You Searched For: Phosphoryl+tribromide

Catalog Number: (10408-508)

Supplier: Bioss

Description: This protein phosphatase specifically mediates the dephosphorylation of mitochondrial proteins and consequently plays a central role in ATP production. It probably has a preference for proteins phosphorylated on Ser and/or Thr residues compared to phosphorylation on Tyr residues. It is likely to be involved in the regulation of insulin secretion in pancreatic beta cells.

Catalog Number: (76081-044)

Supplier: Bioss

Description: Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP25 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC8. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC2 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGOL1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Isoform 1 phosphorylates and activates NEK11 in G1/S-arrested cells. Isoform 2, which is not present in the nucleolus, does not.

Catalog Number: (CAPIPA5-12552)

Supplier: Thermo Scientific

Description: Bad is a member of the BCL-2 family. BCL-2 family members are known to be regulators of programmed cell death. This protein positively regulates cell apoptosis by forming heterodimers with BCL-xL and BCL-2, and reversing their death repressor activity. Proapoptotic activity of this protein is regulated through its phosphorylation. Protein kinases AKT and MAP kinase, as well as protein phosphatase calcineurin are found to be involved in the regulation of this protein. Bad is phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-99 or Ser-75 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-118, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118 the major site of protein kinase A (CAPK) phosphorylation.

Catalog Number: (10068-838)

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. As part of the non-canonical pathway of NF-κ-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-κ-B RelB-p52 complexes. Also phosphorylates NCOA3. Phosphorylates 'Ser-10' of histone H3 at NF-κ-B-regulated promoters during inflammatory responses triggered by cytokines.

Catalog Number: (CA600-401-345)

Supplier: Rockland Immunochemical

Description: This phospho specific polyclonal antibody was tested by ELISA.  Data from ELISA indicates the antibody is reactive with the phosphorylated form of the immunizing peptide and minimally reactive with the non-phosphorylated form of the immunizing peptide. No

Catalog Number: (76078-232)

Supplier: Bioss

Description: Binds VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Binding to Reelin induces tyrosine phosphorylation of Dab1 and modulation of Tau phosphorylation (By similarity).

Catalog Number: (10084-036)

Supplier: Proteintech

Description: Calcium/calmodulin-dependent protein kinase kinase 1 catalyzes the phosphorylation and activation of Ca(2+)/calmodulin kinase (CaMK) as an upstream component of the CaMK cascade that has been implicated in neuronal gene transcription, synaptic plasticity, and long-term memory consolidation .CAMKK1 has two isoforms of 56kda and 58kda and involved in regulating cell apoptosis, promotes cell survival by phosphorylating AKT1/PKB that inhibits pro-apoptotic BAD/Bcl2-antagonist of cell death .Researches showed that Camkk1 plays a selective role in contextual fear memory.This 66-68kda protein can be phosphorylated(probably antophosphorylation).This antibody recognize the N-terminal of CAMKK1 .

Catalog Number: (10346-582)

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: (76083-908)

Supplier: Bioss

Description: Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4).

Catalog Number: (77437-560)

Supplier: Bioss

Description: Serine/threonine-protein kinase involved in variousprocesses such as cell cycle regulation, gluconeogenesis andlipogenesis regulation, muscle growth and differentiation and tumorsuppression. Phosphorylates HDAC4, HDAC5, PPME1, SREBF1,TORC1/CRTC1 and TORC2/CRTC2. Acts as a tumor suppressor and plays akey role in p53/TP53-dependent anoikis, a type of apoptosistriggered by cell detachment: required for phosphorylation ofp53/TP53 in response to loss of adhesion and is able to suppressmetastasis. Part of a sodium-sensing signaling network, probably bymediating phosphorylation of PPME1: following increases inintracellular sodium, SIK1 is activated by CaMK1 and phosphorylatesPPME1 subunit of protein phosphatase 2A (PP2A), leading todephosphorylation of sodium/potassium-transporting ATPase ATP1A1and subsequent increase activity of ATP1A1. Acts as a regulator ofmuscle cells by phosphorylating and inhibiting class II histonedeacetylases HDAC4 and HDAC5, leading to promote expression of MEF2target genes in myocytes. Also required during cardiomyogenesis byregulating the exit of cardiomyoblasts from the cell cycle viadown-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepaticgluconeogenesis by phosphorylating and repressing the CREB-specificcoactivators TORC1/CRTC1 and TORC2/CRTC2, leading to inhibit CREBactivity. Also regulates hepatic lipogenesis by phosphorylating andinhibiting SREBF1.

Catalog Number: (10373-540)

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: (10370-272)

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: (CAPIPA5-15527)

Supplier: Thermo Scientific

Description: Phosphorylation of receptors by protein kinases is a process that can be reversed by a group of enzymes called protein phosphatases. Coordinated control of kinases and phosphatases provides the cell with the capacity to rapidly switch between phosphorylated and dephosphorylated protein states in dynamic response to environmental stimuli. Activation of critical enzymes by kinase phosphorylation alone is not enough to provide adequate regulation ?it is the combination with phosphatase dephosphorylation that effectively creates on/off switches to control cellular events. Errors in control, either through kinases or their counterpart phosphatases, can lead to unchecked cell growth attributable to human cancers and developmental disorders. Potential mechanisms to control dephosphorylation include changes in the expression of protein phosphatases, their subcellular localization, phosphorylation of phosphatase catalytic and regulatory subunits and regulation by endogenous phosphatase inhibitors. Most protein phosphatases are not stringently specific for their substrates. Consequently, changes in phosphatase activity may have a broad impact on dephosphorylation and turnover of phosphoproteins that are substrates for different kinases. This may be an important point of control to connect cellular circuitry of interrelated signaling pathways, and to synchronize physiological responses.

Catalog Number: (10411-028)

Supplier: Bioss

Description: Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation.

Catalog Number: (10411-014)

Supplier: Bioss

Description: Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation.

Catalog Number: (10346-584)

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.