You Searched For: Phosphoryl+tribromide

Catalog Number: (76082-896)

Supplier: Bioss

Description: Non-receptor tyrosine kinase involved in various processes such as cell growth, development, or differentiation. Mediates essential signaling events in both innate and adaptive immunity and plays a crucial role in hematopoiesis during T-cells development. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors sharing the common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. 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, upon IL2R activation by IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits inducing the tyrosine phosphorylation of both receptor subunits on their cytoplasmic domain. Then, STAT5A AND STAT5B are recruited, phosphorylated and activated by JAK1 and JAK3. Once activated, dimerized STAT5 translocates to the nucleus and promotes the transcription of specific target genes in a cytokine-specific fashion.

Catalog Number: (10349-706)

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. MSK2 plays an essential role in the control of RELA transcriptional activity in response to TNF. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors.

Catalog Number: (10337-120)

Supplier: Bioss

Description: Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7. Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.

Catalog Number: (10751-288)

Supplier: Prosci

Description: DYRK2 Antibody: DYRK2 is a member of the dual-specificity tyrosine phosphorylation-regulated kinase (DYRK) family that is thought to be involved in cellular proliferation and apoptosis. Under normal conditions, nuclear but not cytoplasmic DYRK2 is ubiquitinated by MDM2, leading to its constitutive degradation. However, upon exposure to genotoxic stress, ATM phosphorylates DYRK2, leading to its dissociation from MDM2 and its phosphorylation of p53, thereby inducing apoptosis. Recent evidence also suggests that DYRK2 may serve as a scaffold that facilitates assembly of an E3 ubiquitin ligase.

Catalog Number: (10093-330)

Supplier: Proteintech

Description: RPTOR, also named as KIAA1303 and RAPTOR Belongs to the WD repeat RAPTOR family. It is involved in the control of the mammalian target of rapamycin complex 1 (mTORC1) activity which regulates cell growth and survival, and autophagy in response to nutrient and hormonal signals; functions as a scaffold for recruiting mTORC1 substrates. 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. 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-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. The antibody is specific to RPTOR.

Catalog Number: (10386-276)

Supplier: Bioss

Description: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K7/MKK7, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The phosphorylation of the Thr residue by MAP2K7/MKK7 seems to be the prerequisite for JNK activation at least in response to proinflammatory cytokines, while other stimuli activate both MAP2K4/MKK4 and MAP2K7/MKK7 which synergistically phosphorylate JNKs. MAP2K4 is required for maintaining peripheral lymphoid homeostasis. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Whereas MAP2K7/MKK7 exclusively activates JNKs, MAP2K4/MKK4 additionally activates the p38 MAPKs MAPK11, MAPK12, MAPK13 and MAPK14.

Catalog Number: (10366-770)

Supplier: Bioss

Description: Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate(GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].

Catalog Number: (10075-442)

Supplier: Prosci

Description: Aquaporin 2 (AQP2) is a hormonally regulated water channel located in the renal collecting duct. Mutations in the AQP2 gene cause hereditary nephrogenic diabetes insipidus in humans (Iolascon et al.,2007). A vasopressin induced cAMP increase results in the phosphorylation of AQP2 at serine-256 and its translocation from the intracellular vesicles to the apical membrane of principal cells (van Balkom et al., 2002). Recently, serine-261 has been identified as a novel phosphorylation site on AQP2 and levels of phosphorylated S261 have been shown to decrease with vasopressin treatment suggesting its involvement in vasopressin-dependent AQP2 trafficking (Hoffert et al., 2007).

Catalog Number: (10412-266)

Supplier: Bioss

Description: Chk2 is a serine/threonine kinase involved in the control of cell cycle checkpoints, and may also participate in transduction of the DNA damage and replicational stress signals. Chk2 is the mammalian ortholog of the budding yeast Rad53 and fission yeast Cds1 checkpoint kinases. The amino-terminal domain of Chk2 contains a series of seven serine and threonine residues (Ser19, Thr26, Ser28, Ser33, Ser35, Ser50 and Thr68) followed by glutamine (SQ or TQ motif). These are known to be preferred sites for phosphorylation by ATM/ATR kinases. Indeed, after DNA damage by ionizing radiation (IR), UV irradiation or hydroxyurea treatment, Thr68 and other sites in this region become phosphorylated by ATM/ATR. The SQ/TQ cluster domain, therefore, seems to have a regulatory function. Phosphorylation at Thr68 is a prerequisite for the subsequent activation step, which is attributable to autophosphorylation of Chk2 on residues Thr383 and Thr387 in the activation loop of the kinase domain. Chk2 inhibits CDC25C phosphatase by phosphorylating it on Ser-216, preventing the entry into mitosis. This kinase may have a role in meiosis as well. Kinase activity is up regulated by autophosphorylation and the protein is rapidly phosphorylated in response to DNA damage and to replication block.

Catalog Number: (10366-776)

Supplier: Bioss

Description: Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate(GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].

Catalog Number: (10387-022)

Supplier: Bioss

Description: Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D. Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect machanism. Interacts with CRY1 and CRY2; negatively regulates CRY1 phosphorylation.

Catalog Number: (10231-658)

Supplier: Bioss

Description: AKT1-specific substrates have been recently identified, including palladin (PALLD), which phosphorylation modulates cytoskeletal organization and cell motility; prohibitin (PHB), playing an important role in cell metabolism and proliferation; and CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation.

Catalog Number: (10075-426)

Supplier: Prosci

Description: Calcium/calmodulin kinase II (CaM Kinase II) is multi-functional calcium and calmodulin-dependent protein kinase that mediates cellular responses to second messengers. Phosphorylation of Thr286 produces an autonomously active form of CaM Kinase II. The antibody was raised against a synthetic phosphopeptide corresponding to amino acid residues surrounding the phosphorylated-Thr286 found in rat brain CaM Kinase II.

Catalog Number: (76077-794)

Supplier: Bioss

Description: PKMYT1 is a member of the serine/threonine protein kinase family. It preferentially phosphorylates and inactivates cell division cycle 2 protein (cdc2), and thus acts as a negative regulator of entry into mitosis (G2 to M transition). It mediates phosphorylation of cdc2 predominantly on 'Thr-14' and is also involved in Golgi fragmentation. It may be involved in phosphorylation of cdc2 on 'Tyr-15' to a lesser degree, however tyrosine kinase activity is unclear and may be indirect. It may be a downstream target of Notch signaling pathway during eye development. PKMYT1 is negatively regulated by hyperphosphorylation during mitosis.

Catalog Number: (10408-514)

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: (10370-888)

Supplier: Bioss

Description: WNK1 controls sodium and chloride ion transport by inhibiting the activity of WNK4, potentially by either phosphorylating the kinase or via an interaction between WNK4 and the autoinhibitory domain of WNK1. WNK4 regulates the activity of the thiazide sensitive Na/Cl cotransporter, SLC12A3, by phosphorylation. WNK1 may also play a role in actin cytoskeletal reorganization.