487 Results for: "D(-)-Aspartic acid"

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: VWR Chemicals

Animal-free amino acid. Polar. Amide.

Supplier: Thermo Fisher Scientific

Fmoc-Asp(Ompe)-OH 98% (by HPLC)

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Thermo Fisher Scientific

CAS No.: 3130-87-8

Supplier: Thermo Fisher Scientific

DL-Asparagine monohydrate 98%

Supplier: G-Biosciences

TCM-ProteaseArrest™ is a mixture of protease inhibitors with a broad specificity for the inhibition of serine, cysteine, aspartic (acid) proteases and aminopeptidases.

Supplier: Bioss

The amino acid Citrulline is required to detoxify the liver from ammonia, which is a waste product of the body from oxidation. Citrulline promotes energy and assists with the immune system. This unusual amino acid is formed in the urea cycle by the addition of carbon dioxide and ammonia to ornithine. It is then combined with aspartic acid to form arginosuccinic acid, which later is metabolized into the amino acid arginine.

Supplier: Thermo Fisher Scientific

Z-Asp(OMe)-OH 98%

Supplier: USP

USP Reference Standards are specified for use in conducting official USP–NF tests and assays. USP also provides Reference Standards specified in the Food Chemicals Codex as well as authentic substances—high-quality chemical samples—as a service to analytical, clinical, pharmaceutical and research laboratories. To confirm accuracy and reproducibility, USP Reference Standards are rigorously tested and evaluated by multiple independent laboratories including USP, commercial, regulatory, and academic labs. USP also provide publicly available, official documentary standards for pharmaceutical ingredients in the USP–NF that link directly with our primary reference standards.

Supplier: Bioss

WDR79 contains six WD (tryptophan-aspartate) repeat domains found in a number of proteins that function as adaptor molecules in signal transduction and cytoskeletal organization. The WD repeat is defined by four or more repeating units of a conserved core of approximately 40 amino acids ending with tryptophan-aspartic acid (WD). WD repeats may serve as sites of protein-protein interaction for adaptor proteins and facilitate multiprotein complex formation. The function of the WDR79 protein has not been characterized, however significant and consistent single nucleotide polymorphisms in the WDR79 gene have been found to be associated with ER negative breast cancer.

Supplier: Bioss

WDR79 contains six WD (tryptophan-aspartate) repeat domains found in a number of proteins that function as adaptor molecules in signal transduction and cytoskeletal organization. The WD repeat is defined by four or more repeating units of a conserved core of approximately 40 amino acids ending with tryptophan-aspartic acid (WD). WD repeats may serve as sites of protein-protein interaction for adaptor proteins and facilitate multiprotein complex formation. The function of the WDR79 protein has not been characterized, however significant and consistent single nucleotide polymorphisms in the WDR79 gene have been found to be associated with ER negative breast cancer.

Supplier: Bioss

WDR79 contains six WD (tryptophan-aspartate) repeat domains found in a number of proteins that function as adaptor molecules in signal transduction and cytoskeletal organization. The WD repeat is defined by four or more repeating units of a conserved core of approximately 40 amino acids ending with tryptophan-aspartic acid (WD). WD repeats may serve as sites of protein-protein interaction for adaptor proteins and facilitate multiprotein complex formation. The function of the WDR79 protein has not been characterized, however significant and consistent single nucleotide polymorphisms in the WDR79 gene have been found to be associated with ER negative breast cancer.

Supplier: Rockland Immunochemicals

Protease S.aureus V8 (endoproteinase-glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids. In the presence of ammonium, the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27000 daltons and optimum pH's of 4,0 and 7,8 with hemoglobin as the substrate. Enzyme activity is determined by the casein digestion assay.

Supplier: Bioss

The amino acid Citrulline is required to detoxify the liver from ammonia, which is a waste product of the body from oxidation. Citrulline promotes energy and assists with the immune system. This unusual amino acid is formed in the urea cycle by the addition of carbon dioxide and ammonia to ornithine. It is then combined with aspartic acid to form arginosuccinic acid, which later is metabolized into the amino acid arginine.

Supplier: Bioss

WDR79 contains six WD (tryptophan-aspartate) repeat domains found in a number of proteins that function as adaptor molecules in signal transduction and cytoskeletal organization. The WD repeat is defined by four or more repeating units of a conserved core of approximately 40 amino acids ending with tryptophan-aspartic acid (WD). WD repeats may serve as sites of protein-protein interaction for adaptor proteins and facilitate multiprotein complex formation. The function of the WDR79 protein has not been characterized, however significant and consistent single nucleotide polymorphisms in the WDR79 gene have been found to be associated with ER negative breast cancer.

Supplier: Bioss

SLC25A11 catalyzes the transport of 2-oxoglutarate across the inner mitochondrial membrane in an electroneutral exchange for malate or other dicarboxylic acids, and plays an important role in several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism.

Supplier: Bioss

The function of RED is currently unknown. The protein encoded by the RED gene was identified by its RED repeat, a stretch of repeated arginine, glutamic acid and aspartic acid residues. The protein localizes to discrete dots within the nucleus, excluding the nucleolus. This gene maps to chromosome 5; however, a pseudogene may exist on chromosome 2.

Supplier: Bioss

The amino acid Citrulline is required to detoxify the liver from ammonia, which is a waste product of the body from oxidation. Citrulline promotes energy and assists with the immune system. This unusual amino acid is formed in the urea cycle by the addition of carbon dioxide and ammonia to ornithine. It is then combined with aspartic acid to form arginosuccinic acid, which later is metabolized into the amino acid arginine.

Supplier: Bioss

The amino acid Citrulline is required to detoxify the liver from ammonia, which is a waste product of the body from oxidation. Citrulline promotes energy and assists with the immune system. This unusual amino acid is formed in the urea cycle by the addition of carbon dioxide and ammonia to ornithine. It is then combined with aspartic acid to form arginosuccinic acid, which later is metabolized into the amino acid arginine.

Supplier: Bioss

The function of RED is currently unknown. The protein encoded by the RED gene was identified by its RED repeat, a stretch of repeated arginine, glutamic acid and aspartic acid residues. The protein localizes to discrete dots within the nucleus, excluding the nucleolus. This gene maps to chromosome 5; however, a pseudogene may exist on chromosome 2.

Supplier: Bioss

The amino acid Citrulline is required to detoxify the liver from ammonia, which is a waste product of the body from oxidation. Citrulline promotes energy and assists with the immune system. This unusual amino acid is formed in the urea cycle by the addition of carbon dioxide and ammonia to ornithine. It is then combined with aspartic acid to form arginosuccinic acid, which later is metabolized into the amino acid arginine.

Supplier: Bioss

Napsin A is an aspartic proteinase that belongs to the peptidase A1 family and plays a role in pneumocyte surfactant processing. It is a 420-amino acid polypeptide consisting of a 24-residue signal peptide, a 40-amino acid propart, the mature enzyme of 336 amino acids, and a C-terminal extension of 18 residues. The mature Napsin A protein contains 3 predicted disulfide bonds, 3 potential N-linked oligosaccharide attachment sites, an RGD motif, a recognition motif for integrin binding, in the C terminus, immediately before a 4-amino acid insert that is unique to aspartic proteinases. Highest levels of Napsin A have been detected in adult lung (type II pneumocytes), fetal lung, and kidney tissues. Napsin A is also expressed at lower levels in adult spleen and at very low levels in peripheral blood leukocytes. Human napsin A shares 72.6% sequence identity with the mouse homolog.