47226 Results for: "genobe"

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

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: 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: ProSci Inc.

NFKB1 or NFKB2 is bound to REL, RELA, or RELB to form the NFKB complex. The NFKB complex is inhibited by I-kappa-B proteins (NFKBIA or NFKBIB), which inactivate NF-kappa-B by trapping it in the cytoplasm. Phosphorylation of serine residues on the I-kappa-B proteins by kinases (IKBKA, or IKBKB) marks them for destruction via the ubiquitination pathway, thereby allowing activation of the NF-kappa-B complex. Activated NFKB complex translocates into the nucleus and binds DNA at kappa-B-binding motifs such as 5-prime GGGRNNYYCC 3-prime or 5-prime HGGARNYYCC 3-prime (where H is A, C, or T; R is an A or G purine; and Y is a C or T pyrimidine).

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: 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: Corning

PS coated with porcine gelatin. Corning® BioCoat™ gelatin cellware provides an attachment and growth promoting substrate for the culture of a variety of cell types. Gelatin is commonly used in the culture of normal and transfected cell types, including vascular endothelial, muscle, embryonic stem (ES) and F9 teratocarcinoma cells.

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: ProSci Inc.

Ly6/PLAUR domain containing3 (LYPD-3) is a GPI-linked protein. The structure of LYPD-3 is similar to the urokinasetype plasminogen activator receptor (uPAR). LYPD-3 is a 6 -100 kDa molecule with variable cell type-specific N-O-linked glycosylation, mature human LYPD-3 contains two uPAR/Ly6 domains and a Ser/Thr/Pro-rich (STP) region includes a protease sensitive site . The interaction of LYPD-3 with Laminin 1 and 5 on neighboring cells promotes the adhesion, spreading, and migration of tumor cells. LYPD-3 additionally interacts with Galectin-3 and the anterior gradient proteins AG-2 and AG-3. LYPD-3 overexpression in non-small cell lung cancer is predictive of increased mortality.

Supplier: ProSci Inc.

CCL4, (C-C motif chemokine 4; macrophage inflammatory protein 1beta) is a chemokine secreted at sites of inflammation by activated leukocytes, lymphocytes, vascular endothelial cells and pulmonary smooth cells. CCL4 attracts a variety of immune cells to sites of microbial infection as well as to pathologic inflammation, such as allergic asthma and ischemic myocardium. Full-length and truncated CCL4 exert biological activity through the receptor CCR5. The truncated form of CCL4 interacts additionally with CCR1 and CCR2b. The ability of CCL4 to bind CCR5 inhibits the cellular entry of M-tropic HIV. Both CCL4 forms block HIV-1 infection of T cells by inducing the downregulation of CCR5.

Supplier: ProSci Inc.

TMX2 is a single-pass type I membrane protein and contains 1 thioredoxin domain. Thioredoxin plays an important role in various cellular processes through redox regulation. The molecular cloning and characterisation of one member of the thioredoxin superfamily, designated as TMX2.The TMX2 cDNA consists of 1644 nucleotides and contains an open reading frame encoding a protein of 372 amino acids with a predicted molecular mass of 42.5 kDa and an isoelectric point of 8.94. The TMX2 protein may possess an N-terminal signal peptide, a potential transmembrane domain, an Myb DNA-binding domain repeat signature, a thioredoxin consensus pattern, an endoplasmic reticulum (ER) membrane retention signal (KKXX-like motif), and a dileucine motif in the tail.

Supplier: ProSci Inc.

NDE1 is required for centrosome duplication and formation and function of the mitotic spindle. It is essential for the development of the cerebral cortex. NDE1 may regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post-mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex

Supplier: ProSci Inc.

Pigment epithelium-derived factor (PEDF) is a 47 kDa secreted glycoprotein that belongs to the non-inhibitory serpin family group. PEDF is widely expressed in adult and foetal tissues, including brain, spinal cord, plasma, bone, prostate, pancreas, heart and lung. PEDF acts as an angiogenesis inhibitor with neurotrophic, immunomodulation and antitumor properties. It functions as anti-angiogenic agent by counterbalancing the proangiogenic effect of VEGF. PEDF is one of the most abundant proteins released by adipocytes and induces insulin resistance in adipocytes and human skeletal muscle cells. Recently, it has been reported that PEDF is sufficient to maintain the self-renewal of pluripotent human embryonic stem cells.

Supplier: Polyplus-transfection

In vivo-jetRNA®+ is a ready-to-use, efficient and stable lipid-based transfection reagent optimised for in vivo mRNA delivery.

Supplier: ProSci Inc.

NFKB has been detected in numerous cell types that express cytokines, chemokines, growth factors, cell adhesion molecules, and some acute phase proteins in health and in various disease states. NFKB is activated by a wide variety of stimuli such as cytokines, oxidant-free radicals, inhaled particles, ultraviolet irradiation, and bacterial or viral products. Inappropriate activation of NF-kappa-B has been linked to inflammatory events associated with autoimmune arthritis, asthma, septic shock, lung fibrosis, glomerulonephritis, atherosclerosis, and AIDS. In contrast, complete and persistent inhibition of NF-kappa-B has been linked directly to apoptosis, inappropriate immune cell development, and delayed cell growth.

Supplier: ProSci Inc.

NFKB has been detected in numerous cell types that express cytokines, chemokines, growth factors, cell adhesion molecules, and some acute phase proteins in health and in various disease states. NFKB is activated by a wide variety of stimuli such as cytokines, oxidant-free radicals, inhaled particles, ultraviolet irradiation, and bacterial or viral products. Inappropriate activation of NF-kappa-B has been linked to inflammatory events associated with autoimmune arthritis, asthma, septic shock, lung fibrosis, glomerulonephritis, atherosclerosis, and AIDS. In contrast, complete and persistent inhibition of NF-kappa-B has been linked directly to apoptosis, inappropriate immune cell development, and delayed cell growth.

Supplier: Quantabio

FastMixes include buffers and stabilisers optimised for maximum PCR efficiency, reproducibility, and sensitivity with TaqMan® and TaqMan® MGB probe chemistries. A key component of PerfeCTa® qPCR FastMixes is AccuFast™ Taq DNA polymerase that enables instant activation and rapid polymerisation kinetics. Upon heat activation (20 seconds at 95 °C), the antibodies irreversibly denature releasing fully active, unmodified Taq DNA polymerase. This promotes specific and efficient primer extension with the convenience of room temperature reaction assembly. FastMixes deliver maximum PCR efficiency, sensitivity, specificity, and a robust fluorescent signal with either fast or conventional cycling conditions.

Supplier: ProSci Inc.

NFKB has been detected in numerous cell types that express cytokines, chemokines, growth factors, cell adhesion molecules, and some acute phase proteins in health and in various disease states. NFKB is activated by a wide variety of stimuli such as cytokines, oxidant-free radicals, inhaled particles, ultraviolet irradiation, and bacterial or viral products. Inappropriate activation of NF-κ-B has been linked to inflammatory events associated with autoimmune arthritis, asthma, septic shock, lung fibrosis, glomerulonephritis, atherosclerosis, and AIDS. In contrast, complete and persistent inhibition of NF-κ-B has been linked directly to apoptosis, inappropriate immune cell development, and delayed cell growth.