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Bioss
Numéro de catalogue:
(BOSSBS-11337R-HRP)
Fournisseur:
Bioss
Description:
C1q, a subcomponent of the classical complement pathway, is composed of nine subunits that mediate classical complement activation and thereby play an important role in the immune response. Six of these subunits are disulfide-linked dimers of chains A and B, while three of these subunits, designated C1q-A through C1q-C, are disulfide-linked dimers of chain C. The presence of receptors for C1q on effector cells modulates its activity, which may be antibody-dependent or independent. Macrophages are the primary source of C1q, while anti-inflammatory drugs as well as cytokines differentially regulate expression of the mRNA, as well as the protein. However, its ability to modulate the interaction of platelets with collagen and immune complexes suggests C1q influences homeostasis as well as other immune activities, and perhaps thrombotic complications resulting from immune injury. Defects in C1q-A, C1q-B and C1q-C cause inactivation of the classical pathway, leading to a rare genetic disorder characterized by lupus-like symptoms.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11335R-HRP)
Fournisseur:
Bioss
Description:
BEGAIN is a 593 amino acid protein that localizes to cytoplasm and membrane. BEGAIN interacts with PSD-95 and SAPAP1 and forms a ternary complex and may sustain the structure of the postsynaptic density (PSD). BEGAIN is a novel PSD component associated with the core complex of PSD-95 and SAPAP. Because BEGAIN and SAPAP interact with the same region of PSD-95, BEGAIN and SAPAP may compete for the binding to PSD-95 and cannot interact with PSD-95 simultaneously. The C-terminal region of BEGAIN is involved in the interaction with PSD-95 whereas the N-terminal region has a coiled-coil structure that may interact with other molecules. BEGAIN is specifically expressed in brain and enriched in the PSD fraction. BEGAIN is also expressed in neurons and enriched at synaptic junctions, and is likely involved in the organization of synaptic junction components.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3832R-CY5)
Fournisseur:
Bioss
Description:
Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Activates the protein kinase activity of mTORC1. Has low intrinsic GTPase activity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3832R-CY3)
Fournisseur:
Bioss
Description:
Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Activates the protein kinase activity of mTORC1. Has low intrinsic GTPase activity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3832R-CY5.5)
Fournisseur:
Bioss
Description:
Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Activates the protein kinase activity of mTORC1. Has low intrinsic GTPase activity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3832R-FITC)
Fournisseur:
Bioss
Description:
Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Activates the protein kinase activity of mTORC1. Has low intrinsic GTPase activity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3834R-CY7)
Fournisseur:
Bioss
Description:
MRPL12 is a component of the 39S subunit of mammalian mitochondrial ribosomes. This protein forms homodimers whereas in prokaryotic ribosomes two L7/L12 dimers and one L10 protein form the L8 protein complex.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3832R-A647)
Fournisseur:
Bioss
Description:
Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Activates the protein kinase activity of mTORC1. Has low intrinsic GTPase activity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3834R-CY5.5)
Fournisseur:
Bioss
Description:
MRPL12 is a component of the 39S subunit of mammalian mitochondrial ribosomes. This protein forms homodimers whereas in prokaryotic ribosomes two L7/L12 dimers and one L10 protein form the L8 protein complex.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7725R-CY5.5)
Fournisseur:
Bioss
Description:
Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7725R-A647)
Fournisseur:
Bioss
Description:
Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7725R-A555)
Fournisseur:
Bioss
Description:
Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1655R-A750)
Fournisseur:
Bioss
Description:
The p21 activated kinases (PAK) are critical effectors that link Rho GTPases to cytoskeleton reorganization and nuclear signaling. The PAK proteins are a family of serine/threonine kinases that serve as targets for the small GTP binding proteins, CDC42 and RAC1, and have been implicated in a wide range of biological activities. The protein encoded by this gene is activated by proteolytic cleavage during caspase-mediated apoptosis, and may play a role in regulating the apoptotic events in the dying cell.P21-activated kinase (PAK) is actually a family of serine/threonine protein kinases, members of which are activated by small molecular weight GTPases. The three most common isoforms are PAK 1, PAK 2, and PAK 3 (also known as alpha PAK, gamma PAK, and beta PAK, respectively). These kinases contain numerous regulatory elements that trigger diverse signaling processes such as those initiated by activated GTPases, interaction with Src homology 3 (SH3) domains, and caspase mediated proteolytic cleavage. Autophosphorylation of serine 141 (serine 144 for PAK 1 and serine 139 PAK 3), catalysed by Cdc42, is required for activation of PAK.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11384R-A750)
Fournisseur:
Bioss
Description:
Displays cellular triglyceride lipase activity in liver, increases the levels of intracellular fatty acids derived from the hydrolysis of newly formed triglyceride stores and plays a role in very low-density lipoprotein assembly. Displays serine esterase activity in liver. Deacetylates a variety of arylacetamide substrates, including xenobiotic compounds and procarcinogens, converting them to the primary arylamide compounds and increasing their toxicity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3956R-A750)
Fournisseur:
Bioss
Description:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7777R-A647)
Fournisseur:
Bioss
Description:
Involved in intracellular protein transport probably out of a prevacuolar endosomal compartment. May be involved in the release of components of the bilayered coat from the endosomal membrane. The association with ESCRT-III complex mediates the ATP-dependent disassembly of the ESCRT-III complex. In case of infection, the HIV-1 virus takes advantage of it for budding and exocytic cargos of viral proteins.
UOM:
1 * 100 µl
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est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
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