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Product listing: Phospho-APP (Thr668) Antibody, UniProt ID P05067 #3823 to Phospho-Tyrosine Hydroxylase (Ser31) Antibody, UniProt ID P04177 #3370

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase (4). APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Circadian rhythms govern many key physiological processes that fluctuate with a period of approximately 24 hours. These processes include the sleep-wake cycle, glucose, lipid and drug metabolism, heart rate, hormone secretion, renal blood flow, and body temperature, as well as basic cellular processes such as DNA repair and the timing of the cell division cycle (1,2). The mammalian circadian system consists of many individual tissue-specific clocks (peripheral clocks) that are controlled by a master circadian pacemaker residing in the suprachiasmatic nuclei (SCN) of the brain (1,2). The periodic circadian rhythm is prominently manifested by the light-dark cycle, which is sensed by the visual system and processed by the SCN. The SCN processes the light-dark information and synchronizes peripheral clocks through neural and humoral output signals (1,2).The cellular circadian clockwork consists of interwoven positive and negative regulatory loops, or limbs (1,2). The positive limb includes the CLOCK and BMAL1 proteins, two basic helix-loop-helix-PAS containing transcription factors that bind E box enhancer elements and activate transcription of their target genes. CLOCK is a histone acetyltransferase (HAT) protein, which acetylates both histone H3 and H4 (3). BMAL1 binds to CLOCK and enhances its HAT activity (3). The CLOCK/BMAL1 dimer exhibits a periodic oscillation in both nuclear/cytoplasmic localization and protein levels, both of which are regulated by phosphorylation (4,5). CLOCK/BMAL1 target genes include the Cry and Per genes, whose proteins form the negative limb of the circadian clockwork system (1,2). CRY and PER proteins (CRY1, CRY2, PER1, PER2 and PER3) form oligomers that also periodically shuttle between the nucleus and cytoplasm. When in the nucleus, CRY/PER proteins inhibit CLOCK/BMAL1-mediated transcriptional activation, thus completing the circadian transcriptional loop (1,2). In tissues, roughly six to eight percent of all genes exhibit a circadian expression pattern (1,2). This 24-hour periodicity in gene expression results from coordination of the positive and negative regulatory limbs of the cellular clockwork system, and is fine-tuned by outside signals received from the SCN.

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Western Blotting

Background: CaMKII is an important member of the calcium/calmodulin-activated protein kinase family, functioning in neural synaptic stimulation and T cell receptor signaling (1,2). CaMKII has catalytic and regulatory domains. Ca2+/calmodulin binding to the CaMKII regulatory domain relieves autoinhibition and activates the kinase (3). The activated CaMKII further autophosphorylates at Thr286 to render the kinase constitutively active (3). The threonine phosphorylation state of CaMKII can be regulated through PP1/PKA. PP1 (protein phosphatase 1) dephosphorylates phospho-CaMKII at Thr286. PKA (protein kinase A) prevents phospho-CaMKII (Thr286) dephosphorylation through an inhibitory effect on PP1 (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Calcium/Calmodulin-dependent Protein Kinase Kinase 2 (CaMKK2) is a member of the CaMK family that contains a central Ser/Thr kinase domain followed by a regulatory domain consisting of overlapping autoinhibitory and CaM-binding regions (1). CaMKK2 can be distinguished from other CaMK family members by the presence of a unique Pro/Arg/Gly-rich insert following the ATP-binding domain (2). CaMKK2 phosphorylates CaMKI at Thr177 and CaMKIV at Thr200 (3). CaMKK2 also phosphorylates AMPKα in response to calcium (4). CaMKK2 has been implicated in long-term memory formation (5) and adipocyte development (6). CaMKK2 is phosphorylated at Ser511 by death-associated protein kinase (DAPK) in a signaling cascade thought to be involved in neuronal death (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Calcium/Calmodulin-dependent Protein Kinase Kinase 2 (CaMKK2) is a member of the CaMK family that contains a central Ser/Thr kinase domain followed by a regulatory domain consisting of overlapping autoinhibitory and CaM-binding regions (1). CaMKK2 can be distinguished from other CaMK family members by the presence of a unique Pro/Arg/Gly-rich insert following the ATP-binding domain (2). CaMKK2 phosphorylates CaMKI at Thr177 and CaMKIV at Thr200 (3). CaMKK2 also phosphorylates AMPKα in response to calcium (4). CaMKK2 has been implicated in long-term memory formation (5) and adipocyte development (6). CaMKK2 is phosphorylated at Ser511 by death-associated protein kinase (DAPK) in a signaling cascade thought to be involved in neuronal death (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Collapsin Response Mediator Protein-2 (CRMP-2) is expressed at high levels in the developing nervous system and plays a critical role in axonal outgrowth by specifying axon/dendrite fate and establishing neuronal polarity (1,2). CRMP-2 enhances axon elongation and branching by binding to tubulin heterodimers to promote microtubule assembly (3). GSK-3β inactivates CRMP-2 by phosphorylating it at Thr514. CRMP-2 is primed following phosphorylation at Ser522 by CDK5 and at Thr518 by GSK-3β (2). Phosphorylation of CRMP-2, which decreases tubulin binding ability, can be inhibited by NT-3 and BDNF through the PI3 kinase/Akt pathway (2). CRMP-2 also mediates semaphorin-induced growth cone collapse (4). Hyperphosphorylation of CRMP-2 is found in Alzheimer disease plaques with concurrent elevated GSK-3β activity in these patients (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Reelin signaling pathway plays a critical role in neuronal development. Reelin is a secreted glycoprotein that binds to the lipoprotein receptors VLDLR and ApoER2 or alpha3beta1 integrin on the surface of neurons (1,2). Activation of these receptors induces tyrosine phosphorylation of Disabled 1 (Dab1), an intracellular adaptor. It is generally believed that tyrosine phosphorylation of Dab1 by Src family tyrosine kinases is the most critical downstream event in Reelin signaling. The phosphotyrosine-binding (PTB) domain within its amino terminus enables Dab1 to recognize and bind to a conserved sequence motif within the cytoplasmic tail of the receptors. In addition, the PTB contains a Pleckstrin Homology-like subdomain that binds to phosphoinositides. The phosphoinositide-binding region within the Dab1 PTB domain is required for membrane localization and basal tyrosine phosphorylation of Dab1 independent of VLDLR and ApoER2 (3). It has been demonstrated that Src, CrkII, CrkL and Dock1 associate with tyrosine-phosphorylated Dab. The CrkII-Dab1 interaction requires tyrosine phosphorylation of Dab1 at residues 220 or 232 (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Reelin signaling pathway plays a critical role in neuronal development. Reelin is a secreted glycoprotein that binds to the lipoprotein receptors VLDLR and ApoER2 or alpha3beta1 integrin on the surface of neurons (1,2). Activation of these receptors induces tyrosine phosphorylation of Disabled 1 (Dab1), an intracellular adaptor. It is generally believed that tyrosine phosphorylation of Dab1 by Src family tyrosine kinases is the most critical downstream event in Reelin signaling. The phosphotyrosine-binding (PTB) domain within its amino terminus enables Dab1 to recognize and bind to a conserved sequence motif within the cytoplasmic tail of the receptors. In addition, the PTB contains a Pleckstrin Homology-like subdomain that binds to phosphoinositides. The phosphoinositide-binding region within the Dab1 PTB domain is required for membrane localization and basal tyrosine phosphorylation of Dab1 independent of VLDLR and ApoER2 (3). It has been demonstrated that Src, CrkII, CrkL and Dock1 associate with tyrosine-phosphorylated Dab. The CrkII-Dab1 interaction requires tyrosine phosphorylation of Dab1 at residues 220 or 232 (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: DARPP-32 (dopamine and cyclic AMP-regulated phosphoprotein, relative molecular mass 32,000) is a cytosolic protein highly enriched in medium-sized spiny neurons of the neostriatum (1). It is a bifunctional signaling molecule that controls serine/threonine kinase and serine/threonine phosphatase activity (2). Dopamine stimulates phosphorylation of DARPP-32 through D1 receptors and activation of PKA. PKA phosphorylation of DARPP-32 at Thr34 converts it into an inhibitor of protein phosphatase 1 (1). DARPP-32 is converted into an inhibitor of PKA when phosphorylated at Thr75 by cyclin-dependent kinase 5 (CDK5) (2). Mice containing a targeted deletion of the DARPP-32 gene exhibit an altered biochemical, electrophysiological, and behavioral phenotype (3).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: 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).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunoprecipitation, 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).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Guanylate kinase-associated protein (GKAP, DLGAP1 or SAPAP1) is part of the postsynaptic scaffolding complex that includes the PSD-95, SAP90, and SHANK proteins (1-3). GKAP links the synaptic protein SHANK to a PSD-95 complex that includes NMDA glutamate receptors (3,4). Synaptic activity induces ubiquitination of GKAP protein by the E3 ubiquitin ligase TRIM3, which results in decreased GKAP protein levels through degradation (5,6). GKAP protein turnover is regulated by a CaMKII-dependent, bidirectional mechanism. Synaptic over-excitation leads to CaMKIIα-mediated GKAP phosphorylation at Ser346, which induces polyubiquitination of GKAP and removal of the scaffold protein from synapses. In contrast, during low-level synaptic activity CaMKIIβ phosphorylates GKAP, which triggers dissociation of GKAP from the motor protein complex responsible for GKAP transport to the base of the synapse and its subsequent incorporation into the postsynaptic density (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: Microtubule-associated protein 2 (MAP2) is a neuronal phosphoprotein that regulates the structure and stability of microtubules, neuronal morphogenesis, cytoskeleton dynamics, and organelle trafficking in axons and dendrites (1). Multiple MAP2 isoforms are expressed in neurons, including high molecular weight MAP2A and MAP2B (280 and 270 kDa), and low molecular weight MAP2C and MAP2D (70 and 75 kDa). Phosphorylation of MAP2 modulates its association with the cytoskeleton and is developmentally regulated. GSK-3 and p44/42 MAP kinase phosphorylate MAP2 at Ser136, Thr1620, and Thr1623 (2,3). Phosphorylation at Thr1620/1623 by GSK-3 inhibits MAP2 association with microtubules and microtubule stability (3).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Microtubule-associated protein 2 (MAP2) is a neuronal phosphoprotein that regulates the structure and stability of microtubules, neuronal morphogenesis, cytoskeleton dynamics, and organelle trafficking in axons and dendrites (1). Multiple MAP2 isoforms are expressed in neurons, including high molecular weight MAP2A and MAP2B (280 and 270 kDa), and low molecular weight MAP2C and MAP2D (70 and 75 kDa). Phosphorylation of MAP2 modulates its association with the cytoskeleton and is developmentally regulated. GSK-3 and p44/42 MAP kinase phosphorylate MAP2 at Ser136, Thr1620, and Thr1623 (2,3). Phosphorylation at Thr1620/1623 by GSK-3 inhibits MAP2 association with microtubules and microtubule stability (3).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Neurofibromatosis 2 (NF2) is an autosomal dominant, inherited disorder characterized by the occurrence of vestibular schwannomas, meningiomas, and other nervous system tumors. Both the familial tumors of NF2 and equivalent sporadic tumors found in the general population are caused by inactivation of the NF2 tumor suppressor gene. Merlin (moesin, ezrin, and radixin-like protein) is the NF2 gene product, displaying striking similarity to ezrin, radixin, and moesin (ERM) proteins. Regulation of merlin (also called schwannomin) and ERM proteins involves intramolecular and intermolecular head-to-tail associations between family members (1). Merlin and ERM proteins act as linkers between the plasma membrane and the cytoskeleton, affecting cell morphology, polarity, and signal transduction (2). Merlin is phosphorylated by the Rac/Cdc42 effector p21-activated kinase (PAK) at Ser518, negatively regulating Rac (3,4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Postsynaptic Density Protein 93 (PSD93) is a member of the PSD subfamily of the membrane-associated guanylate kinase (PSD-MAGUK) proteins. Structurally, it most closely resembles PSD95, consisting of an N-terminal variable segment followed by three PDZ domains, an SH3 domain, and an inactive guanylate kinase (GK) domain (1,2). PSD93 is expressed in neuronal cells and located at the synapse where it interacts with neuronal receptors and proteins including the NMDA receptor (2-4), K+ channels (5,6), and the AMPA receptor (7) to regulate their membrane localization and neuronal signaling. Research studies have implicated PSD93 in postsynaptic related persistent pain induction, making PSD93 a potential target for treatment of this syndrome (3).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Western Blotting

Background: Postsynaptic Density protein 95 (PSD95) is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins. These family members consist of an amino-terminal variable segment followed by three PDZ domains, a SH3 domain, and an inactive guanylate kinase (GK) domain. PSD95 is a scaffolding protein involved in the assembly and function of the postsynaptic density complex (1-2). PSD95 participates in synaptic targeting of AMPA receptors through an indirect manner involving Stargazin and related transmembrane AMPA receptor regulatory proteins (TARPs) (3). It is implicated in experience-dependent plasticity and plays an indispensable role in learning (4). Mutations in PSD95 are associated with autism (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Ras activity is regulated by GAP (GTPase activating proteins) and GEFs (guanine nucleotide exchange factors). Ras-GRF1 (also known as CDC25Mm) is neuronal RasGEF and is regulated by heterotrimeric G proteins and calcium influx (1,2). Binding to calmodulin and phosphorylation stimulate Ras-GRF1 activity (1,2). Multiple PKA phosphorylation sites on Ras-GRF have been identified. Phosphorylation on the two major sites, Ser54 and Ser822, inhibits Ras-GRF activity (3). Carbachol (a muscarinic agonist)-induced phosphorylation on Ser916 is essential but not sufficient for maximal Ras-GRF activity (4). It has been reported that Ras-GRF1 also shows GEF activity toward Rac after phosphorylation by the tyrosine kinase Src (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The semaphorin family of proteins is involved in axon guidance, cell migration, angiogenesis, and immune response. Plexins and neuropilins bind with high affinity to semaphorins to mediate their functions. Semaphorins are divided into seven classes of secreted or membrane-bound proteins. Members of Class 4 semaphorins include 4A through 4G; semaphorin 4B is a membrane-associated protein (1,2). Semaphorin 4B binds to the CLCP1 receptor and regulates cell motility (3). Furthermore, semaphorin 4B, like many other semaphorins, has a PDZ domain-binding motif at the carboxy terminus that interacts with PSD95 and localizes to the post-synaptic membrane (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Synapsins, a group of at least five related members (synapsins Ia, Ib, IIa, IIb, and IIIa), are abundant brain proteins essential for regulating neurotransmitter release (1,2). All synapsins contain a short amino-terminal domain that is highly conserved and phosphorylated by PKA or CaM kinase I (1). Phosphorylation of the synapsin amino-terminal domain at Ser9 inhibits its binding to phospholipids and dissociates synapsins from synaptic vesicles (2).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Tau is a heterogeneous microtubule-associated protein that promotes and stabilizes microtubule assembly, especially in axons. Six isoforms with different amino-terminal inserts and different numbers of tandem repeats near the carboxy terminus have been identified, and tau is hyperphosphorylated at approximately 25 sites by Erk, GSK-3, and CDK5 (1,2). Phosphorylation decreases the ability of tau to bind to microtubules. Neurofibrillary tangles are a major hallmark of Alzheimer's disease; these tangles are bundles of paired helical filaments composed of hyperphosphorylated tau. In particular, phosphorylation at Ser396 by GSK-3 or CDK5 destabilizes microtubules. Furthermore, research studies have shown that inclusions of tau are found in a number of other neurodegenerative diseases, collectively known as tauopathies (1,3).

$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The family of Trk receptor tyrosine kinases consists of TrkA, TrkB, and TrkC. While the sequence of these family members is highly conserved, they are activated by different neurotrophins: TrkA by NGF, TrkB by BDNF or NT4, and TrkC by NT3 (1). Neurotrophin signaling through these receptors regulates a number of physiological processes, such as cell survival, proliferation, neural development, and axon and dendrite growth and patterning (1). In the adult nervous system, the Trk receptors regulate synaptic strength and plasticity. TrkA regulates proliferation and is important for development and maturation of the nervous system (2). Phosphorylation at Tyr490 is required for Shc association and activation of the Ras-MAP kinase cascade (3,4). Residues Tyr674/675 lie within the catalytic domain, and phosphorylation at these sites reflects TrkA kinase activity (3-6). Point mutations, deletions, and chromosomal rearrangements (chimeras) cause ligand-independent receptor dimerization and activation of TrkA (7-10). TrkA is activated in many malignancies including breast, ovarian, prostate, and thyroid carcinomas (8-13). Research studies suggest that expression of TrkA in neuroblastomas may be a good prognostic marker as TrkA signals growth arrest and differentiation of cells originating from the neural crest (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of the neurotransmitter dopamine and other catecholamines. TH functions as a tetramer, with each subunit composed of a regulatory and catalytic domain, and exists in several different isoforms (1,2). This enzyme is required for embryonic development since TH knockout mice die before or at birth (3). Levels of transcription, translation and posttranslational modification regulate TH activity. The amino-terminal regulatory domain contains three serine residues: Ser9, Ser31 and Ser40. Phosphorylation at Ser40 by PKA positively regulates the catalytic activity of TH (4-6). Phosphorylation at Ser31 by CDK5 also increases the catalytic activity of TH through stabilization of TH protein levels (7-9).