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Monoclonal Antibody Immunohistochemistry Paraffin Glutamate Secretion

Also showing Monoclonal Antibody Immunohistochemistry Paraffin Regulation of Glutamate Secretion

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

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

Background: Adenosine Receptor A2a (A2AR) is a G-protein-coupled receptor (GPCR). As a member of the purinergic adenosine receptors (A1, A2, and A3), A2AR activates classic G-protein signaling pathways upon binding of adenosine (1). Adenosine is present in all cells and extracellular fluids. Adenosine signaling, via A2AR, is mobilized during both physiological and pathological conditions. For example, adenosine, via A2AR, modulates neuronal function, acting to fine-tune neuronal function (2). A2AR function is modulated, in part, by its ability to form functional heteromers with other GPCRs, including dopamine receptors (D1 and D3), metabotropic glutamate receptors (mGluR5), and others (3). In the brain, A2AR is enriched in the basal ganglia, suggesting that A2AR may be a potential drug target for neurodegenerative diseases like Parkinson’s disease, drug addiction, and psychiatric disorders (4). Outside of the brain, A2AR may act as an immune checkpoint molecule to maintain an immunosuppressive tumor microenvironment, an environment that exhibits relatively elevated adenosine levels (5, 6).

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

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

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Interleukin-1β (IL-1β), one of the major caspase-1 targets, is a multifunctional cytokine that is involved in a host of immune and proinflammatory responses (1). It is produced primarily by activated monocytes and macrophages. It signals through various adaptor proteins and kinases that lead to activation of numerous downstream targets (2-6). Human IL-1β is synthesized as a 31 kDa precursor. To gain activity, the precursor must be cleaved by caspase-1 between Asp116 and Ala117 to yield a 17 kDa mature form (7,8). Detection of the 17 kDa mature form of IL-1β is a good indicator of caspase-1 activity.

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

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

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Vesicle-associated membrane protein 2 (VAMP2, also called synaptobrevin) is part of the R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex (1). The SNARE complex is involved in vesicular transport and membrane fusion, a process regulated by calcium (2). In neurons, VAMP2 is predominantly inserted in presynaptic vesicle membranes. Assembly of VAMP2 with the plasma membrane SNAREs syntaxin 1 and SNAP25 is a key event necessary for membrane fusion and neurotransmitter release (2). In addition to this important function, VAMP2 is also involved in granule exocytosis in neutrophils (3) and release of bioactive peptides from cardiac myocytes (4) and juxtaglomerular cells (5).

$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, Monkey, Mouse, Rat

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

Background: Glutamate dehydrogenase is a mitochondrial enzyme that catalyzes the oxidative deamination of glutamate to α-ketoglutarate through association with the cofactor nicotinamide adenine dinucleotide phosphate (1). Glutamate dehydrogenase is highly expressed in various tissues such as the liver, brain, kidney, heart, pancreas, ovaries, and testis. Two isoforms produced by two distinct genes are found in mammalian tissues. The GLUD1 gene is ubiquitously expressed (2), while the GLUD2 gene is specifically expressed in testicular tissues and astrocytes (3,4). Glutamate dehydrogenase links glutamate to the Krebs cycle, thereby playing a critical role in the regulation of energy homeostasis. Research studies have shown that changes in glutamate dehydrogenase activity in pancreatic β-cells can cause a hyperinsulinism syndrome (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin)

Background: Glutamate-ammonia ligase (GLUL), also known as glutamine synthetase (GS), catalyzes the de novo synthesis of glutamine from glutamate and ammonia. GLUL is ubiquitously expressed with particularly high expression in the muscle, liver, and brain (1). GLUL expression is elevated in various cancers. Its expression is upregulated by oncogenic c-Myc (2). High expression of GLUL in breast cancer patients is associated with larger tumor size and high level of HER2 expression. It is a predictor of poor survival in patients with glioma and liver cancers (3-6).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Huntington's Disease (HD) is a fatal neurodegenerative disorder characterized by psychiatric, cognitive, and motor dysfunction. Neuropathology of HD involves specific neuronal subpopulations: GABA-ergic neurons of the striatum and neurons within the cerebral cortex selectively degenerate (1,2). The genetic analysis of HD has been the flagship study of inherited neurological diseases from initial chromosomal localization to identification of the gene.Huntingtin is a large (340-350 kD) cytosolic protein that may be involved in a number of cellular functions such as transcription, gastrulation, neurogenesis, neurotransmission, axonal transport, neural positioning, and apoptosis (2,3). The HD gene from unaffected individuals contains between 6 and 34 CAG trinucleotide repeats, with expansion beyond this range causing the onset of disease symptoms. A strong inverse correlation exists between the age of onset in patients and the number of huntingtin gene CAG repeats encoding a stretch of polyglutamine peptides (1,2). The huntingtin protein undergoes numerous post-translational modifications including phosphorylation, ubiquitination, sumoylation, palmitoylation, and cleavage (2). Phosphorylation of Ser421 by Akt can partially counteract the toxicity that results from the expanded polyglutamine tract. Varying Akt expression in the brain correlates with regional differences in huntingtin protein phosphorylation; this pattern inversely correlates with the regions that are most affected by degeneration in diseased brain (2). A key step in the disease is the proteolytic cleavage of huntingtin protein into amino-terminal fragments that contain expanded glutamine repeats and translocate into the nucleus. Caspase mediated cleavage of huntingtin at Asp513 is associated with increased polyglutamine aggregate formation and toxicity. Phosphorylation of Ser434 by CDK5 protects against cleavage (2,3).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: GAS6 (Growth Arrest Specific gene 6) is a vitamin K-dependent ligand of the TAM (Tyro3, Axl and MerTK) RTK family. It has an N-terminal Gla domain containing multiple Asp gamma-carboxylation sites, followed by four EGF repeats and two C-terminal LG domains. Vitamin K mediates multiple gamma-carboxylations of glutamic acid residues in the GAS6 Gla domain. These modifications are required for GAS6 to to activate its receptor (1,2). The two C-terminal LG (SHBG) domains form a V-shaped structure and provide a direct binding site for receptor interaction. Among the TAM family members, GAS6 has high affinity for Axl and low affinity for Tyro3 and MerTK. Ligand/receptor interaction activates multiple downstream signaling pathways such as PI3K/AKT, STAT/SOCS, PLC/FAK, and Grb2/RAS, and promotes cell survival, proliferation, migration and differentiation (3,4). GAS6 has been implicated in cancer development and immune-related disorders (inflammation and multiple sclerosis), and as such has been identified as a potential therapeutic target (3-6).