"L-Ornithine+L-Aspartate"

Supplier: Bioss

N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate-gated ion channels. These receptors have been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of the key receptor subunit NMDAR1 (GRIN1) and 1 or more of the 4 NMDAR2 subunits: NMDAR2A (GRIN2A), NMDAR2B (GRIN2B), NMDAR2C (GRIN2C) and NMDAR2D (GRIN2D). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2008]

Supplier: Bioss

N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate receptors. NMDA receptor channel has been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of three different subunits: NR1 (GRIN1), NR2 (GRIN2A, GRIN2B, GRIN2C, or GRIN2D) and NR3 (GRIN3A or GRIN3B). The NR2 subunit acts as the agonist binding site for glutamate. This receptor is the predominant excitatory neurotransmitter receptor in the mammalian brain. [provided by RefSeq, Jul 2008].

Supplier: Bioss

ZNF148 is a zinc finger transcription factor that is universally expressed. ZBP-89, a Kruppel-like repressor protein, is the silencer element binding factor for Vimentin. ZBP-89 has been shown to bind to GC-rich DNA elements in promoters for gastrin, ornithine decarboxylase and the cyclin-dependent kinase inhibitor p21 (also designated Cip1 or WAF1). ZBP-89 expression is induced by trans-retinoic acid or butyrate, which also induces terminal differentiation of colon cancer cells. ZBP-89 cooperates with histone acetyltransferase coactivator p300 in the regulation of p21, a cyclin-dependent kinase inhibitor whose associated gene is a target gene of p53. ZBP-89 also regulates cell proliferation, in part, through its ability to directly bind the p53 protein and retard its nuclear export. Elevated levels of ZBP-89 induce growth arrest and apoptosis in human gastrointestinal cells.

Supplier: Biorbyt

Anti-ODC1 Rabbit Polyclonal Antibody

Supplier: Bioss

N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate-gated ion channels. These receptors have been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of the key receptor subunit NMDAR1 (GRIN1) and 1 or more of the 4 NMDAR2 subunits: NMDAR2A (GRIN2A), NMDAR2B (GRIN2B), NMDAR2C (GRIN2C) and NMDAR2D (GRIN2D). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2008]

Supplier: Bioss

N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate receptors. NMDA receptor channel has been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of three different subunits: NR1 (GRIN1), NR2 (GRIN2A, GRIN2B, GRIN2C, or GRIN2D) and NR3 (GRIN3A or GRIN3B). The NR2 subunit acts as the agonist binding site for glutamate. This receptor is the predominant excitatory neurotransmitter receptor in the mammalian brain. [provided by RefSeq, Jul 2008].

Supplier: Bioss

N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate receptors. NMDA receptor channel has been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of three different subunits: NR1 (GRIN1), NR2 (GRIN2A, GRIN2B, GRIN2C, or GRIN2D) and NR3 (GRIN3A or GRIN3B). The NR2 subunit acts as the agonist binding site for glutamate. This receptor is the predominant excitatory neurotransmitter receptor in the mammalian brain. [provided by RefSeq, Jul 2008].

Supplier: US Biological

Anti-CORO1A Mouse Monoclonal Antibody [clone: 4G10]

Supplier: ProSci Inc.

ASPH is thought to play an important role in calcium homeostasis. Alternative splicing of this gene results in five transcript variants which vary in protein translation, the coding of catalytic domains, and tissue expression. Variation among these transcripts impacts their functions which involve roles in the calcium storage and release process in the endoplasmic and sarcoplasmic reticulum as well as hydroxylation of aspartic acid and asparagine in epidermal growth factor-like domains of various proteins.

Supplier: ProSci Inc.

SPPL2B is a member of the GXGD family of aspartic proteases. The GXGD proteases are transmembrane proteins with two conserved catalytic motifs localized within the membrane-spanning regions. This enzyme localizes to endosomes, lysosomes, and the plasma membrane. It cleaves the transmembrane domain of tumor necrosis factor alpha to release the intracellular domain, which triggers cytokine expression in the innate and adaptive immunity pathways.

Supplier: Thermo Fisher Scientific

Anidulafungin 97%

Supplier: Bioss

N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate receptors. NMDA receptor channel has been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of three different subunits: NR1 (GRIN1), NR2 (GRIN2A, GRIN2B, GRIN2C, or GRIN2D) and NR3 (GRIN3A or GRIN3B). The NR2 subunit acts as the agonist binding site for glutamate. This receptor is the predominant excitatory neurotransmitter receptor in the mammalian brain. [provided by RefSeq, Jul 2008].

Supplier: Bioss

G-protein coupled receptor. Has been shown to bind the neuroprotective and glioprotective factor prosaposin (PSAP), leading to endocytosis followed by an ERK phosphorylation cascade. However, other studies have shown that prosaposin does not increase activity. It has been suggested that GPR37L1 is a constitutively active receptor which signals through the guanine nucleotide-binding protein G(s) subunit alpha. Participates in the regulation of postnatal cerebellar development by modulating the Shh pathway. Regulates baseline blood pressure in females and protects against cardiovascular stress in males. Mediates inhibition of astrocyte glutamate transporters and reduction in neuronal N-methyl-D-aspartate receptor activity.

Supplier: Bioss

G-protein coupled receptor. Has been shown to bind the neuroprotective and glioprotective factor prosaposin (PSAP), leading to endocytosis followed by an ERK phosphorylation cascade. However, other studies have shown that prosaposin does not increase activity. It has been suggested that GPR37L1 is a constitutively active receptor which signals through the guanine nucleotide-binding protein G(s) subunit alpha. Participates in the regulation of postnatal cerebellar development by modulating the Shh pathway. Regulates baseline blood pressure in females and protects against cardiovascular stress in males. Mediates inhibition of astrocyte glutamate transporters and reduction in neuronal N-methyl-D-aspartate receptor activity.

Supplier: US Biological

Anti-BACE1 Mouse Monoclonal Antibody [clone: 2C13]

Supplier: Bioss

Aspartyl/asparaginyl beta-hydroxylase (ASPH) is a widely-expressed type II membrane protein involved in calcium homeostasis. Located in the endoplasmic reticulum, ASPH specifically hydroxylates an Asp or Asn residue in the epidermal growth factor-like (EGF) domains of several proteins, using iron as a cofactor. The ASPH gene encodes 3 proteins, ASPH, Junctin, and Junctate (or Humbug), that differ significantly in their C-terminal domains. These ASPH gene products are expressed as five transcript variants that differ by their roles in calcium storage and release, hydroxylation capabilities, and tissue specificity. While all ASPH variants are expressed in skeletal muscle, only some are detected in heart, brain, pancreas, placenta, lung, liver, and kidney tissues. In the lumen of the endoplasmic reticulum, ASPH can be processed into two different forms.