You Searched For: Phosphoryl+tribromide

Catalog Number: (89362-770)

Supplier: Genetex

Description: Akt (Protein Kinase B, PKB) is a key regulator of many signal transduction pathways (reviewed in ref 1). Its tight control over cell proliferation and cell viability are manifold; overexpression or inappropriate activation of Akt has been seen in many types of cancer. Akt mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits Akt to the membrane, where it is activated by PDK1 phosphorylation (reviewed in 2). Once phosphorylated, Akt dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. Akt has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation.

Catalog Number: (10352-432)

Supplier: Bioss

Description: OXSR1 is a serine/threonine kinase which regulates downstream kinases in response to environmental stress such as osmotic stresses, notably sorbitol and, to a lesser extent, NaCl. OXSR1 phosphorylated thr84 within the N-terminal regulatory domain of PAK1. Replacement of thr84 with gln reduced activation of PAK1 by an active form of the small G protein CDC42, suggesting that phosphorylation by OXSR1 modulates the G protein sensitivity of PAK. OXSR1 interacts with chloride channel proteins SLC12A6 isoform 2, SLC12A1 and SLC12A2 but not with SLC12A4 and SLC12A7, possibly establishing sensor/signaling modules that initiate the cellular response to environmental stress. Binds to and phosphorylates RELL1, RELL2 AND RELT. OXSR1 may have a role in regulating the actin cytoskeleton.

Catalog Number: (10411-270)

Supplier: Bioss

Description: Cell cycle progression is regulated by cyclins and their cognate Cdks. p27 KIP 1 is a cell cycle regulatory mitotic inhibitor of cdk activity. p27 KIP 1 is a candidate tumor suppressor gene, and has been proposed to function as a possible mediator of TGF beta induced G1 arrest. p27 KIP 1 is up regulated in response to antimitogenic stimuli. The increased protein expression of p27 results in cellular arrest by binding to cyclin/Cdk complexes such as cyclin D1/Cdk4. p27 Kip1 is regulated by phosphorylation on serine 10 (S10) and threonine 187 (T187). Phosphorylation by CDK2 on T187 results in ubiquitylation and degradation of p27 Kip 1; while phosphorylation by hKIS on S10 signals the nuclear export to the cytoplasm.

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: (10416-780)

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.

Catalog Number: (10463-892)

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: (10463-914)

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: (76079-966)

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: (10410-978)

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: (10410-980)

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: (10410-984)

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: (10349-958)

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: (10349-944)

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: (10352-176)

Supplier: Bioss

Description: Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine FLT3LG and regulates differentiation, proliferation and survival of hematopoietic progenitor cells and of dendritic cells. Promotes phosphorylation of SHC1 and AKT1, and activation of the downstream effector MTOR. Promotes activation of RAS signaling and phosphorylation of downstream kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation of FES, FER, PTPN6/SHP, PTPN11/SHP-2, PLCG1, and STAT5A and/or STAT5B. Activation of wild-type FLT3 causes only marginal activation of STAT5A or STAT5B. Mutations that cause constitutive kinase activity promote cell proliferation and resistance to apoptosis via the activation of multiple signaling pathways.

Catalog Number: (76082-214)

Supplier: Bioss

Description: MSK1 is a mitogen and stress activated protein kinase 1 which belongs to the AGC family of kinases and is related in structure to the ribosomal p70 S6 kinase subfamily. MSK1 can be activated by ERK1/2 and SAPK2/p38 MAP kinase. It is also known to be required for the phosphorylation of CREB, ATF1 H3 and HMG14 in response to mitogen and stress. Similar to RSK, MSK1 contains two kinase domains (N term and a C term). Once phosphorylated on Thr581 and Ser360 by ERK1/2 and SAPK2/p38, MSK1 autophosphorylate on at least 5 sites. Of these autophosphorylation sites Ser212 and Ser376 get phosphorylated by the C terminal kinase domain of MSK1 which is essential for the catalytic activity of the N terminal kinase domain.