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Monoclonal Antibody Western Blotting Protein Kinase Activity

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Necroptosis, a regulated pathway for necrotic cell death, is triggered by a number of inflammatory signals including cytokines in the tumor necrosis factor (TNF) family, pathogen sensors such as toll-like receptors (TLRs), and ischemic injury (1,2). The process is negatively regulated by caspases and is initiated through a complex containing the RIP1 and RIP3 kinases, typically referred to as the necrosome. Mixed lineage kinase domain-like protein (MLKL) is a pseudokinase that was identified as downstream target of RIP3 in the necroptosis pathway (3,4). During necroptosis RIP3 is phosphorylated at Ser227, which recruits MLKL and leads to its phosphorylation at Thr357 and Ser358 (3). Knockdown of MLKL through multiple mechanisms results in inhibition of necroptosis (3-5). While the precise mechanism for MLKL-induced necroptosis is unclear, some studies have shown that necroptosis leads to oligomerization of MLKL and translocation to the plasma membrane, where it effects membrane integrity (6-9).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The cyclin-dependent kinases form complexes with their cyclin partners and with CDK inhibitors. CDK6 and CDK4 associate with the D-type cyclins and target the retinoblastoma protein, allowing passage through the G1/S phase restriction point (1). CDK6/cyclin D complexes are sequestered in their inactive form through binding to one of the INK4 CDK inhibitor family members (2,3). Unlike the INK4 family of CDK inhibitors, the CDK inhibitor p21 Waf1/Cip1 may enhance the association of CDK4 and CDK6 with their cyclin D partners (4).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The cyclin-dependent kinases form complexes with their cyclin partners and with CDK inhibitors. CDK6 and CDK4 associate with the D-type cyclins and target the retinoblastoma protein, allowing passage through the G1/S phase restriction point (1). CDK6/cyclin D complexes are sequestered in their inactive form through binding to one of the INK4 CDK inhibitor family members (2,3). Unlike the INK4 family of CDK inhibitors, the CDK inhibitor p21 Waf1/Cip1 may enhance the association of CDK4 and CDK6 with their cyclin D partners (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Necroptosis, a regulated pathway for necrotic cell death, is triggered by a number of inflammatory signals including cytokines in the tumor necrosis factor (TNF) family, pathogen sensors such as toll-like receptors (TLRs), and ischemic injury (1,2). The process is negatively regulated by caspases and is initiated through a complex containing the RIP1 and RIP3 kinases, typically referred to as the necrosome. Mixed lineage kinase domain-like protein (MLKL) is a pseudokinase that was identified as downstream target of RIP3 in the necroptosis pathway (3,4). During necroptosis RIP3 is phosphorylated at Ser227, which recruits MLKL and leads to its phosphorylation at Thr357 and Ser358 (3). Knockdown of MLKL through multiple mechanisms results in inhibition of necroptosis (3-5). While the precise mechanism for MLKL-induced necroptosis is unclear, some studies have shown that necroptosis leads to oligomerization of MLKL and translocation to the plasma membrane, where it effects membrane integrity (6-9).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Activity of the cyclin-dependent kinases CDK4 and CDK6 is regulated by T-loop phosphorylation, by the abundance of their cyclin partners (the D-type cyclins), and by association with CDK inhibitors of the Cip/Kip or INK family of proteins (1). The inactive ternary complex of cyclin D/CDK4 and p27 Kip1 requires extracellular mitogenic stimuli for the release and degradation of p27 concomitant with a rise in cyclin D levels to affect progression through the restriction point and Rb-dependent entry into S-phase (2). The active complex of cyclin D/CDK4 targets the retinoblastoma protein for phosphorylation, allowing the release of E2F transcription factors that activate G1/S-phase gene expression (3). Levels of cyclin D protein drop upon withdrawal of growth factors through downregulation of protein expression and phosphorylation-dependent degradation (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Cyclin Dependent Kinase 10 (CDK10) is a Cdc2-related protein kinase that binds to and inhibits the transactivation activity of the transcription factor Ets2 (1).CDK10 is activated by cyclin M, which is mutated and unable to activate CDK10 in the human developmental disorder, STAR syndrome. Phosphorylation of Ets2 by CDK10/Cyclin M leads to degradation of Ets2 by the proteasome (2). CDK10 also plays a role in the development of the zebrafish nervous system (3). Studies have shown that expression of CDK10, which is modulated by promoter hypermethylation, is decreased in human cancer (4-6). Further, studies show that CDK10 expression in breast cancer affects response to tamoxifen (7), and is correlated with disease progression (8). CDK10 regulates the expression of c-RAF, and signaling through the MAPK pathway (2-3, 6-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: PEAK1 (Pseudopodium-enriched atypical kinase 1 or sgk269) is a member of nonreceptor atypical tyrosine kinase family identified by MS analysis of purified psedopodium (1). PEAK1 is a multi-domain protein with a N-terminal Erk binding site, followed by actin-targeting/Src substrate/Erk substrate region, Crk binding site, Shc binding site, and a C-terminal kinase domain (1, 2). By interacting with different adaptors like Shc, Grb2, Src, and others, PEAK1 functions as an important regulator in different signaling pathways, namely the Src/PEAK1/ErbB2 (3), EGFR Shc1/PEAK1/Grb2(4), TGFβ/PEAK1/Src/MAPK (5), and fibronectin/PEAK1/Src (6) pathways. PEAK1 plays an instrumental role in a wide variety of biological processes including epithelial-mesenchymal transition (EMT), dynamics of focal adhesion, cancer metastatic growth and invasion as well as cancer drug resistance (3, 5-8). Phosphorylation of PEAK1 at Tyr665 or Tyr635 by SFK (Src family Kinases) has been shown to be essential for cancer cell migration and invasion as well as the turnover of focal adhesions (7, 9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Activity of the cyclin-dependent kinases CDK4 and CDK6 is regulated by T-loop phosphorylation, by the abundance of their cyclin partners (the D-type cyclins), and by association with CDK inhibitors of the Cip/Kip or INK family of proteins (1). The inactive ternary complex of cyclin D/CDK4 and p27 Kip1 requires extracellular mitogenic stimuli for the release and degradation of p27 concomitant with a rise in cyclin D levels to affect progression through the restriction point and Rb-dependent entry into S-phase (2). The active complex of cyclin D/CDK4 targets the retinoblastoma protein for phosphorylation, allowing the release of E2F transcription factors that activate G1/S-phase gene expression (3). Levels of cyclin D protein drop upon withdrawal of growth factors through downregulation of protein expression and phosphorylation-dependent degradation (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: DRAK2 (DAP kinase related apoptosis inducing protein kinase 2) is a member of the novel DAP (death associated protein) pro-apoptotic kinase family (1). Overexpression of DRAK2 in NIH/3T3 cells induces morphological changes associated with apoptosis, which are likely to occur in a p53-dependent manner (1,2). DRAK2 is preferentially expressed in lymphoid tissues and regulates the TCR activation threshold during thymocyte selection (3). Indeed, T cells from DRAK2(-/-) mice exhibit enhanced sensitivity to T cell receptor-mediated stimulation and have a reduced requirement for co-stimulation (4).

$122
20 µl
$307
100 µl
$719
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Chk1 kinase acts downstream of ATM/ATR kinase and plays an important role in DNA damage checkpoint control, embryonic development, and tumor suppression (1). Activation of Chk1 involves phosphorylation at Ser317 and Ser345 by ATM/ATR, followed by autophosphorylation of Ser296. Activation occurs in response to blocked DNA replication and certain forms of genotoxic stress (2). While phosphorylation at Ser345 serves to localize Chk1 to the nucleus following checkpoint activation (3), phosphorylation at Ser317 along with site-specific phosphorylation of PTEN allows for re-entry into the cell cycle following stalled DNA replication (4). Chk1 exerts its checkpoint mechanism on the cell cycle, in part, by regulating the cdc25 family of phosphatases. Chk1 phosphorylation of cdc25A targets it for proteolysis and inhibits its activity through 14-3-3 binding (5). Activated Chk1 can inactivate cdc25C via phosphorylation at Ser216, blocking the activation of cdc2 and transition into mitosis (6). Centrosomal Chk1 has been shown to phosphorylate cdc25B and inhibit its activation of CDK1-cyclin B1, thereby abrogating mitotic spindle formation and chromatin condensation (7). Furthermore, Chk1 plays a role in spindle checkpoint function through regulation of aurora B and BubR1 (8). Research studies have implicated Chk1 as a drug target for cancer therapy as its inhibition leads to cell death in many cancer cell lines (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Chk1 kinase acts downstream of ATM/ATR kinase and plays an important role in DNA damage checkpoint control, embryonic development, and tumor suppression (1). Activation of Chk1 involves phosphorylation at Ser317 and Ser345 by ATM/ATR, followed by autophosphorylation of Ser296. Activation occurs in response to blocked DNA replication and certain forms of genotoxic stress (2). While phosphorylation at Ser345 serves to localize Chk1 to the nucleus following checkpoint activation (3), phosphorylation at Ser317 along with site-specific phosphorylation of PTEN allows for re-entry into the cell cycle following stalled DNA replication (4). Chk1 exerts its checkpoint mechanism on the cell cycle, in part, by regulating the cdc25 family of phosphatases. Chk1 phosphorylation of cdc25A targets it for proteolysis and inhibits its activity through 14-3-3 binding (5). Activated Chk1 can inactivate cdc25C via phosphorylation at Ser216, blocking the activation of cdc2 and transition into mitosis (6). Centrosomal Chk1 has been shown to phosphorylate cdc25B and inhibit its activation of CDK1-cyclin B1, thereby abrogating mitotic spindle formation and chromatin condensation (7). Furthermore, Chk1 plays a role in spindle checkpoint function through regulation of aurora B and BubR1 (8). Research studies have implicated Chk1 as a drug target for cancer therapy as its inhibition leads to cell death in many cancer cell lines (9).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Pyruvate generated from glycolysis is converted to acetyl-CoA by pyruvate dehydrogenase (PDH) under normoxia (1-3). This is a critical link between glycolysis and the TCA cycle (3). PDH activity is regulated by phosphorylation and dephosphorylation (3). Pyruvate dehydrogenase kinase (PDHK) phosphorylates PDH and inactivates it, whereas dephosphorylation of PDH is carried out by pyruvate dehydrogenase phosphatase to generate the active form (3). Hypoxia can directly induce pyruvate dehydrogenase kinase 1 (PDHK1) expression, which results in inactivation of PDH and the TCA cycle and subsequent suppression of metabolism (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Three distinct types of phosphoinositide 3-kinases (PI3K) have been characterized. Unlike other PI3Ks, PI3K class III catalyzes the phosphorylation of phosphatidylinositol at the D3 position, producing phosphatidylinositol-3-phosphate (PIP3) (1). PI3K class III is the mammalian homolog of Vps34, first identified in yeast. PI3K class III interacts with the regular subunit p150, the mammalian homolog of Vps15, which regulates cellular membrane association through myristoylation (2,3). PIP3 recruits several proteins with FYVE or PX domains to membranes regulating vesicular transport and protein sorting (4). Moreover, PI3K class III has been shown to regulate autophagy, trimeric G-protein signaling, and the mTOR nutrient-sensing pathway (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Chk1 kinase acts downstream of ATM/ATR kinase and plays an important role in DNA damage checkpoint control, embryonic development, and tumor suppression (1). Activation of Chk1 involves phosphorylation at Ser317 and Ser345 by ATM/ATR, followed by autophosphorylation of Ser296. Activation occurs in response to blocked DNA replication and certain forms of genotoxic stress (2). While phosphorylation at Ser345 serves to localize Chk1 to the nucleus following checkpoint activation (3), phosphorylation at Ser317 along with site-specific phosphorylation of PTEN allows for re-entry into the cell cycle following stalled DNA replication (4). Chk1 exerts its checkpoint mechanism on the cell cycle, in part, by regulating the cdc25 family of phosphatases. Chk1 phosphorylation of cdc25A targets it for proteolysis and inhibits its activity through 14-3-3 binding (5). Activated Chk1 can inactivate cdc25C via phosphorylation at Ser216, blocking the activation of cdc2 and transition into mitosis (6). Centrosomal Chk1 has been shown to phosphorylate cdc25B and inhibit its activation of CDK1-cyclin B1, thereby abrogating mitotic spindle formation and chromatin condensation (7). Furthermore, Chk1 plays a role in spindle checkpoint function through regulation of aurora B and BubR1 (8). Research studies have implicated Chk1 as a drug target for cancer therapy as its inhibition leads to cell death in many cancer cell lines (9).

$134
20 µl
$336
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Chk1 kinase acts downstream of ATM/ATR kinase and plays an important role in DNA damage checkpoint control, embryonic development, and tumor suppression (1). Activation of Chk1 involves phosphorylation at Ser317 and Ser345 by ATM/ATR, followed by autophosphorylation of Ser296. Activation occurs in response to blocked DNA replication and certain forms of genotoxic stress (2). While phosphorylation at Ser345 serves to localize Chk1 to the nucleus following checkpoint activation (3), phosphorylation at Ser317 along with site-specific phosphorylation of PTEN allows for re-entry into the cell cycle following stalled DNA replication (4). Chk1 exerts its checkpoint mechanism on the cell cycle, in part, by regulating the cdc25 family of phosphatases. Chk1 phosphorylation of cdc25A targets it for proteolysis and inhibits its activity through 14-3-3 binding (5). Activated Chk1 can inactivate cdc25C via phosphorylation at Ser216, blocking the activation of cdc2 and transition into mitosis (6). Centrosomal Chk1 has been shown to phosphorylate cdc25B and inhibit its activation of CDK1-cyclin B1, thereby abrogating mitotic spindle formation and chromatin condensation (7). Furthermore, Chk1 plays a role in spindle checkpoint function through regulation of aurora B and BubR1 (8). Research studies have implicated Chk1 as a drug target for cancer therapy as its inhibition leads to cell death in many cancer cell lines (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Mutations in Doublecortin cause Lissencephaly (smooth brain), a neuronal migration disorder characterized by epilepsy and mental retardation (1). Doublecortin is a microtubule associated protein that stabilizes and bundles microtubules. A conserved doublecortin domain mediates the interaction with microtubules, and interestingly most missense mutations cluster in this domain (2). Kinases JNK, CDK5 and PKA phosphorylate doublecortin. JNK phosphorylates Thr321, Thr331 and Ser334 while PKA phosphorylates Ser47 and CDK5 phosphorylates Ser297 (3-5). Phosphorylation of Ser297 lowers the affinity of doublecortin to microtubules. Furthermore, mutations of Ser297 result in migration defects (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: RNase L is an antiviral protein that is expressed in most mammalian cells (1). Latent RNase L in the cytoplasm is activated by the second messenger 2’,5’-linked oligoadenylate (2-5A), which is produced by oligoadenylate synthase (OAS) after it binds viral double-stranded RNA (dsRNA) (2, 3). RNase L forms a crossed homodimer that is stabilized by kinase homology and ankyrin domains, which position two kinase extension nuclease domains for RNA recognition (4). RNase L then degrades both viral and cellular RNA (5). In mouse models, RNase L has been shown to produce small self-RNAs that act to amplify innate antiviral immunity through IFN-β induction (6). Research has also shown that RNase L forms a complex with Filamin A that acts as a barrier to restrict virus entry, and that RNase L can induce autophagy in response to viral infection (7, 8). Finally, research suggests RNase L may contribute to type I diabetes onset through immune response regulation (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Doublecortin-like kinase 1 (DCLK1, DCAMKL1) is a serine/threonine kinase that belongs to the CaM kinase family and shares homology with the neuronal microtubule binding protein doublecortin. DCLK1 is thought to be involved in calcium signaling pathways controlling neuronal development in the embryonic brain (1,2). The kinase also functions in the mature nervous system and is highly expressed in regions of active neurogenesis in the neocortex and cerebellum (3,4). Research studies suggest that the DCLK1 kinase is highly expressed in subpopulations of cells within the colon and gastric epithelium and in the pancreas (5-8). The nature of these cell populations, whether normal, stem-like, or tumor-initiating, is unclear.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: G-protein-coupled receptor kinase 3 (GRK3), also known as beta-adrenergic receptor kinase 2 (beta-ARK2), is a member of the GRK family, which phosphorylates the activated form of G-protein-coupled receptors (GPCRs) and initiates the desensitization process of GPCR (1). GRK3 has been implicated in the phosphorylation of GPCRs, enabling their interaction with beta-arrestin, and facilitating their signaling through ERK1/2 phosphorylation (2). More recently, GRK3 was found to play a critical role in tumor progression through stimulation of angiogenesis; furthermore, GRK3 was found to be overexpressed in human prostate cancer, in particular in metastatic tumors (3).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Chk1 kinase acts downstream of ATM/ATR kinase and plays an important role in DNA damage checkpoint control, embryonic development, and tumor suppression (1). Activation of Chk1 involves phosphorylation at Ser317 and Ser345 by ATM/ATR, followed by autophosphorylation of Ser296. Activation occurs in response to blocked DNA replication and certain forms of genotoxic stress (2). While phosphorylation at Ser345 serves to localize Chk1 to the nucleus following checkpoint activation (3), phosphorylation at Ser317 along with site-specific phosphorylation of PTEN allows for re-entry into the cell cycle following stalled DNA replication (4). Chk1 exerts its checkpoint mechanism on the cell cycle, in part, by regulating the cdc25 family of phosphatases. Chk1 phosphorylation of cdc25A targets it for proteolysis and inhibits its activity through 14-3-3 binding (5). Activated Chk1 can inactivate cdc25C via phosphorylation at Ser216, blocking the activation of cdc2 and transition into mitosis (6). Centrosomal Chk1 has been shown to phosphorylate cdc25B and inhibit its activation of CDK1-cyclin B1, thereby abrogating mitotic spindle formation and chromatin condensation (7). Furthermore, Chk1 plays a role in spindle checkpoint function through regulation of aurora B and BubR1 (8). Research studies have implicated Chk1 as a drug target for cancer therapy as its inhibition leads to cell death in many cancer cell lines (9).