21004 Results for: "Copper+edetate+solution"

Supplier: MULTIROIR

Reinforced HDPE container, ideal for laboratory use. Undeformable, unbreakable, food-safe. Smooth, hygienic, easy-care surface. Perfect for medical, pharmaceutical or research environments. 100% recyclable, durable and safe.

Supplier: Bioss

Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids. May also be activated by insulin. Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (PubMed:10708449, PubMed:23492904). Acts as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses (PubMed:10051606, PubMed:10196349).

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Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids. May also be activated by insulin. Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (PubMed:10708449, PubMed:23492904). Acts as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses (PubMed:10051606, PubMed:10196349).

Supplier: Bioss

Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes (By similarity).

Supplier: VWR Collection

VWR® Universal low retention filter tips repel liquid by creating a hydrophobic surface on the inside of the tip increasing your accuracy and data quality.

Supplier: VWR Collection

VWR® Universal low retention pipette tips repel liquid by creating a hydrophobic surface on the inside of the tip increasing your accuracy and data quality.

Supplier: ProSci Inc.

SLC25A16 is a protein that contains three tandemly repeated mitochondrial carrier protein domains. The protein is localized in the inner membrane and facilitates the rapid transport and exchange of molecules between the cytosol and the mitochondrial matrix space. SLC25A16 gene has a possible role in Graves' disease.This gene encodes a protein that contains three tandemly repeated mitochondrial carrier protein domains. The encoded protein is localized in the inner membrane and facilitates the rapid transport and exchange of molecules between the cytosol and the mitochondrial matrix space. This gene has a possible role in Graves' disease.

Supplier: ProSci Inc.

SLC27A6 is a member of the fatty acid transport protein family (FATP). FATPs are involved in the uptake of long-chain fatty acids and have unique expression patterns. Alternatively spliced transcript variants encoding the same protein have been found for this gene.This gene encodes a member of the fatty acid transport protein family (FATP). FATPs are involved in the uptake of long-chain fatty acids and have unique expression patterns. Alternatively spliced transcript variants encoding the same protein have been found for this gene.

Supplier: ProSci Inc.

The absorption of vitamin C into the body and its distribution to organs requires two sodium-dependent vitamin C transporters. This gene encodes one of the two required transporters and the encoded protein accounts for tissue-specific uptake of vitamin C. Previously, this gene had an official symbol of SLC23A1.The absorption of vitamin C into the body and its distribution to organs requires two sodium-dependent vitamin C transporters. This gene encodes one of the two required transporters and the encoded protein accounts for tissue-specific uptake of vitamin C. Previously, this gene had an official symbol of SLC23A1.

Supplier: ProSci Inc.

SLC22A14 is a member of the organic-cation transporter family. SLC22A14 is a transmembrane protein which is thought to transport small molecules and since this protein is conserved among several species, it is suggested to have a fundamental role in mammalian systems.This gene encodes a member of the organic-cation transporter family. It is located in a gene cluster with another member of the family, organic cation transporter like 3. The encoded protein is a transmembrane protein which is thought to transport small molecules and since this protein is conserved among several species, it is suggested to have a fundamental role in mammalian systems.

Supplier: Brady

Securely label tubes and vials for cryogenic storage with this self-laminating, ultra-thin polyester label material (B-461). Print almost anywhere with a compact Brady portable label printer.

Supplier: Bioss

Calcium signaling in mitochondria is important in order for it to function in response to a variety of extracellular stimuli. Signaling begins with Ca(2+) entry in mitochondria via the Ca(2+) uniporter followed by Ca(2+) activation of three dehydrogenases in the mitochondrial matrix. ARALAR, the neuronal Ca(2+)-binding mitochondrial aspartate-glutamate carrier, has Ca(2+) binding domains facing the extramitochondrial space and functions in the malate-aspartate NADH shuttle (MAS). ARALAR is encoded by the SLC25A12 gene and is expressed in brain and skeletal muscle. ARALAR is required for the synthesis of brain aspartate and N-acetylaspartatemay and plays a role in myelin formation. It is also essential for the transmission of small Ca(2+) signals to mitochondria via an increase in mitochondrial NADH. In addition, ARALAR is implicated in conferring susceptibility to schizophrenia.

Supplier: Bioss

Calcium signaling in mitochondria is important in order for it to function in response to a variety of extracellular stimuli. Signaling begins with Ca(2+) entry in mitochondria via the Ca(2+) uniporter followed by Ca(2+) activation of three dehydrogenases in the mitochondrial matrix. ARALAR, the neuronal Ca(2+)-binding mitochondrial aspartate-glutamate carrier, has Ca(2+) binding domains facing the extramitochondrial space and functions in the malate-aspartate NADH shuttle (MAS). ARALAR is encoded by the SLC25A12 gene and is expressed in brain and skeletal muscle. ARALAR is required for the synthesis of brain aspartate and N-acetylaspartatemay and plays a role in myelin formation. It is also essential for the transmission of small Ca(2+) signals to mitochondria via an increase in mitochondrial NADH. In addition, ARALAR is implicated in conferring susceptibility to schizophrenia.

Supplier: Bioss

Calcium signaling in mitochondria is important in order for it to function in response to a variety of extracellular stimuli. Signaling begins with Ca(2+) entry in mitochondria via the Ca(2+) uniporter followed by Ca(2+) activation of three dehydrogenases in the mitochondrial matrix. ARALAR, the neuronal Ca(2+)-binding mitochondrial aspartate-glutamate carrier, has Ca(2+) binding domains facing the extramitochondrial space and functions in the malate-aspartate NADH shuttle (MAS). ARALAR is encoded by the SLC25A12 gene and is expressed in brain and skeletal muscle. ARALAR is required for the synthesis of brain aspartate and N-acetylaspartatemay and plays a role in myelin formation. It is also essential for the transmission of small Ca(2+) signals to mitochondria via an increase in mitochondrial NADH. In addition, ARALAR is implicated in conferring susceptibility to schizophrenia.

Supplier: EBRO

The SL1011 set by ebro, featuring the EBI 12-T101 data logger, PHX800 pH tester, and TDS3 conductivity meter, is designed for validating and monitoring bedpan washers in healthcare settings, ensuring hygiene standards.

Supplier: Bioss

Calcium signaling in mitochondria is important in order for it to function in response to a variety of extracellular stimuli. Signaling begins with Ca(2+) entry in mitochondria via the Ca(2+) uniporter followed by Ca(2+) activation of three dehydrogenases in the mitochondrial matrix. ARALAR, the neuronal Ca(2+)-binding mitochondrial aspartate-glutamate carrier, has Ca(2+) binding domains facing the extramitochondrial space and functions in the malate-aspartate NADH shuttle (MAS). ARALAR is encoded by the SLC25A12 gene and is expressed in brain and skeletal muscle. ARALAR is required for the synthesis of brain aspartate and N-acetylaspartatemay and plays a role in myelin formation. It is also essential for the transmission of small Ca(2+) signals to mitochondria via an increase in mitochondrial NADH. In addition, ARALAR is implicated in conferring susceptibility to schizophrenia.

Supplier: Bioss

The sodium-coupled neutral amino acid transporters (SNAT) of the SLC38 gene family include System A subtypes SNAT1, SNAT2 and SNAT4 and System N subtypes SNAT3 and SNAT5. The SLC38 transporters are essential for the uptake of nutrients, energy production, metabolism, detoxification, and the cycling of neurotransmitters. SNAT2, also designated ATA2, PRO1068 and SAT2 is encoded by the human gene SLC38A2. The functional role of SNAT2 in the nervous system is unclear. Protein expression is notably enriched in the spinal cord and brain stem nuclei of the auditory system. System A transport proteins are also present in placental tissue. These SNAT proteins may play a significant role in fetal development and inhibition of the transport system has been associated with fetal growth retardation.

Supplier: Bioss

NHE-3 are integral membrane proteins that are expressed in most mammalian tissues, where they regulate intracellular pH and cell volume. NHEs mediate the transport of hydrogen (H+) ions out of cells in exchange for extracellular sodium (Na+) ions. While NHE-1 is ubiquitously expressed, the NHE isoforms 2-8 have distinct tissue- and cell type-dependent expression and inhibitory characteristics. NHE-3 localizes to the apical membrane of renal proximal tubules where it is responsible for most of the sodium transport and fluid reabsorption. NHE-3 translocates to internal pools where it mediates natriuresis when blood pressure increases abruptly. NHE-3 is also expressed in the stomach and functions to protect the mucosa by secreting protons that diffuse into the mucous cells.

Supplier: Bioss

NHE-3 are integral membrane proteins that are expressed in most mammalian tissues, where they regulate intracellular pH and cell volume. NHEs mediate the transport of hydrogen (H+) ions out of cells in exchange for extracellular sodium (Na+) ions. While NHE-1 is ubiquitously expressed, the NHE isoforms 2-8 have distinct tissue- and cell type-dependent expression and inhibitory characteristics. NHE-3 localizes to the apical membrane of renal proximal tubules where it is responsible for most of the sodium transport and fluid reabsorption. NHE-3 translocates to internal pools where it mediates natriuresis when blood pressure increases abruptly. NHE-3 is also expressed in the stomach and functions to protect the mucosa by secreting protons that diffuse into the mucous cells.

Supplier: ProSci Inc.

SLC22A8 is involved in the sodium-independent transport and excretion of organic anions, some of which are potentially toxic. SLC22A8 is an integral membrane protein and appears to be localized to the basolateral membrane of the kidney.The protein encoded by this gene is involved in the sodium-independent transport and excretion of organic anions, some of which are potentially toxic. The encoded protein is an integral membrane protein and appears to be localized to the basolateral membrane of the kidney. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: ProSci Inc.

Sodium hydrogen antiporters, such as NHEDC2, convert the proton motive force established by the respiratory chain or the F1F0 mitochondrial ATPase into sodium gradients that drive other energy-requiring processes, transduce environmental signals into cell responses, or function in drug efflux.Sodium hydrogen antiporters, such as NHEDC2, convert the proton motive force established by the respiratory chain or the F1F0 mitochondrial ATPase into sodium gradients that drive other energy-requiring processes, transduce environmental signals into cell responses, or function in drug efflux (Xiang et al., 2007 [PubMed 18000046]).

Supplier: Thermo Fisher Scientific

Pierce™ Iodination Tubes are 12×75 mm glass test tubes that are pre-coated at the bottom with Pierce™ Iodination Reagent, which activates iodine-125 for protein or peptide iodination procedures.

Supplier: Bioss

NHE-3 are integral membrane proteins that are expressed in most mammalian tissues, where they regulate intracellular pH and cell volume. NHEs mediate the transport of hydrogen (H+) ions out of cells in exchange for extracellular sodium (Na+) ions. While NHE-1 is ubiquitously expressed, the NHE isoforms 2-8 have distinct tissue- and cell type-dependent expression and inhibitory characteristics. NHE-3 localizes to the apical membrane of renal proximal tubules where it is responsible for most of the sodium transport and fluid reabsorption. NHE-3 translocates to internal pools where it mediates natriuresis when blood pressure increases abruptly. NHE-3 is also expressed in the stomach and functions to protect the mucosa by secreting protons that diffuse into the mucous cells.

Supplier: Bioss

Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes (By similarity).

Supplier: KIMBERLY CLARK

These soap dispensers have been designed to promote hygiene, improve comfort and care.

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Band 3, also designated AE1, is an erythrocyte membrane glycoprotein that contributes to cell stuctural integrity and mediates exchange of chloride and bicarbonate across the phospholipid bilayer. The diverse functions of the approximately 900 amino acid protein are mediated by two distinct domains. The amino terminal domain, also known as cdb3 for cytoplasmic domain of erthrocyte membrane band 3, acts as an attachment site for the erythrocyte skeleton by binding ankyrin. The carboxy-terminal, membrane-associated domain carries out exchange transport of anions. Degradation of band 3 can generate an aging antigen known as senescent cell antigen, or SCA, which is expressed on old cells and marks them for removal by the immune system. An isoform of band 3, which lacks the first 65 amino acids and does not bind ankryin, is expressed in kidney.

Supplier: Bioss

Band 3, also designated AE1, is an erythrocyte membrane glycoprotein that contributes to cell stuctural integrity and mediates exchange of chloride and bicarbonate across the phospholipid bilayer. The diverse functions of the approximately 900 amino acid protein are mediated by two distinct domains. The amino terminal domain, also known as cdb3 for cytoplasmic domain of erthrocyte membrane band 3, acts as an attachment site for the erythrocyte skeleton by binding ankyrin. The carboxy-terminal, membrane-associated domain carries out exchange transport of anions. Degradation of band 3 can generate an aging antigen known as senescent cell antigen, or SCA, which is expressed on old cells and marks them for removal by the immune system. An isoform of band 3, which lacks the first 65 amino acids and does not bind ankryin, is expressed in kidney.

Supplier: Bioss

The sodium-coupled neutral amino acid transporters (SNAT) of the SLC38 gene family include System A subtypes SNAT1, SNAT2 and SNAT4 and System N subtypes SNAT3 and SNAT5. The SLC38 transporters are essential for the uptake of nutrients, energy production, metabolism, detoxification, and the cycling of neurotransmitters. SNAT2, also designated ATA2, PRO1068 and SAT2 is encoded by the human gene SLC38A2. The functional role of SNAT2 in the nervous system is unclear. Protein expression is notably enriched in the spinal cord and brain stem nuclei of the auditory system. System A transport proteins are also present in placental tissue. These SNAT proteins may play a significant role in fetal development and inhibition of the transport system has been associated with fetal growth retardation.

Supplier: Bioss

Calcium signaling in mitochondria is important in order for it to function in response to a variety of extracellular stimuli. Signaling begins with Ca(2+) entry in mitochondria via the Ca(2+) uniporter followed by Ca(2+) activation of three dehydrogenases in the mitochondrial matrix. ARALAR, the neuronal Ca(2+)-binding mitochondrial aspartate-glutamate carrier, has Ca(2+) binding domains facing the extramitochondrial space and functions in the malate-aspartate NADH shuttle (MAS). ARALAR is encoded by the SLC25A12 gene and is expressed in brain and skeletal muscle. ARALAR is required for the synthesis of brain aspartate and N-acetylaspartatemay and plays a role in myelin formation. It is also essential for the transmission of small Ca(2+) signals to mitochondria via an increase in mitochondrial NADH. In addition, ARALAR is implicated in conferring susceptibility to schizophrenia.

Supplier: Bioss

NHE-3 are integral membrane proteins that are expressed in most mammalian tissues, where they regulate intracellular pH and cell volume. NHEs mediate the transport of hydrogen (H+) ions out of cells in exchange for extracellular sodium (Na+) ions. While NHE-1 is ubiquitously expressed, the NHE isoforms 2-8 have distinct tissue- and cell type-dependent expression and inhibitory characteristics. NHE-3 localizes to the apical membrane of renal proximal tubules where it is responsible for most of the sodium transport and fluid reabsorption. NHE-3 translocates to internal pools where it mediates natriuresis when blood pressure increases abruptly. NHE-3 is also expressed in the stomach and functions to protect the mucosa by secreting protons that diffuse into the mucous cells.