You Searched For: phosphoryle

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.

Supplier: Ambeed

Description: 3-(Hydroxy(phenyl)phosphoryl)propanoic acid, Purity: 97%, CAS number: 14657-64-8, Appearance: Form: Crystal - Powder / Colour: White - Almost white, Storage: Sealed in dry, 2-8C, Size: 500G

Supplier: Sino Biological

Description: Recombinant full length human Alpha-synuclein was expressed in <i>E. coli </i>cells using an N-terminal His tag and was phosphorylated by co-expression with PLK2 <i>in vivo</i>.

New Product

Catalog Number: (89161-030)

Supplier: Enzo Life Sciences

Description: This peptide sequence, KKKVSRSGLYRSPSMPENLNRPR, corresponds to amino acids 206-225 of the phosphatase CDC25C, which is a phosphorylation target of Chk1 on Ser216. The addition of three N-terminal lysines allows the peptide to be used in phosphocellulose kinase assays. Both Chk1 and Chk2 will phosphorylate this peptide.

Catalog Number: (10294-298)

Supplier: Bioss

Description: Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK4/MAPK4 is phosphorylated at Ser-186 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK4/MAPK4. May promote entry in the cell cycle (By similarity).

Supplier: VWR

Description: One of the best general-purpose buffers for biological research. Excellent for tissue culture, oxidative phosphorylation, protein synthesis with cell-free bacterial systems, photophosphorylation, and CO₂ fixation.

SDS Certificates

Catalog Number: (76545-514)

Supplier: BIOASSAY SYSTEMS

Description: Determination of AKT1(S473) phosphorylation status in whole cells and evaluation of pathway modulation by activators, inhibitors, siRNA etc.

Catalog Number: (10416-776)

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: (10358-850)

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.

Catalog Number: (89155-886)

Supplier: Enzo Life Sciences

Description: This kit offers a set of seven different MAbs specific for tyrosine phosphorylation sites. Phosphorylation patterns in a given cell extract may differ when probed with different antibodies due to sequence specificity. Recognition therefore depends on two criteria: Phosphorylation and surrounding aa motif. If one of the two criteria is not fulfilled, the antibody will not detect the phosphorylation site. Specificity has been determined by epitope mapping using degenerated phosphopeptide libraries.

Catalog Number: (10071-822)

Supplier: Prosci

Description: RPS6KB1 phosphorylates the Ribosomal Protein-S6. Activation of RPS6KB1 requires a complex, ordered series of conformational changes and phosphorylation reactions. While the role of sequential, multi-site phosphorylation has been extensively detailed, characterization of the priming step required to initiate this cascade has remained elusive. Probably this priming process is dependent on calcium. Calcium-dependent regulation of RPS6KB1 does not specifically target Thr-229 and Thr-389, the key regulatory phosphorylation sites; rather, calcium chelation results in a global inhibition of RPS6KB1 phosphorylation. The initial calcium-dependent process is required to release an inhibitory interaction between the C- and N-termini of RPS6KB1, thus allowing phosphorylation of key domains. The priming event involves formation of a calcium-dependent protein complex that releases the interaction between the N- and C-termini. RPS6KB1 is then accessible for activation by the kinases that target the known regulatory phosphorylation sites.

Catalog Number: (RL600-401-270)

Supplier: Rockland Immunochemical

Description: Anti-CREB pS133 antibody reacts with phosphorylated human CREB at pS133 and shows minimal reactivity by western blot with non-phosphorylated CREB and minimal reactivity (1%) by ELISA against the non-phosphorylated form of the immunizing peptide.

Catalog Number: (10070-040)

Supplier: Prosci

Description: Required for checkpoint mediated cell cycle arrest in response to DNA damage or the presence of unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A. Inhibition of CDC25 activity leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. Binds to and phosphorylates RAD51 at 'Thr-309', which may enhance the association of RAD51 with chromatin and promote DNA repair by homologous recombination. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may affect chromatin assembly during S phase or DNA repair. May also phosphorylate multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and enhances suppression of cellular proliferation.

Catalog Number: (10071-888)

Supplier: Prosci

Description: Kinase subunit of both mTORC1 and mTORC2, which regulate cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Amino-acid-signaling to mTORC1 is mediated by Rag GTPases, which cause amino-acid-induced relocalization of mTOR within the endomembrane system. Growth factor-stimulated mTORC1 activation involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-421', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.

Catalog Number: (10068-896)

Supplier: Prosci

Description: Kinase subunit of both mTORC1 and mTORC2, which regulate cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Amino-acid-signaling to mTORC1 is mediated by Rag GTPases, which cause amino-acid-induced relocalization of mTOR within the endomembrane system. Growth factor-stimulated mTORC1 activation involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-421', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.

Catalog Number: (10323-736)

Supplier: Bioss

Description: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation.