You Searched For: Phosphoryl+tribromide

Catalog Number: (10368-106)

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: (77436-900)

Supplier: Bioss

Description: Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress-induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase-independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. Regulates cellular migration with alteration of PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits its activity and may regulate PXN phosphorylation through PTPN12. May act as a key regulator of axon regeneration in the optic nerve and radial nerve.

Catalog Number: (77528-326)

Supplier: AFG Bioscience

Description: Mouse pMAPT/pTAU (Phosphorylated Microtubule-Associated Protein tau) ELISA Kit

Catalog Number: (76116-708)

Supplier: Bioss

Description: Cellular localization: Nucleus. Cytoplasm. Golgi apparatus membrane. Cell membrane. Membrane > caveola. Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin (By similarity). Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments.

Catalog Number: (77511-366)

Supplier: AFG Bioscience

Description: Rat p-AMPK (Phosphorylated Adenosine Monophosphate Activated Protein Kinase) ELISA Kit

Catalog Number: (10396-376)

Supplier: Bioss

Description: Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis.

Catalog Number: (76083-854)

Supplier: Bioss

Description: Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of APC/C inhibitors, and the regulation of mitotic exit and cytokinesis. Required for recovery after DNA damage checkpoint and entry into mitosis. Required for kinetochore localization of BUB1B. Phosphorylates SGOL1. Required for spindle pole localization of isoform 3 of SGOL1 and plays a role in regulating its centriole cohesion function. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Regulates TP53 stability through phosphorylation of TOPORS. Phosphorylates NEDD1. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylates both ECT2 and RACGAP1, and thereby stimulates their interaction that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2.

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: (10081-590)

Supplier: Proteintech

Description: Three members of c-Jun N-terminal kinases (JNK), JNK1, JNK2 and JNK3, have been reported, which are distant members of the MAP kinase family. JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif during response to UV light. JNK1 functions to phosphorylate c-Jun at N-terminal serine regulatory sites of Ser-63 and Ser-73, mapping within the transactivation domain. Phosphorylation of these sites in response to UV results in transcriptional activation of c-Jun.

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: (10463-908)

Supplier: Bioss

Description: Cellular localization: Nucleus. Cytoplasm. Golgi apparatus membrane. Cell membrane. Membrane >caveola. Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin (By similarity). Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments.

Catalog Number: (10463-912)

Supplier: Bioss

Description: Cellular localization: Nucleus. Cytoplasm. Golgi apparatus membrane. Cell membrane. Membrane >caveola. Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin (By similarity). Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments.

Catalog Number: (10411-050)

Supplier: Bioss

Description: Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.

Catalog Number: (10411-006)

Supplier: Bioss

Description: Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.

Catalog Number: (10410-990)

Supplier: Bioss

Description: Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.

Catalog Number: (CAPI20307)

Supplier: Thermo Scientific

Description: Thermo Scientific Pierce p-Amino Phosphoryl Choline Agarose enables purification of C-reactive protein (CRP) from plasma, ascites and other biological fluids.

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