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3,5-Dibromo-p-cresol
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3,5-Dibromo-p-cresol
Catalog Number:
(10306-072)
Supplier:
Bioss
Description:
The calcium-activated chloride channel (CLCA) protein family, which includes the human homologs CLCA1 and CLCA2, display distinct tissue distribution patterns. CLCA1 is expressed as a precursor protein that is processed into two cell surface associated subunits and a group of proteins. CLCA1 is upregulated by interleukin-9 and regulates the expression of mucins. CLCA1 may provide a therapeutic target to control mucus overproduction in airway disease patients with cystic fibrosis. CLCA2 expression is downregulated in breast cancer, therefore CLCA2 is thought to act as a tumor suppressor in normal cells. CLCA3 (known as Clca3 in mouse) is a structurally divergent member of the CLCA family that does not function as a channel protein. CLCA4 is a CLCA member that is expressed in human rectal mucosa, CLCA5 shows strong expression in eye and spleen, and CLCA6 is primarily expressed in intestine and stomach.
Catalog Number:
(10270-170)
Supplier:
Bioss
Description:
GAD-65 and GAD-67, glutamate decarboxylases, function to catalyze the production of GABA (gamma-aminobutyric acid). In the central nervous system, GABA functions as the main inhibitory transmitter by increasing a Cl- (chloride) conductance that inhibits neuronal firing. GABA has been shown to activate both ionotropic (GABAA) and metabotropic (GABAB) receptors, as well as a third class of receptors called GABAC. The Gamma subunit of GABAA receptors are important for benzodiazepine binding and modulation of GABA-mediated Cl- current. GABAA R Gamma 1 (gamma-aminobutyric acid (GABA) A receptor, gamma 1), also known as GABRG1, is a 465 amino acid multi-pass membrane protein belonging to the ligand-gated ionic channel (TC 1.A.9) family. GABAA R gamma 1 participates in neurotransmission inhibition and has been linked to alcohol dependence.
Catalog Number:
(10286-350)
Supplier:
Bioss
Description:
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.
Catalog Number:
(10306-074)
Supplier:
Bioss
Description:
The calcium-activated chloride channel (CLCA) protein family, which includes the human homologs CLCA1 and CLCA2, display distinct tissue distribution patterns. CLCA1 is expressed as a precursor protein that is processed into two cell surface associated subunits and a group of proteins. CLCA1 is upregulated by interleukin-9 and regulates the expression of mucins. CLCA1 may provide a therapeutic target to control mucus overproduction in airway disease patients with cystic fibrosis. CLCA2 expression is downregulated in breast cancer, therefore CLCA2 is thought to act as a tumor suppressor in normal cells. CLCA3 (known as Clca3 in mouse) is a structurally divergent member of the CLCA family that does not function as a channel protein. CLCA4 is a CLCA member that is expressed in human rectal mucosa, CLCA5 shows strong expression in eye and spleen, and CLCA6 is primarily expressed in intestine and stomach.
Catalog Number:
(10286-538)
Supplier:
Bioss
Description:
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.
Catalog Number:
(10286-352)
Supplier:
Bioss
Description:
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.
Catalog Number:
(10286-348)
Supplier:
Bioss
Description:
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.
Catalog Number:
(10075-540)
Supplier:
Prosci
Description:
Gamma-amGlycine is an important inhibitory transmitter in the brainstem and spinal cord. Glycine receptors are members of the ligand-gated ion channel family (LGICs) that mediate rapid chemical neurotransmission. The binding of glycine to its receptor produces a large increase in chloride conductance, which causes membrane hyperpolarization. Glycine receptors are anchored at inhibitory chemical synapses by a cytoplasmic protein, gephyrin. Gene targeting in mice showed that gephyrin is required for synaptic clustering of glycine receptors in spinal cord. The glycine receptor has been used to great advantage in the identification of the binding sites for alcohol on the LGIC family of proteins. These receptors have also been extremely useful in studies of synaptic clustering of receptors. During postnatal motoneuron development, the glycine receptor alpha subunit changes from alpha2 (fetal) to alpha1 (adult).
Catalog Number:
(10306-076)
Supplier:
Bioss
Description:
The calcium-activated chloride channel (CLCA) protein family, which includes the human homologs CLCA1 and CLCA2, display distinct tissue distribution patterns. CLCA1 is expressed as a precursor protein that is processed into two cell surface associated subunits and a group of proteins. CLCA1 is upregulated by interleukin-9 and regulates the expression of mucins. CLCA1 may provide a therapeutic target to control mucus overproduction in airway disease patients with cystic fibrosis. CLCA2 expression is downregulated in breast cancer, therefore CLCA2 is thought to act as a tumor suppressor in normal cells. CLCA3 (known as Clca3 in mouse) is a structurally divergent member of the CLCA family that does not function as a channel protein. CLCA4 is a CLCA member that is expressed in human rectal mucosa, CLCA5 shows strong expression in eye and spleen, and CLCA6 is primarily expressed in intestine and stomach.
Catalog Number:
(10306-078)
Supplier:
Bioss
Description:
The calcium-activated chloride channel (CLCA) protein family, which includes the human homologs CLCA1 and CLCA2, display distinct tissue distribution patterns. CLCA1 is expressed as a precursor protein that is processed into two cell surface associated subunits and a group of proteins. CLCA1 is upregulated by interleukin-9 and regulates the expression of mucins. CLCA1 may provide a therapeutic target to control mucus overproduction in airway disease patients with cystic fibrosis. CLCA2 expression is downregulated in breast cancer, therefore CLCA2 is thought to act as a tumor suppressor in normal cells. CLCA3 (known as Clca3 in mouse) is a structurally divergent member of the CLCA family that does not function as a channel protein. CLCA4 is a CLCA member that is expressed in human rectal mucosa, CLCA5 shows strong expression in eye and spleen, and CLCA6 is primarily expressed in intestine and stomach.
Catalog Number:
(10286-524)
Supplier:
Bioss
Description:
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.
Catalog Number:
(10286-536)
Supplier:
Bioss
Description:
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:
Adipogen
Description:
Verapamil hydrochloride is an alpha-adrenergic receptor (alpha-AR) antagonist and calcium channel protein inhibitor that blocks the L-type Ca2+ channels in smooth and cardiac muscle cells. Verapamil is an antiarrhythmic agent and vasodilator known to reduce the renal clearance of digoxin and induce apoptosis in primary and metastatic colon adenocarcinoma human cell lines in vitro. It has been observed that verapamil can induce currents by itself, presumably by acting on the potassium and chloride leakage. Verapamil has also been used as an inhibitor of drug efflux pump proteins such as Mdr (P-glycoprotein). Verapamil is a substrate of CYP3A4 and CYP2C6. It is also used in fluorescent cell sorting for DNA content, as it blocks efflux of a variety of DNA-binding fluorophores such as Hoechst 33342. Recent research has shown verapamil to be an effective treatment for diabetes in animal models. Verapamil helps treat diabetes by limiting TXNIP expression.
Supplier:
WORLD PRECISION INSTRUMENTS LLC
Description:
WPI™s microelectrode holder-half-cells couple fluid-filled glass micropipettes to high input impedance amplifiers. A Ag/AgCl pellet (or a silver wire) molded into the holder body provides stable potential. Electrical connection is made via male 2 mm pins or female 2 mm sockets. The pipette may be mounted axially or at right angles to the holder. Pipettes are held with screw-caps or rubber gaskets (without caps). Filling WPI microelectrode holders with electrolytes containing chloride results in stable electrode potential. Suitable electrolytes include KCl, NaCl and CaCl₂. Holders are supplied for standard WPI single capillary tubing of 1.0, 1.2, 1.5 and 2.0 mm ext.Ø. (Call WPI regarding custom designs for other glass diameter.) The holder style you select will depend on your experimental application, space, and instrumentation.
Supplier:
WORLD PRECISION INSTRUMENTS LLC
Description:
Microelectrode holder-half-cells couple fluid-filled glass micropipettes to high input impedance amplifiers. A Ag/AgCl pellet (or a silver wire) molded into the holder body provides stable potential. Electrical connection is made via male 2 mm pins or female 2 mm sockets. The pipette may be mounted axially or at right angles to the holder. Pipettes are held with screw-caps or rubber gaskets (without caps). Filling WPI microelectrode holders with electrolytes containing chloride results in stable electrode potential. Suitable electrolytes include KCl, NaCl and CaCl₂. Holders are supplied for standard WPI single capillary tubing of 1.0, 1.2, 1.5 and 2.0 mm outside diameters. (Call WPI regarding custom designs for other glass Ø.) The holder style you select will depend on your experimental application, space, and instrumentation.
Supplier:
WORLD PRECISION INSTRUMENTS LLC
Description:
WPI™s microelectrode holder-half-cells couple fluid-filled glass micropipettes to high input impedance amplifiers. A Ag/AgCl pellet (or a silver wire) molded into the holder body provides stable potential. Electrical connection is made via male 2 mm pins or female 2 mm sockets. The pipette may be mounted axially or at right angles to the holder. Pipettes are held with screw-caps or rubber gaskets (without caps). Filling WPI microelectrode holders with electrolytes containing chloride results in stable electrode potential. Suitable electrolytes include KCl, NaCl and CaCl₂. Holders are supplied for standard WPI single capillary tubing of 1.0, 1.2, 1.5 and 2.0 mm outside Ø. (Call WPI regarding custom designs for other glass diameters.) The holder style you select will depend on your experimental application, space, and instrumentation.
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 is still displayed and you need assistance, please call us at 1-800-932-5000.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
is still displayed and you need assistance, please call us at 1-800-932-5000.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
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