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Product listing: SynGAP (D88G1) Rabbit mAb, UniProt ID Q96PV0 #9479 to Tyrosine Hydroxylase (A8Y7R) Rabbit mAb, UniProt ID P07101 #13106

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: SynGAP is a synaptic GTPase-activating protein selectively expressed in the brain and found at higher concentrations specifically at excitatory synapses in the mammalian forebrain. SynGAP has a PH domain, a C2 domain, and a highly conserved RasGAP domain, which negatively regulates both Ras activity and its downstream signaling pathways. SynGAP interacts with the PDZ domains of SAP102, as well as PSD95, a postsynaptic scaffolding protein that couples SynGAP to NMDA receptors (1). SynGAP is phosphorylated by Ca2+/calmodulin-dependent protein kinase II (CaMKII) at Ser765 and Ser1123, among other sites (2,3). Phosphorylation of SynGAP results in stimulation of the GTPase activity of Ras, and PSD95 dependent CaMKII phosphorylation of SynGAP increases after transient brain ischemia (1,4). SynGAP is implicated in NMDAR- and CaMKII-dependent regulation of AMPAR trafficking and plays an important role in synaptic plasticity (3,5). SynGAP is critical during neuronal development as mice lacking SynGAP protein die postnatally. Furthermore, SynGAP mutant mice have reduced long-term potentiation (LTP) and perform poorly in spatial memory tasks (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Syntaxin 1A (STX1A) is a SNARE protein involved in intracellular membrane fusion, including synaptic vesicle fusion (1). At the synapse, syntaxin 1 is located at the presynaptic plasma membrane and is therefore categorized as a t-SNARE protein (2). The amino-terminal domain of syntaxin 1 interacts with Munc18-1 and this interaction is essential for synaptic vesicle fusion (3). Although originally characterized from neural tissues, research studies have demonstrated syntaxin 1A expression in exocrine tissues such as pancreatic islets (4) where it negatively regulates insulin release (5).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for direct immunofluorescent analysis in mouse tissue. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Tau (D1M9X) XP® Rabbit mAb #46687.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen)

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).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), 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).

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

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Paraffin), Immunohistochemistry (Paraffin), 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).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct immuno fluorescence analysis in mouse tissue. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated TBR1 (D6C6X) Rabbit mAb #49661.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen)

Background: T-box, brain, 1 (TBR1) is a transcription factor important in vertebrate embryo development. As a member of T-Box family of transcription factors, TBR1 is expressed in postmitotic glutamatergic projection neurons (1). During cortical neurogenesis, sequential expression of transcription factors Pax6, TBR2, and TBR1 regulates discrete steps in projection neuron differentiation (2). TBR1 is enriched in layer 6 of the developing cortex. In the absence of TBR1, TBR1 mutants exhibit profound defects in frontal cortex and layer 6 differentiation, suggesting that TBR1 regulates regional and laminar identity of postmitotic cortical neurons (3). Therefore, TBR1 expression can be used as a marker for postmitotic glutamatergic neurons and cortical laminar specificity.

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for direct immunofluorescent analysis in mouse tissue. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated TBR1 (D6C6X) Rabbit mAb #49661.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen)

Background: T-box, brain, 1 (TBR1) is a transcription factor important in vertebrate embryo development. As a member of T-Box family of transcription factors, TBR1 is expressed in postmitotic glutamatergic projection neurons (1). During cortical neurogenesis, sequential expression of transcription factors Pax6, TBR2, and TBR1 regulates discrete steps in projection neuron differentiation (2). TBR1 is enriched in layer 6 of the developing cortex. In the absence of TBR1, TBR1 mutants exhibit profound defects in frontal cortex and layer 6 differentiation, suggesting that TBR1 regulates regional and laminar identity of postmitotic cortical neurons (3). Therefore, TBR1 expression can be used as a marker for postmitotic glutamatergic neurons and cortical laminar specificity.

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct immunofluorescent analysis in mouse tissue. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated TBR1 (D6C6X) Rabbit mAb #49661.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen)

Background: T-box, brain, 1 (TBR1) is a transcription factor important in vertebrate embryo development. As a member of T-Box family of transcription factors, TBR1 is expressed in postmitotic glutamatergic projection neurons (1). During cortical neurogenesis, sequential expression of transcription factors Pax6, TBR2, and TBR1 regulates discrete steps in projection neuron differentiation (2). TBR1 is enriched in layer 6 of the developing cortex. In the absence of TBR1, TBR1 mutants exhibit profound defects in frontal cortex and layer 6 differentiation, suggesting that TBR1 regulates regional and laminar identity of postmitotic cortical neurons (3). Therefore, TBR1 expression can be used as a marker for postmitotic glutamatergic neurons and cortical laminar specificity.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Paraffin)

Background: T-box, brain, 1 (TBR1) is a transcription factor important in vertebrate embryo development. As a member of T-Box family of transcription factors, TBR1 is expressed in postmitotic glutamatergic projection neurons (1). During cortical neurogenesis, sequential expression of transcription factors Pax6, TBR2, and TBR1 regulates discrete steps in projection neuron differentiation (2). TBR1 is enriched in layer 6 of the developing cortex. In the absence of TBR1, TBR1 mutants exhibit profound defects in frontal cortex and layer 6 differentiation, suggesting that TBR1 regulates regional and laminar identity of postmitotic cortical neurons (3). Therefore, TBR1 expression can be used as a marker for postmitotic glutamatergic neurons and cortical laminar specificity.

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: TDP43 (TAR DNA-binding protein 43) is involved in transcriptional regulation and exon splicing (1,2). While normal TDP43 is a nuclear protein, pathological TDP43 is a component of insoluble aggregates in patients with frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). In these disorders, TDP43 is abnormally ubiquitinated, phosphorylated and cleaved to generate carboxy-terminal fragments that are sequestered as insoluble aggregates in neuronal nuclei, perikarya, and neurites (3,4). Additionally, TDP43 inhibits the expression of the HIV-1 gene and regulates CFTR gene splicing (1,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Tenascin C is a large hexameric extracellular matrix glycoprotein that exhibits de-adhesive effects on cell-matrix interaction, enhancing cell proliferation and motility in most cell types. It is highly expressed in remodeling tissues during embryonic development and under pathological conditions in adults, and research studies have shown markedly increased expression in cancerous tissues (1,2). Tenascin C has been implicated in a variety of cellular processes relevant to atherosclerosis, including cell proliferation, migration, and apoptosis. Expression of Tenascin C is tightly controlled in adults and is upregulated in tissues undergoing wound healing (3). In development, the expression of Tenascin C is known to be associated with epithelial-mesenchymal transition (EMT) events including gastrulation and formation of the neural crest, endocardial cushion, and secondary palate (1). Investigators have shown that Tenascin C is a key determinant of the tumor stroma and that it is involved in the initiation of tumorigenesis and progression to metastasis (2). Immature and mature astrocytes, radial glial cells, Schwann cells, and a subset of neurons express Tenascin C. Upon CNS trauma or exposure of neurons to excitotoxic agents, Tenascin C expression is upregulated by glial cells. Research studies have shown that Tenascin C is involved in guidance of migrating axons and neurons, synaptic plasticity, and neuronal regeneration, promoting spinal cord regeneration after injury (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: TFAM (Transcription Factor A, Mitochondrial; aka TCF6) is a member of the high-mobility group (HMG) proteins because it contains two HMG boxes. TFAM is a transcription factor for mitochondrial DNA (mtDNA), and enhances mtDNA transcription in a promoter-specific fashion in the presence of mitochondrial RNA polymerase and transcription factor B (1). Because the majority of ATP production depends on the mitochondrial respiratory chain, maintenance of the mitochondrial genome is critical for normal health. TFAM plays an essential role in the maintenance of mtDNA and thus, ATP production (2). TFAM binds to mtDNA both nonspecifically and in a sequence-specific manner. It is known to have a dual effect on mtDNA: protection of mtDNA and initiation of transcription from mtDNA (3). TFAM attenuates age-dependent impairment of the brain by preventing oxidative stress and mitochondrial dysfunctions in microglia (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The neurological condition Dystonia is associated with sustained muscle contractions and abnormal posturing (1). TorsinA, torsinB, torp2A and torp3A belong to the family of ATPases associated with cellular activites (AAA+) and mutations in torsinA cause early onset dystonia (2). TorsinA has been shown to suppress intracellular protein aggregation in C. elegans and possesses chaperon activity. Interestingly, torsinA is highly expressed in dopaminergic neurons and associates with alpha-synuclein in Lewy bodies, which pathologically characterize Parkinson's Disease (3-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Tryptophan hydroxylase (TPH) is the rate-limiting enzyme in the biosynthesis of serotonin (1) by converting tryptophan to 5-hydroxy-L-tryptophan (2). Two isoforms of TPH exist: TPH-1 is mainly expressed in the periphery, whereas the expression of TPH-2 is restricted to neuronal cells and the central nervous system (3). Most of the serotonin found throughout the body is synthesized by TPH-1 in enterochromaffin cells of the gastrointestinal tract. Targeted disruption of the tph1 gene results in low levels of circulating and tissue serotonin (4).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: Tryptophan hydroxylase (TPH) is the rate-limiting enzyme in the biosynthesis of serotonin (1) by converting tryptophan to 5-hydroxy-L-tryptophan (2). Two isoforms of TPH exist: TPH-1 is mainly expressed in the periphery, whereas the expression of TPH-2 is restricted to neuronal cells and the central nervous system (3). Most of the serotonin found throughout the body is synthesized by TPH-1 in enterochromaffin cells of the gastrointestinal tract. Targeted disruption of the tph1 gene results in low levels of circulating and tissue serotonin (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Transthyretin (TTR) is a highly conserved homotetremric protein that is synthesized in the liver and choroid plexus of the brain. TTR was originally discovered as a protein found in human plasma and cerebrospinal fluid (CSF) (1). TTR transports thyroid hormones (TH) and retinol by binding to retinol-binding protein (2). Although TTR is synthesized in the liver and choroid plexus, TTR is detected in blood plasma and cerebrospinal fluid migrating as monomers, dimers, and tetramers. Beyond its function as a carrier protein of TH and retinol in plasma and CSF, several additional TTR functions have been described, including proteolytic cleavage of specific substrates like apolipoprotein, neuropeptide Y (NPY), and APP (3, 4, 5). These neuronal substrates suggest a functional role for TTR in the central nervous system. Consistent with a CNS function, TTR null mice exhibit memory impairments and altered sensorimotor behavior (6, 7). TTR may also be linked to neurodegenerative disease: TTR levels in Alzheimer’s disease (AD) patients are negatively correlated with disease progression, and a protective role for TTR, at least in AD mouse models, has been described (8, 9). TTR itself may play a more direct role in disease as gain-of-function mutations in TTR cause the protein to misfold and aggregate into amyloid fibrils, contributing to autosomal dominant hereditary amyloidosis in diseases such as familial amyloid polyneuropathy, familial amyloid cardiomyopathy, and familial leptomeningeal amyloidosis (10). 

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The triggering receptor expressed on myeloid cells 2 (TREM2) protein is an innate immune receptor that is expressed on the cell surface of microglia, macrophages, osteoclasts, and immature dendritic cells (1). The TREM2 receptor is a single-pass type I membrane glycoprotein that consists of an extracellular immunoglobulin-like domain, a transmembrane domain, and a cytoplasmic tail. TREM2 interacts with the tyrosine kinase-binding protein DAP12 to form a receptor-signaling complex (2). The TREM2 protein plays a role in innate immunity and a rare functional variant (R47H) of TREM2 is associated with the late-onset risk of Alzheimer’s disease (1,3). Research studies using mouse models of Alzheimer’s disease indicate that deficiency and haploinsufficiency of TREM2 can lead to increased β-amyloid (Aβ) accumulation as a result of dysfunctional microglia response (4). These results agree with the distribution of TREM2 in human brain regions (e.g., white matter, the hippocampus, and neocortex) that are involved in Alzheimer's disease pathology (2). In addition, amyloid plaque formation induces expression of TREM2 and amyloid phagocytosis (5). Loss-of-function mutations in the corresponding TREM2 or DAP12 genes can result in Nasu-Hakola disease, a rare form of progressive presenile dementia that results from polycystic osseous lesions (6). TREM2 membrane shedding occurs by cleavage at the extracellular site between H157/S158 generating an N-terminal shedded fragment and a membrane bound C-terminal fragment (7, 8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: The triggering receptor expressed on myeloid cells 2 (TREM2) protein is an innate immune receptor that is expressed on the cell surface of microglia, macrophages, osteoclasts, and immature dendritic cells (1). The TREM2 receptor is a single-pass type I membrane glycoprotein that consists of an extracellular immunoglobulin-like domain, a transmembrane domain, and a cytoplasmic tail. TREM2 interacts with the tyrosine kinase-binding protein DAP12 to form a receptor-signaling complex (2). The TREM2 protein plays a role in innate immunity and a rare functional variant (R47H) of TREM2 is associated with the late-onset risk of Alzheimer’s disease (1,3). Research studies using mouse models of Alzheimer’s disease indicate that deficiency and haploinsufficiency of TREM2 can lead to increased β-amyloid (Aβ) accumulation as a result of dysfunctional microglia response (4). These results agree with the distribution of TREM2 in human brain regions (e.g., white matter, the hippocampus, and neocortex) that are involved in Alzheimer's disease pathology (2). In addition, amyloid plaque formation induces expression of TREM2 and amyloid phagocytosis (5). Loss-of-function mutations in the corresponding TREM2 or DAP12 genes can result in Nasu-Hakola disease, a rare form of progressive presenile dementia that results from polycystic osseous lesions (6). TREM2 membrane shedding occurs by cleavage at the extracellular site between H157/S158 generating an N-terminal shedded fragment and a membrane bound C-terminal fragment (7, 8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: The triggering receptor expressed on myeloid cells 2 (TREM2) protein is an innate immune receptor that is expressed on the cell surface of microglia, macrophages, osteoclasts, and immature dendritic cells (1). The TREM2 receptor is a single-pass type I membrane glycoprotein that consists of an extracellular immunoglobulin-like domain, a transmembrane domain, and a cytoplasmic tail. TREM2 interacts with the tyrosine kinase-binding protein DAP12 to form a receptor-signaling complex (2). The TREM2 protein plays a role in innate immunity and a rare functional variant (R47H) of TREM2 is associated with the late-onset risk of Alzheimer’s disease (1,3). Research studies using mouse models of Alzheimer’s disease indicate that deficiency and haploinsufficiency of TREM2 can lead to increased β-amyloid (Aβ) accumulation as a result of dysfunctional microglia response (4). These results agree with the distribution of TREM2 in human brain regions (e.g., white matter, the hippocampus, and neocortex) that are involved in Alzheimer's disease pathology (2). In addition, amyloid plaque formation induces expression of TREM2 and amyloid phagocytosis (5). Loss-of-function mutations in the corresponding TREM2 or DAP12 genes can result in Nasu-Hakola disease, a rare form of progressive presenile dementia that results from polycystic osseous lesions (6). TREM2 membrane shedding occurs by cleavage at the extracellular site between H157/S158 generating an N-terminal shedded fragment and a membrane bound C-terminal fragment (7, 8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The triggering receptor expressed on myeloid cells 2 (TREM2) protein is an innate immune receptor that is expressed on the cell surface of microglia, macrophages, osteoclasts, and immature dendritic cells (1). The TREM2 receptor is a single-pass type I membrane glycoprotein that consists of an extracellular immunoglobulin-like domain, a transmembrane domain, and a cytoplasmic tail. TREM2 interacts with the tyrosine kinase-binding protein DAP12 to form a receptor-signaling complex (2). The TREM2 protein plays a role in innate immunity and a rare functional variant (R47H) of TREM2 is associated with the late-onset risk of Alzheimer’s disease (1,3). Research studies using mouse models of Alzheimer’s disease indicate that deficiency and haploinsufficiency of TREM2 can lead to increased β-amyloid (Aβ) accumulation as a result of dysfunctional microglia response (4). These results agree with the distribution of TREM2 in human brain regions (e.g., white matter, the hippocampus, and neocortex) that are involved in Alzheimer's disease pathology (2). In addition, amyloid plaque formation induces expression of TREM2 and amyloid phagocytosis (5). Loss-of-function mutations in the corresponding TREM2 or DAP12 genes can result in Nasu-Hakola disease, a rare form of progressive presenile dementia that results from polycystic osseous lesions (6). TREM2 membrane shedding occurs by cleavage at the extracellular site between H157/S158 generating an N-terminal shedded fragment and a membrane bound C-terminal fragment (7, 8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, 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).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Trk (pan) (A7H6R) Rabbit mAb #92991.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: 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).

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

Application Methods: 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunohistochemistry (Paraffin)

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Transient Receptor Potential Canonical 3 (TRPC3) belongs to the superfamily of TRP cation channels. The TRPC subfamily (TRPC1-7) is a group of calcium-permeable cation channels that mediates the increase in intracellular [Ca2+] following activation by G-protein-coupled receptors or receptor tyrosine kinases (1). TRPC3 is mainly expressed in the brain and various other tissues, though at a much lower level (2). In the brain, TRPC3 is involved in BDNF-induced axonal growth cone plasticity, dendritic spine formation, and neuronal survival (3-6). It is also required for synaptic transmission and motor coordination (7). Outside of the central nervous system, TRPC3 also exerts other important biological functions such as regulating cardiac and vascular contractility, maintaining Ca2+ homeostasis in primary T cells and endothelial cells (8-10). TRPC3 is activated by diacylglycerol and Inositol 1,4,5-trisphosphate (11,12). It is also activated by internal calcium store depletion and regulates mitochondrial calcium uptake (13,14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Transient receptor potential (TRP) canonical 6 (TRPC6) belongs to the superfamily of TRP cation channels. The TRPC subfamily (TRPC1-7) is a group of calcium-permeable cation channels that mediates the increase in intracellular [Ca2+] following activation by G-protein-coupled receptors or receptor tyrosine kinases (1). TRPC6 is directly activated by diacylglycerol (DAG) (2). Various tissues express TRPC6, including brain, lung, kidney, ovary and small intestine. TRPC6 exerts a variety of biological functions in various tissues. In brain, TRPC6 plays important roles in synaptic plasticity, spatial cognition (3) and protects neurons from ischemic excitotoxicity (4). In kidney, TRPC6 is expressed in mesangial cells and podocytes of renal glomeruli (5) and regulates glomerular filtration (6). Mutations in TRPC6 gene cause autosomal dominant focal segmental glomerulosclerosis (7). In smooth muscle cells, TRPC6 mediates Na+ influx followed by Ca2+ entry via Na+/Ca2+ -exchanger (NCX) reversal which leads to contraction (8, 9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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