You Searched For: Phosphoryl+tribromide

Catalog Number: (10342-252)

Supplier: Bioss

Description: Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK1/JNK3. In turn, MAPK1/JNK3 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. Plays regulatory roles in the signaling pathways during neuronal apoptosis. Phosphorylates the neuronal microtubule regulator STMN2. Acts in the regulation of the beta-amyloid precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons.

Catalog Number: (10417-334)

Supplier: Bioss

Description: PDK1 (3 Phosphoinositide Dependent Protein Kinase 1) phosphorylates AGC kinases. PDK1 activates conventional PKC and PKC zeta through phosphorylation of critical threonine residues in the activation loop. PDK1 also phosphorylates Protein Kinase B (PKB) at threonine 308 in the presence of phosphatidylinositol-3,4,5-trisphosphate. Active Akt inactivates Glycogen Synthase Kinase 3 (GSK3), eventually leading to the dephosphorylation and activation of glycogen synthase and the stimulation of glycogen synthesis. Because of the role that PDK plays in insulin-induced glycogen synthesis and PKC activation it is a potentially important target for metabolic drug research. There are three named isoforms.

Catalog Number: (10417-336)

Supplier: Bioss

Description: PDK1 (3 Phosphoinositide Dependent Protein Kinase 1) phosphorylates AGC kinases. PDK1 activates conventional PKC and PKC zeta through phosphorylation of critical threonine residues in the activation loop. PDK1 also phosphorylates Protein Kinase B (PKB) at threonine 308 in the presence of phosphatidylinositol-3,4,5-trisphosphate. Active Akt inactivates Glycogen Synthase Kinase 3 (GSK3), eventually leading to the dephosphorylation and activation of glycogen synthase and the stimulation of glycogen synthesis. Because of the role that PDK plays in insulin-induced glycogen synthesis and PKC activation it is a potentially important target for metabolic drug research. There are three named isoforms.

Catalog Number: (10421-080)

Supplier: Bioss

Description: Rsk1 is a member of a family of 90kDa ribosomal protein S6 kinases, which includes Rsk1, Rsk2 and Rsk3. These are broadly expressed serine/threonine protein kinases activated in response to mitogenic stimuli, including extracellular signal regulated protein kinases Erk1 and Erk2. Rsk1 is activated by MAPK in vitro and in vivo via phosphorylation. Active Rsks appear to play a major role in transcriptional regulation by translocating to the nucleus and phosphorylating c Fos and CREB.

Catalog Number: (10421-074)

Supplier: Bioss

Description: Rsk1 is a member of a family of 90kDa ribosomal protein S6 kinases, which includes Rsk1, Rsk2 and Rsk3. These are broadly expressed serine/threonine protein kinases activated in response to mitogenic stimuli, including extracellular signal regulated protein kinases Erk1 and Erk2. Rsk1 is activated by MAPK in vitro and in vivo via phosphorylation. Active Rsks appear to play a major role in transcriptional regulation by translocating to the nucleus and phosphorylating c Fos and CREB.

Catalog Number: (10421-072)

Supplier: Bioss

Description: Rsk1 is a member of a family of 90kDa ribosomal protein S6 kinases, which includes Rsk1, Rsk2 and Rsk3. These are broadly expressed serine/threonine protein kinases activated in response to mitogenic stimuli, including extracellular signal regulated protein kinases Erk1 and Erk2. Rsk1 is activated by MAPK in vitro and in vivo via phosphorylation. Active Rsks appear to play a major role in transcriptional regulation by translocating to the nucleus and phosphorylating c Fos and CREB.

Catalog Number: (10374-896)

Supplier: Bioss

Description: PLK1 (polo-like kinase 1) is a member of the serine/threonine protein kinase family, cdc5/polo subfamily. PLK1 contains two polo box domains with a predicted molecular weight of 68 kDa. PLK1 has been shown to regulate cdc2/cyclin B through phosphorylation and activation of cdc25c phosphatase. PLK1 is modified by phosphorylation at Threonine 210. PLK1 may also be required for cell division. Depletion of PLK1 results in apoptosis and deregulation of expression of PKL1 is correlated with development of many malignancies.

Catalog Number: (10107-600)

Supplier: Prosci

Description: Epithelial cell cadherin is endocytosed as a consequence of tyrosine phosphorylation and ubiquitination. CBLL1 is an E3 ubiquitin ligase that mediates ubiquitination of the CDH1 complex.Epithelial cell cadherin (CDH1; MIM 192090) is endocytosed as a consequence of tyrosine phosphorylation and ubiquitination. HAKAI is an E3 ubiquitin ligase (see UBE3A; MIM 601623) that mediates ubiquitination of the CDH1 complex.

Catalog Number: (10069-028)

Supplier: Prosci

Description: Acts as part of the IKK complex in the conventional pathway of NF-κ-B activation and phosphorylates inhibitors of NF-κ-B thus leading to the dissociation of the inhibitor/NF-κ-B complex and ultimately the degradation of the inhibitor. Also phosphorylates NCOA3.

Catalog Number: (10071-198)

Supplier: Prosci

Description: FUNCTION: beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.
DISEASE: Polymorphic forms of ADRB2 could impart some form of nocturnal asthma.
SUBUNIT: Binds SLC9A3R1.
PTM: Phosphorylated by PKA and BARK; mediate homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK

Catalog Number: (89358-948)

Supplier: Genetex

Description: The Akt family of serine/threonine protein kinases (also called protein kinase B/PKB) plays a key role in insulin signaling, cellular survival, and transformation. Akt1 is activated by phosphorylation on residues threonine 308 and Serine 473. Thr308, in the catalytic domain, is phosphorylated by the protein kinase PDK1, and Ser473, in the COOH-terminal regulatory domain, is phosphorylated by putative serine 473 kinase. To date, a couple of proteins have been shown to physically interact with PKB.

Catalog Number: (89360-602)

Supplier: Genetex

Description: c-Jun amino terminal kinases (JNKs) are MAP kinase family members that differ from other MAP kinases in that they are phosphorylated at the Thr-Pro-Tyr phosphorylation motif instead of the characteristic MAP kinase Thr-Glu-Tyr motif. JNK2 (p54a, SAPK1a), along with JNK1 and JNK3, is thought to play an important role in nuclear signal transduction through its environmental stress activation and subsequent phosphorylation of the nuclear transcription factor p53.

Catalog Number: (76082-308)

Supplier: Bioss

Description: IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1). Inhibits viral replication via phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (EIF2S1), this phosphorylation impairs the recycling of EIF2S1 between successive rounds of initiation leading to inhibition of translation which eventually results in shutdown of cellular and viral protein synthesis. Also phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation. Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding proinflammatory cytokines and IFNs. Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6. Can act as both a positive and negative regulator of the insulin signaling pathway (ISP). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2).

Catalog Number: (10813-822)

Supplier: Prosci

Description: Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation.

Catalog Number: (89141-430)

Supplier: Enzo Life Sciences

Description: The mTOR (mammalian target of rapamycin) pathway coordinates nutrient signals with growth factor dependent signaling. mTOR is organized in two independent protein complexes, mTORC1 and mTORC2. The mTORC1 complex containing mTOR, GβL/mLST8 and Raptor is sensitive to rapamycin, while the mTORC2 complex containing mTOR, GβL/mLST8, SIN1, and Rictor is rapamycin insensitive. The mTOR/Rictor complex phosphorylates numerous substrates associated with regulation of the actin cytoskeleton, and is also responsible for phosphorylation of Akt/PKB at Ser473, a critical step in Akt activation.

Catalog Number: (89155-884)

Supplier: Enzo Life Sciences

Description: This kit offers a set of three different monoclonal antibodies specific for threonine phosphorylation sites.