You Searched For: Phosphoryl+tribromide

Catalog Number: (BOSSBS-0908R-CY3)

Supplier: Bioss

Description: Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-0908R-CY7)

Supplier: Bioss

Description: Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-3353R-A647)

Supplier: Bioss

Description: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-13038R-A350)

Supplier: Bioss

Description: Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-4166R-FITC)

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.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-10726R-HRP)

Supplier: Bioss

Description: Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Interacts with cyclins A, B1, B3, D, or E. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-3345R-A488)

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.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-3345R-HRP)

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.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-12567R-CY7)

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.This antibody recognise the phosphorylation site of human Ser75, mouse Ser111, rat Ser112.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-7523R-CY3)

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.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-7523R-CY5)

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.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-13651R)

Supplier: Bioss

Description: APS (adapter molecule containing PH and SH2 domains), SH2-B and Lnk compose a family of adapter proteins, which contain a pleckstrin homology (PH) domain, an SH2 domain and a tyrosine phosphorylation site. Stimulation of B cell receptor (BCR) or T cell receptor (TCR) results in the phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of BCR, TCR and several substrates. APS, SH2-B and Lnk may bind to the ITAM domain of BCR and TCR. Lnk is tyrosine phosphorylated in response to TCR stimulation and APS has been shown to be tyrosine phosphorylated in response to BCR stimulation.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-13651R-FITC)

Supplier: Bioss

Description: APS (adapter molecule containing PH and SH2 domains), SH2-B and Lnk compose a family of adapter proteins, which contain a pleckstrin homology (PH) domain, an SH2 domain and a tyrosine phosphorylation site. Stimulation of B cell receptor (BCR) or T cell receptor (TCR) results in the phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of BCR, TCR and several substrates. APS, SH2-B and Lnk may bind to the ITAM domain of BCR and TCR. Lnk is tyrosine phosphorylated in response to TCR stimulation and APS has been shown to be tyrosine phosphorylated in response to BCR stimulation.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-13651R-A350)

Supplier: Bioss

Description: APS (adapter molecule containing PH and SH2 domains), SH2-B and Lnk compose a family of adapter proteins, which contain a pleckstrin homology (PH) domain, an SH2 domain and a tyrosine phosphorylation site. Stimulation of B cell receptor (BCR) or T cell receptor (TCR) results in the phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of BCR, TCR and several substrates. APS, SH2-B and Lnk may bind to the ITAM domain of BCR and TCR. Lnk is tyrosine phosphorylated in response to TCR stimulation and APS has been shown to be tyrosine phosphorylated in response to BCR stimulation.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-13651R-A680)

Supplier: Bioss

Description: APS (adapter molecule containing PH and SH2 domains), SH2-B and Lnk compose a family of adapter proteins, which contain a pleckstrin homology (PH) domain, an SH2 domain and a tyrosine phosphorylation site. Stimulation of B cell receptor (BCR) or T cell receptor (TCR) results in the phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of BCR, TCR and several substrates. APS, SH2-B and Lnk may bind to the ITAM domain of BCR and TCR. Lnk is tyrosine phosphorylated in response to TCR stimulation and APS has been shown to be tyrosine phosphorylated in response to BCR stimulation.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-5487R-A555)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Sale