You Searched For: bra30

Catalog Number: (10800-146)

Supplier: Rockland Immunochemical

Description: Ataxin-1 is a member of the ATXN1 protein family and contains a single AXH domain. It is a neurodegenerative disorder protein thought to have a role in the metabolism of RNA as it has been shown to localize to the RNA and transcription dependent inclusions within the nucleus. A mutation of Ataxin-1 is the cause of spinocerebellar ataxia type-1 (SCA1), a progressive, neurodegenerative disease that is autosomal dominant and primarily affects the Purjinke cells found in brain stem neuronal populations and the cerebellum. Expression of Ataxin-1 is almost ubiquitous, except in the brain where it is isolated to populations of neurons. Anti-Ataxin-1 is ideal for research in Neuroscience.

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Catalog Number: (10108-316)

Supplier: Prosci

Description: GAMT is a methyltransferase that converts guanidoacetate to creatine, using S-adenosylmethionine as the methyl donor. Defects in its gene have been implicated in neurologic syndromes and muscular hypotonia, probably due to creatine deficiency and accumulation of guanidinoacetate in the brain of affected individuals.The protein encoded by this gene is a methyltransferase that converts guanidoacetate to creatine, using S-adenosylmethionine as the methyl donor. Defects in this gene have been implicated in neurologic syndromes and muscular hypotonia, probably due to creatine deficiency and accumulation of guanidinoacetate in the brain of affected individuals. Two transcript variants encoding different isoforms have been described for this gene.

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Catalog Number: (10424-782)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

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Catalog Number: (10424-960)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

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Catalog Number: (10424-770)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

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Catalog Number: (76081-284)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

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Catalog Number: (10662-888)

Supplier: Bioss

Description: The oligodendrocyte lineage-specific basic helix-loop-helix (OLIG) family of transcription factors include OLIG1-OLIG3, which differ in tissue expression. OLIG1 and OLIG2 are specifically expressed in nervous tissue as gene regulators of oligodendrogenesis. OLIG2 is more widely expressed in embryonic brain than OLIG1, while OLIG3 is primarily expressed in non-neural tissues. OLIG1 and OLIG2 interact with the Nkx-2.2 homeodomain protein, which is responsible for directing ventral neuronal patterning in response to graded Sonic hedgehog signaling in the embryonic neural tube. These interactions between OLIG proteins and Nkx-2.2 appear to promote the formation of alternate cell types by inhibiting V3 interneuron development. OLIG1 and OLIG2 are abundantly expressed in oligodendroglioma and nearly absent in astrocytomas. Therefore, OLIG proteins are candidates for molecular markers of human glial brain tumors, which are the most common primary malignancies of the human brain.

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Catalog Number: (89365-270)

Supplier: Genetex

Description: Neuromedin U Receptor 2 is a Neuromedin Receptor. NMU2R may mediate the contractile activity of neuromedin U in the uterus. Neuromedin U Receptor 2 has been reported in the central nervous system and in the uterus. ESTs have been isolated from diseased brain and colon carcinoma libraries.

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Catalog Number: (10424-784)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

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Catalog Number: (76081-282)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

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Catalog Number: (10480-124)

Supplier: Bioss

Description: Carbonic anhydrases (CAs) are members of a large family of zinc metalloenzymes responsible for catalyzing the reversible hydration of carbon dioxide. CAs show extensive diversity in their distribution and subcellular localization. They are involved in a variety of biological processes, including calcification, bone resorption, respiration, acid-base balance and the formation of aqueous humor, saliva, gastric juice and cerebrospinal fluid. CA XI, also referred to as carbonic anhydrase-related protein 11 precursor (CA-RP XI) or carbonic anhydrase-related protein 2 (CA-RP II), is a member of the carbonic anhydrase family that lacks two of the three Zn-binding motifs essential for carbonic anhydrase activity. For this reason, CA XI does not exhibit catalytic activity. It is expressed primarily in brain but is also found in spinal cord and thyroid. CA XI may play a role in brain development.Tissue specificity:Expressed abundantly in the brain with moderate expression also present in spinal cord and thyroid.

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Catalog Number: (10338-864)

Supplier: Bioss

Description: Regulator of microtubule stability. When phosphorylated by MAPK8, stabilizes microtubules and consequently controls neurite length in cortical neurons. In the developing brain, negatively regulates the rate of exit from multipolar stage and retards radial migration from the ventricular zone (By similarity).

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Catalog Number: (10453-984)

Supplier: Bioss

Description: Enhances transcription activation by YY1.Tissue specificity:Ubiquitous. Detected in small intestine, skeletal muscle, lung, pancreas, brain, stomach, spleen, colon and heart. Detected at very low levels in healthy liver. Highly expressed in most liver carcinomas.

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Catalog Number: (10270-684)

Supplier: Bioss

Description: Glutamate receptors mediate most excitatory neurotransmissions in the brain and play an important role in neural plasticity, neural development and neurodegeneration. Ionotropic glutamate receptors are divided into two categories, namely NMDA receptors and kainate/AMPA receptors, both of which contain glutamate-gated, cation-specific ion channels. Kainate/AMPA receptors consist of seven structurally related subunits, designated GluR-1 to -7, and are primarily responsible for fast excitatory neurotransmissions carried out by glutamate. GluR-delta 1 (Glutamate receptor delta-1 subunit), also known as GRID1, is a multi-pass membrane protein that belongs to the kainate/AMPA receptor family and is expressed primarily in the brain. Localized to the cell junction and the postsynaptic cell membrane, GluR-delta 1 functions as a glutamate receptor that regulates synaptic transmissions in the central nervous system (CNS) and is thought to play an important role in synaptic plasticity. Defects in the gene encoding GluR-delta 1 are associated with schizophrenia, a chronic and severe brain disorder.

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Catalog Number: (10267-236)

Supplier: Bioss

Description: LIMK 1 and 2 likely regulate aspects of the cytoskeleton, through control of the organization of actin filaments. They can phosphorylate an actin-binding protein, cofilin which binds to actin monomers and polymers and promotes the disassembly of actin filament.The phosphorylation of cofilin via LIMK inactivates this potential. LIMK1 is highly active in the brain and spinal chord, where it is believed to be involved in the development of nerve cells whilst LIMK2 is ubiquitously expressed in many adult tissues. LIMK1 may play an important role in areas of the brain that are responsible for processing visual-spatial information (visuospatial constructive cognition). These parts of the brain are important for visualizing an object as a set of parts and performing tasks such as writing, drawing, constructing models, and assembling puzzles. LIMK1 is specifically stimulated by Rac, one of the Rho family proteins, while LIMK2 activity is activated under the control of other Rho family members, Rho and Cdc42, suggesting that two distinct pathways exist in the Rho family driven actin cytoskeleton dynamics.

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Catalog Number: (10270-682)

Supplier: Bioss

Description: Glutamate receptors mediate most excitatory neurotransmissions in the brain and play an important role in neural plasticity, neural development and neurodegeneration. Ionotropic glutamate receptors are divided into two categories, namely NMDA receptors and kainate/AMPA receptors, both of which contain glutamate-gated, cation-specific ion channels. Kainate/AMPA receptors consist of seven structurally related subunits, designated GluR-1 to -7, and are primarily responsible for fast excitatory neurotransmissions carried out by glutamate. GluR-delta 1 (Glutamate receptor delta-1 subunit), also known as GRID1, is a multi-pass membrane protein that belongs to the kainate/AMPA receptor family and is expressed primarily in the brain. Localized to the cell junction and the postsynaptic cell membrane, GluR-delta 1 functions as a glutamate receptor that regulates synaptic transmissions in the central nervous system (CNS) and is thought to play an important role in synaptic plasticity. Defects in the gene encoding GluR-delta 1 are associated with schizophrenia, a chronic and severe brain disorder.

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