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Product listing: DJ-1 Antibody, UniProt ID Q99497 #2134 to LRP1 Antibody, UniProt ID Q07954 #64099

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Western Blotting

Background: Parkinson's disease (PD) is characterized by the presence of Lewy bodies (intracellular inclusions) and by the loss of dopaminergic neurons. Research studies have shown that mutations in α-synuclein, Parkin, and DJ-1 are linked to PD (1). α-synuclein is a major component of the aggregates found in Lewy bodies. Parkin is involved in protein degradation through the ubiquitin-proteasome pathway, and investigators have shown that mutations in Parkin cause early onset of PD (1). Loss-of-function mutations in DJ-1 cause early onset of PD, but DJ-1 is associated with multiple functions: it cooperates with Ras to increase cell transformation, it positively regulates transcription of the androgen receptor, and it may function as an indicator of oxidative stress (2-5). Dopamine D2 receptor-mediated functions are greatly impaired in DJ-1 (-/-) mice, resulting in reduced long-term depression (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Dopamine β-Hydroxylase (DBH) is an enzyme of the copper type II ascorbate-dependent mono-oxygenase family. This enzyme forms homotetramers composed of two noncovalently bound disulfide-linked dimers and is found as both membrane-associated and soluble forms (1-3). The soluble form is present in the lumen of secretory granules (4) and is released from cells by exocytosis (5). DBH converts dopamine to noradrenaline (6). Deficiency in this enzyme causes a rare disease characterized by a complete absence of noradrenaline and adrenaline in plasma together with increased plasma dopamine levels (7). Orthostatic hypotension, the main symptom of DBH deficiency, can be alleviated by administration of dihydroxyphenylserine, a synthetic precursor of noradrenaline (8).

$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, 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).

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

Application Methods: Western Blotting

Background: Developmentally-regulated brain proteins (Drebrins) are cytoplasmic proteins that were originally identified in the brain as F-actin-binding proteins. There are two mammalian isoforms: adult type (A) and embryonic type (E). These isoforms are derived from a single gene through alternative RNA splicing mechanisms (1). Drebrin E has been observed to accumulate in the developmental stage of migrating neurons and in the growing cell processes of neurons. Drebrin A is found at the dendritic spines of mature cortical neurons where it plays a role in synaptic plasticity (2,3). Although drebrins are primarily found in neurons, they have also been found in skeletal muscle, heart, pancreas, and kidney. Research studies have shown that reduced expression of drebrin in the brain could be associated with Alzheimer’s Disease, Down Syndrome (4), and bipolar disorders (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Developmentally-regulated brain proteins (Drebrins) are cytoplasmic proteins that were originally identified in the brain as F-actin-binding proteins. There are two mammalian isoforms: adult type (A) and embryonic type (E). These isoforms are derived from a single gene through alternative RNA splicing mechanisms (1). Drebrin E has been observed to accumulate in the developmental stage of migrating neurons and in the growing cell processes of neurons. Drebrin A is found at the dendritic spines of mature cortical neurons where it plays a role in synaptic plasticity (2,3). Although drebrins are primarily found in neurons, they have also been found in skeletal muscle, heart, pancreas, and kidney. Research studies have shown that reduced expression of drebrin in the brain could be associated with Alzheimer’s Disease, Down Syndrome (4), and bipolar disorders (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The DYRK family includes several dual-specificity tyrosine-phosphorylated and regulated kinases capable of phosphorylating proteins at both Tyr and Ser/Thr residues (1). The DYRK family was identified based on homology to the yeast Yak1 (2) and the Drosophila minibrain (mnb) kinases (3). Seven mammalian isoforms have been discovered, including DYRK1A, DYRK1B, DYRK1C, DYRK2, DYRK3, DYRK4, and DYRK4B. Differences in substrate specificity, expression, and subcellular localization are seen across the DYRK family (4,5). All DYRK proteins have a Tyr-X-Tyr motif in the catalytic domain activation loop; phosphorylation of the second Tyr residue (e.g. Tyr312 of DYRK1A) is necessary for kinase activity. DYRKs typically autophosphorylate the Tyr residue within their activation loop, but phosphorylate substrates at Ser and Thr residues (1,6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The DYRK family includes several dual-specificity tyrosine-phosphorylated and regulated kinases capable of phosphorylating proteins at both Tyr and Ser/Thr residues (1). The DYRK family was identified based on homology to the yeast Yak1 (2) and the Drosophila minibrain (mnb) kinases (3). Seven mammalian isoforms have been discovered, including DYRK1A, DYRK1B, DYRK1C, DYRK2, DYRK3, DYRK4, and DYRK4B. Differences in substrate specificity, expression, and subcellular localization are seen across the DYRK family (4,5). All DYRK proteins have a Tyr-X-Tyr motif in the catalytic domain activation loop; phosphorylation of the second Tyr residue (e.g. Tyr312 of DYRK1A) is necessary for kinase activity. DYRKs typically autophosphorylate the Tyr residue within their activation loop, but phosphorylate substrates at Ser and Thr residues (1,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Dysbindin, or dystrobrevin-binding protein 1, is a coiled-coil-containing protein expressed in muscle and brain that was identified as a binding partner of dystrobrevin (1). Dysbindin upregulates expression of the pre-synaptic proteins SNAP25 and synapsin I, thereby increasing glutamate release and promoting neuronal viability through Akt signaling. In particular, Akt phosphorylation is suppressed with downregulation of dysbindin and increased with upregulation of dysbindin (2). A nonsense mutation of dysbindin causes Hermansky-Pudlak disease, an autosomal recessive disorder characterized by lysosomal storage defects and prolonged bleeding. (2). Genetic variation in the gene encoding dysbindin is strongly associated with schizophrenia and protein levels are reduced in the prefrontal cortex, midbrain and hippocampus of brains from patients with schizophrenia (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system. During neurotransmission, glutamate is released from vesicles of the pre-synaptic cell, and glutamate receptors (e.g. NMDA Receptor, AMPA Receptor) bind glutamate for activation at the opposing post-synaptic cell. Excitatory amino acid transporters (EAATs) regulate and maintain extracellular glutamate concentrations below excitotoxic levels. In addition, glutamate transporters may limit the duration of synaptic excitation by an electrogenic process in which the transmitter is cotransported with three sodium ions and one proton, followed by countertransport of a potassium ion. Five EAATs (EAAT1-5) are characterized: EAAT2 (GLT-1) is primarily expressed in astrocytes but is also expressed in neurons of the retina and during fetal development (1). Homozygous EAAT2 knockout mice have spontaneous, lethal seizures and an increased predisposition to acute cortical injury (2). PKC phosphorylates Ser113 of EAAT2 and coincides with glutamate transport (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system. During neurotransmission, glutamate is released from vesicles of the pre-synaptic cell, and glutamate receptors (e.g. NMDA Receptor, AMPA Receptor) bind glutamate for activation at the opposing post-synaptic cell. Excitatory amino acid transporters (EAATs) regulate and maintain extracellular glutamate concentrations below excitotoxic levels. In addition, glutamate transporters may limit the duration of synaptic excitation by an electrogenic process in which the transmitter is cotransported with three sodium ions and one proton, followed by countertransport of a potassium ion. Five EAATs (EAAT1-5) are characterized: EAAT2 (GLT-1) is primarily expressed in astrocytes but is also expressed in neurons of the retina and during fetal development (1). Homozygous EAAT2 knockout mice have spontaneous, lethal seizures and an increased predisposition to acute cortical injury (2). PKC phosphorylates Ser113 of EAAT2 and coincides with glutamate transport (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Early growth response 3 (EGR3) is a zinc finger transcription factor and one of four members of the early growth response family (1). Members of this family are basally expressed in the brain (2) and are immediate early response genes that are important for the induction of cellular programs of differentiation, proliferation, and cell death in response to environmental stimuli (1). EGR3 plays important roles in cellular growth and neuronal development (2) and an essential role in learning and memory processing of both short- and long-term hippocampus-dependent memory; it also mediates adaptation to stress and novelty (3). Research studies show that a lack of EGR3 results in abnormal neuronal and T cell development (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: FE65, FE65L1 and FE65L2 are members of the FE65 protein family. FE65 is an adaptor protein with protein-protein interaction domains including a WW domain followed by two phosphotyrosine interaction domains (PID1 and PID2) (1). Amyloid beta precursor protein (APP) binds to PID2 and undergoes sequential cleavage. First alpha-/beta secretases cleave and release the ectodomain into the extracellular environment. Subsequent processing by the gamma-secretase complex results in the APP intracellular domain (AICD) and the beta-amyloid peptides. The latter A-beta fragments form the main components of amyloid plaques in patients with Alzheimer's disease (2). FE65 family members can regulate APP processing, resulting in elevated levels of A-beta (3). Double knock-out mice of FE65 and FE65L1 display a phenotype that occurs in animals lacking APP family members, supporting a functional interaction between FE65 and APP (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: GABA (γ-aminobutyric acid) is the primary inhibitory neurotransmitter in the central nervous system and interacts with three different receptors: GABA(A), GABA(B) and GABA(C) receptor. The ionotropic GABA(A) and GABA(C) receptors are ligand-gated ion channels that produce fast inhibitory synaptic transmission. In contrast, the metabotropic GABA(B) receptor is coupled to G proteins that modulate slow inhibitory synaptic transmission (1). Functional GABA(B) receptors form heterodimers of GABA(B)R1 and GABA(B)R2 where GABA(B)R1 binds the ligand and GABA(B)R2 is the primary G protein contact site (2). Two isoforms of GABA(B)R1 have been cloned: GABA(B)R1a is a 130 kD protein and GABA(B)R1b is a 95 kD protein (3). G proteins subsequently inhibit adenyl cylase activity and modulate inositol phospholipid hydrolysis. GABA(B) receptors have both pre- and postsynaptic inhibitions: presynaptic GABA(B) receptors inhibit neurotransmitter release through suppression of high threshold calcium channels, while postsynaptic GABA(B) receptors inhibit through coupled activation of inwardly rectifying potassium channels. In addition to synaptic inhibition, GABA(B) receptors may also be involved in hippocampal long-term potentiation, slow wave sleep and muscle relaxation (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: GABA (γ-aminobutyric acid) is the primary inhibitory neurotransmitter in the central nervous system and interacts with three different receptors: GABA(A), GABA(B) and GABA(C) receptor. The ionotropic GABA(A) and GABA(C) receptors are ligand-gated ion channels that produce fast inhibitory synaptic transmission. In contrast, the metabotropic GABA(B) receptor is coupled to G proteins that modulate slow inhibitory synaptic transmission (1). Functional GABA(B) receptors form heterodimers of GABA(B)R1 and GABA(B)R2 where GABA(B)R1 binds the ligand and GABA(B)R2 is the primary G protein contact site (2). Two isoforms of GABA(B)R1 have been cloned: GABA(B)R1a is a 130 kD protein and GABA(B)R1b is a 95 kD protein (3). G proteins subsequently inhibit adenyl cylase activity and modulate inositol phospholipid hydrolysis. GABA(B) receptors have both pre- and postsynaptic inhibitions: presynaptic GABA(B) receptors inhibit neurotransmitter release through suppression of high threshold calcium channels, while postsynaptic GABA(B) receptors inhibit through coupled activation of inwardly rectifying potassium channels. In addition to synaptic inhibition, GABA(B) receptors may also be involved in hippocampal long-term potentiation, slow wave sleep and muscle relaxation (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The enzyme glutamate decarboxylase (GAD) is responsible for the synthesis of the essential neurotransmitter gamma-aminobutyric acid (GABA) from L-glutamic acid (1). GAD1 (GAD67) and GAD2 (GAD65) are expressed in nervous and endocrine systems (2) and are thought to be involved in synaptic transmission (3) and insulin secretion (4), respectively. Autoantibodies against GAD2 may serve as markers for type I diabetes (5). Many individuals suffering from an adult onset disorder known as Stiff Person Syndrome (SPS) also express autoantibodies to GAD2 (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: The enzyme glutamate decarboxylase (GAD) is responsible for the synthesis of the essential neurotransmitter gamma-aminobutyric acid (GABA) from L-glutamic acid (1). GAD1 (GAD67) and GAD2 (GAD65) are expressed in nervous and endocrine systems (2) and are thought to be involved in synaptic transmission (3) and insulin secretion (4), respectively. Autoantibodies against GAD2 may serve as markers for type I diabetes (5). Many individuals suffering from an adult onset disorder known as Stiff Person Syndrome (SPS) also express autoantibodies to GAD2 (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: GAP43 is a nervous system specific, growth-associated protein enriched in growth cones and areas of high plasticity (1). Phosphorylation of GAP43 at Ser41 by PKC is regulated by intracellular Ca2+ and affects the ability of GAP43 to bind calmodulin (2,3). GAP43 is integral to growth cone formation, neurite outgrowth, and the development of a functional cerebral cortex (4,5). Aberrant GAP43 expression can be seen in patients diagnosed with schizophrenia and Alzheimer's disease (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The solute carrier 6 gene (SLC6), also known as the neurotransmitter–sodium-symporter family or Na+/Cl- -dependent transporter, encodes for proteins that regulate neurotransmitter (NTT) transport, including monoamine transmitters serotonin, dopamine, and norepinephrin (SERT), GABA transmitters (GAT1, GAT2, GAT3, and BGT1), and glycine transmitters (GLYT1 and GLYT2) (1). These proteins express ubiquitously in the brain and regulate the release and uptake of neurotransmitters in terminal clefts, in both neuronal and non-neuronal cells (2-4). Dysregulation of NTT-transporters is associated with neurological disease like epilepsy, schizophrenia, anxiety, bipolar disorder, and addictions to cocaine and methamphetamines (1). Inhibitors of NTT-transporters are widely used as drugs to treat disorders like depression (tricyclic antidepressants), and antiepileptic tiagabine (5). GAT1 is the only GABA transporter genetically studied in GAT1-KO mouse models where an accumulation of extracellular GABA, leading to a decrease in anxiety and depression-like behaviors (6-8). The lack or reduction of GAT1 diminished aggression in mice, and a condition known as hypoaglesia, where there is a decreased sensitivity to painful stimuli (8,9). GAT1 post-translational modifications include phosphorylation at Tyr107 (IL1), and Tyr317 (IL3), and these mutations identify as the phospho-acceptor-sites, therefore regulating GAT1 (10,11). GABA trafficking is regulated by Tyr phosphorylation, and it has been shown that activation of adenosine A2A receptors in the hippocampus synaptosomes enhanced BAGA uptake by opposing a constitutive PKC-mediated down-regulation of GAT1 (11-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The neurotransmitters GABA and glycine activate ligand-gated chloride channels and thus mediate fast synaptic inhibition. Gephyrin is a postsynaptic, scaffolding protein anchoring type A GABA and glycine receptors to the cytoskeleton. In addition to gephyrin’s function clustering synaptic neurotransmitter receptors, it plays an essential role in the biosynthesis of the molybdenum cofactor (MoCo). Molybdenum cofactor chelates and activates sulfite oxidase, an enzyme crucial for survival (1). GSK-3β and Erk1/2 phosphorylate gephyrin at residue Ser270 and Ser268, respectively. These post-translational modifications alter the clustering of gephyrin, effecting the amplitude and frequency of GABAergic inhibitory currents (2,3). Researchers are analyzing the role of abnormal gephyrin clustering and function in major neurological, neuro-developmental and psychiatric disorders (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: GGA3 is a member of the GGA family of proteins which also includes GGA1 and GGA2. These proteins consist of four distinct segments: a VHS domain that binds the di-leucine sorting signal DXXLL; a GAT domain that binds Arf-GTP; a hinge region that recruits clathrin; and a GAE domain that has sequence similarity to γ-adaptin and recruits a number of proteins. Arf1-GTPase recruits GGA3 to the trans-Golgi network. GGAs sort acid hydrolases to the lysosome and are involved in transporting proteins containing the DXXLL signal from the Golgi complex to the endosome (1). During apoptosis or cerebral ischemia, GGA3 is cleaved by caspase-3 at Asp313, reducing GGA3 levels and lysosomal degradation of β-secretase (BACE). The resulting elevated amount and activity of BACE plays a role in amyloid-β (Aβ) production, consistent with BACE elevation and Aβ accumulation in Alzheimer’s Disease (2).

$260
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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Heterotrimeric guanine nucleotide-binding proteins, G proteins, transduce ligand binding to G protein-coupled receptors (GPCRs) into intracellular responses (1). G proteins are comprised of 3 subunits, alpha (Gα), beta (Gβ), and gamma (Gγ). Upon activation of GPCRs, the receptor promotes the exchange of GDP to GTP of Gα, changing the confirmation of the switch regions within Gα. The receptor bound heterotimeric G protein (inactive) is then released, and dissociates into the GTP-bound Gα (active) monomer and the Gβ/Gγ heterodimer (1,2). Gα activates adenylyl cyclase, which converts ATP to the second messenger cAMP. Gα also activates phosphoinositide-specific phospholipase C (PLC), which catalyzes hydrolysis of the phospholipid of phosphatidylinositol 4,5-biphosphate (PIP2), releasing the second messengers IP3 and 1,2-diacylglycerol (DAG). IP3 activates IP3 receptors to release Ca2+ from the ER. DAG is an activator of protein kinase C (PKC), which in turn activates the Erk1/2 pathway (1,3). The primary function of the Gβ/Gγ heterodimer is to inhibit Gα, although it may also activate second messengers (e.g. PLC pathway) or gate ion channels (e.g. GIRK) (1). Guanine nucleotide-binding protein b3 (GNB3) is an isoform of the b subunit. Research studies have shown that a polymorphism in the GNB3 gene, C825T, is associated with hypertension, obesity, and depression (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: GTPase Regulator Associated with Focal Adhesion Kinase-1 (GRAF1), is a GTPase-activating protein for the small G proteins RhoA and Cdc42 (1). It is composed of an N-terminal BAR domain, a PH domain, a RhoGAP domain, a proline-rich domain, and a C-terminal SH3 domain. GRAF1 contributes to the clathrin-independent carriers/GPI-enriched early endosomal compartments (CLIC/GEEC) pathway, and was the first specific protein component of this endocytic pathway to be discovered (2). GRAF1 was identified as an important protein necessary for adeno-associated virus 2 infection (3). In addition, research studies have linked GRAF1 to mental retardation (4), skeletal muscle differentiation (5), and myeloid leukemia (6,7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: G-protein-coupled receptor kinase 2 (GRK2), also known as beta-adrenergic receptor kinase 1 (beta-ARK1), 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). GRK2 kinase activity and cellular localization are tightly regulated by interactions with activated receptors, G-beta and G-gamma subunits, adaptor proteins, phospholipids, caveolin and calmodulin, as well as by phosphorylation (1). PKC phosphorylation enhances GRK2 activity by promoting its membrane localization and by abolishing the inhibitory association of calmodulin (2,3). PKA phosphorylates GRK2 at Ser685, which facilitates the association of GRK2 with a beta-adrenergic receptor (4). Erk inhibits GRK2 activity via phosphorylation at Ser670 (5). Src phosphorylates GRK2 at multiple tyrosine residues (Tyr13, 86 and 92), which activates GRK2 activity and promotes GRK2 degradation (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Homer1, Homer2 and Homer3 are scaffolding proteins, composed of an EVH protein–binding domain, a coiled-coil domain and a leucine zipper domain. The EVH domain is a protein-protein binding module that binds to the proline-rich motifs PPXXF, PPXF, and LPSSP of G protein–coupled receptors (GPCRs), inositol 1,4,5-triphosphate (IP3) receptors (IP3Rs), ryanodine receptors, and TRP channels (1-2). The coiled-coil and the leucine zipper domains cause multimerization of Homers and assemble signaling proteins complexes. The Homer1 gene encodes a short isoform (Homer1a, aa 1-186) and two long isoforms (Homer1b, aa 1-354; Homer1c, aa 1-366). Homer1a lacks the coiled-coil domain and leucine zipper, antagonizing multimerization of Homers and thus disassembling signaling proteins complexes (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: JAKMIP1, or Janus kinase and microtubule interactin protein 1, localizes in mitrotubules and the plasma membrane, which associates with microtubules and plays a role in migration of pyramidal neurons (1). JAKMIP1 participates in the microtubule-dependent transport of GABA-B receptor (2). It is also linked to autistic-spectrum disorders (3,4). JAKMIP1 may participate in the JAK1 pathway (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Leucine-rich repeat and immunoglobulin domain-containing protein (LINGO-1) is a potent negative modulator of neuronal processes including neuronal survival, axonal integrity, oligodendrocyte differentiation, and myelination (1-5). LINGO-1, Nogo receptor (NgR), and p75 neurotrophin receptor (p75NTR), or TNF receptor orphan Y (TROY) form a tripartite receptor complex, which activates RhoA/ROCK signaling and is responsible for the inhibition effect of myelin- associated factors (6,7). LINGO-1 is abundantly expressed in the brain and is implicated in various neurodegenerative disorders such as Essential tremor, multiple sclerosis and Parkinson’s disease (8-11). Recently, LINGO-1 was reported to bind directly to amyloid precursor protein (APP), promoting its degradation through lysosomal proteolysis (12). This research study implicated that Lingo-1 plays a critical role in the pathophysiology of Alzheimer's disease.

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

Application Methods: Western Blotting

Background: LIS1 is a cytoskeleton-interacting protein that contains an N-terminal dimerization domain and a C-terminal β-propeller domain that interacts with the motor domain of dynein (1-3). Research studies have shown that mutations in the LIS1 gene are involved in lissencephaly, a disease characterized by severe defects in brain development (4). LIS1 also plays a critical role in cortical migration and development in the brain (5). LIS1 activity is required for retrograde translocation of excitatory synapses in developing interneuron dendrites in a microtubule-dependent fashion (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Low density lipoprotein receptor related protein 1 ( LRP1) is a type I transmembrane receptor that mediates the endocytosis of various ligands (1). LRP1 plays important roles in lipid homeostasis, signaling transduction, embryonic development, and glucose metabolism (2-6). In addition, LRP1 regulates APP processing and facilitates the clearance of beta-amyloid (7-9). This finding makes LRP1 a potential therapeutic target for Alzheimer’s disease. LRP1 preprotein is proteolytically processed by furin to generate a 515 kDa extracellular α subunit and a membrane-anchored 85 kDa β subunit, which together form the mature receptor (10).