47183 Results for: "genobe"

Supplier: ProSci Inc.

Cell Growth Regulator with EF Hand Domain Protein 1 (CGREF1) is a secreted calcium ion binding protein. CGREF1 contains two EF-hand domains and both EF-hands are required for function. Human CGREF1 is synthesized as a 301 amino acid precursor that contains a 19 amino acid signal sequence, and a 282 amino acid mature chain. CGREF1 is probably digested extracellularly by an unknown serine protease generating extremely hydrophobic bioactive peptides. CGREF1 mediates cell-cell adhesion in a calcium-dependent manner. In addition, CGREF1 is able to inhibit growth in several cell lines.

Supplier: ProSci Inc.

Pituitary growth hormone (GH) plays a crucial role in stimulating and controlling the growth, metabolism and differentiation of many mammalian cell types by modulating the synthesis of multiple mRNA species. These effects are mediated by the binding of GH to its membrane-bound receptor, GHR, and involve a phosphorylation cascade that results in the modulation of numerous signaling pathways. GH is synthesised by acidophilic or somatotropic cells of the anterior pituitary gland. Anti-GH is a useful marker in classification of pituitary tumors and the study of pituitary disease (acromegaly).

Supplier: Bioss

CBG is a monomeric enzyme involved in the absorption and metabolism of flavonoid glucosides. CBG is found predominately in the liver, but is also located in tissues such as spleen, small intestine and kidney. Through its catalytic activity, CBG is able to hydrolyze a variety of glycosides including phytoestrogens, cyanogens, and flavonols. Although its catalytic activity extends to many dietary flavonoids, CBG has increased specificity for hydrophobic aglycones such as beta-D-glucoside and beta-D-galactoside. Hydrolysis is inhibited by sodium taurocholate and glucosyl-sphingosine, both of which regulate CBG enzymatic activity. Deficiencies in CBG have been implicated in Gaucher’s disease, a lysosomal storage disease that causes a build up of fatty material in the spleen, liver, lung and kidneys.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: TriLink BioTechnologies

CleanScribe™ RNA Polymerase is a novel enzyme that reduces double-stranded RNA (dsRNA) formation in IVT RNA synthesis.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

CBG is a monomeric enzyme involved in the absorption and metabolism of flavonoid glucosides. CBG is found predominately in the liver, but is also located in tissues such as spleen, small intestine and kidney. Through its catalytic activity, CBG is able to hydrolyze a variety of glycosides including phytoestrogens, cyanogens, and flavonols. Although its catalytic activity extends to many dietary flavonoids, CBG has increased specificity for hydrophobic aglycones such as beta-D-glucoside and beta-D-galactoside. Hydrolysis is inhibited by sodium taurocholate and glucosyl-sphingosine, both of which regulate CBG enzymatic activity. Deficiencies in CBG have been implicated in Gaucher’s disease, a lysosomal storage disease that causes a build up of fatty material in the spleen, liver, lung and kidneys.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: HICHROM

CIMmultus™ columns are based on an innovative monolithic technology. Distinguished by large pores/flow through channels these columns are designed for the production, purification, and analytics of large proteins (IgG, IgM, PEGylated proteins), viruses (AAV, adenovirus, lentivirus, influenza, bacteriophages), VLPs, exosomes and pDNA for example.

Supplier: ProSci Inc.

Clusterin is a secreted protein which belongs to the Clusterin family. Clusterin is expressed in adult testis, heart, ovary, adrenal gland, brain and liver. Clusterin has been suggested to be involved in several basic biological events such as cell death, tumor progression, and neurodegenerative disorders. In addition,Clusterin is up/ down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

CBG is a monomeric enzyme involved in the absorption and metabolism of flavonoid glucosides. CBG is found predominately in the liver, but is also located in tissues such as spleen, small intestine and kidney. Through its catalytic activity, CBG is able to hydrolyze a variety of glycosides including phytoestrogens, cyanogens, and flavonols. Although its catalytic activity extends to many dietary flavonoids, CBG has increased specificity for hydrophobic aglycones such as beta-D-glucoside and beta-D-galactoside. Hydrolysis is inhibited by sodium taurocholate and glucosyl-sphingosine, both of which regulate CBG enzymatic activity. Deficiencies in CBG have been implicated in Gaucher’s disease, a lysosomal storage disease that causes a build up of fatty material in the spleen, liver, lung and kidneys.

Supplier: Bioss

CBG is a monomeric enzyme involved in the absorption and metabolism of flavonoid glucosides. CBG is found predominately in the liver, but is also located in tissues such as spleen, small intestine and kidney. Through its catalytic activity, CBG is able to hydrolyze a variety of glycosides including phytoestrogens, cyanogens, and flavonols. Although its catalytic activity extends to many dietary flavonoids, CBG has increased specificity for hydrophobic aglycones such as beta-D-glucoside and beta-D-galactoside. Hydrolysis is inhibited by sodium taurocholate and glucosyl-sphingosine, both of which regulate CBG enzymatic activity. Deficiencies in CBG have been implicated in Gaucher’s disease, a lysosomal storage disease that causes a build up of fatty material in the spleen, liver, lung and kidneys.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Quantabio

PerfeCTa® qPCR SuperMixes are 2X concentrated, ready to use reaction cocktails containing all components except primers, probe and template for qPCR.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

CBG is a monomeric enzyme involved in the absorption and metabolism of flavonoid glucosides. CBG is found predominately in the liver, but is also located in tissues such as spleen, small intestine and kidney. Through its catalytic activity, CBG is able to hydrolyze a variety of glycosides including phytoestrogens, cyanogens, and flavonols. Although its catalytic activity extends to many dietary flavonoids, CBG has increased specificity for hydrophobic aglycones such as beta-D-glucoside and beta-D-galactoside. Hydrolysis is inhibited by sodium taurocholate and glucosyl-sphingosine, both of which regulate CBG enzymatic activity. Deficiencies in CBG have been implicated in Gaucher’s disease, a lysosomal storage disease that causes a build up of fatty material in the spleen, liver, lung and kidneys.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

Supplier: Bioss

CBG is a monomeric enzyme involved in the absorption and metabolism of flavonoid glucosides. CBG is found predominately in the liver, but is also located in tissues such as spleen, small intestine and kidney. Through its catalytic activity, CBG is able to hydrolyze a variety of glycosides including phytoestrogens, cyanogens, and flavonols. Although its catalytic activity extends to many dietary flavonoids, CBG has increased specificity for hydrophobic aglycones such as beta-D-glucoside and beta-D-galactoside. Hydrolysis is inhibited by sodium taurocholate and glucosyl-sphingosine, both of which regulate CBG enzymatic activity. Deficiencies in CBG have been implicated in Gaucher’s disease, a lysosomal storage disease that causes a build up of fatty material in the spleen, liver, lung and kidneys.

Supplier: Bioss

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.