooth muscle contraction. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene.

Catalog Number: (10370-868)

Supplier: Bioss

Description: Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity. May phosphorylate ATG13/KIAA652 and RPTOR; however such data need additional evidences. Plays a role early in neuronal differentiation and is required for granule cell axon formation.