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Catalog Number: (BOSSBS-12497R-FITC)
Supplier: Bioss
Description: Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).
UOM: 1 * 100 µl


Supplier: Apollo Scientific
Description: trans-1,2-Diaminocyclohexane-N,N,N',N'-tetraacetic acid monohydrate

Catalog Number: (BOSSBS-12497R-A750)
Supplier: Bioss
Description: Apolipoproteins are protein components of plasma lipoproteins. The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins. The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages. The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyses triglycerides in plasma and transfers the fatty acids to tissues. The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase. The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12497R-A350)
Supplier: Bioss
Description: Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12496R-HRP)
Supplier: Bioss
Description: Apolipoproteins are protein components of plasma lipoproteins. The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins. The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages. The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues. The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase. The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12497R-A488)
Supplier: Bioss
Description: Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12497R-A555)
Supplier: Bioss
Description: Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11104R)
Supplier: Bioss
Description: Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11104R-HRP)
Supplier: Bioss
Description: Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11104R-CY7)
Supplier: Bioss
Description: Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11104R-A647)
Supplier: Bioss
Description: Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11036R)
Supplier: Bioss
Description: Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11104R-A350)
Supplier: Bioss
Description: Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11104R-A750)
Supplier: Bioss
Description: Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11104R-CY5)
Supplier: Bioss
Description: Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11104R-A488)
Supplier: Bioss
Description: Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.
UOM: 1 * 100 µl


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