47226 Results for: "gene"

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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.

Supplier: ProSci Inc.

The Galectin family of proteins, with specificity for Nacetyllactosamine containing glycoproteins, consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs).They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide; they can be secreted by one or more as yet unidentified non-classical secretory pathways. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications.

Supplier: ProSci Inc.

NFKB1 (MIM 164011) or NFKB2 (MIM 164012) is bound to REL (MIM 164910), RELA (MIM 164014), or RELB (MIM 604758) to form the NFKB complex. The NFKB complex is inhibited by I-kappa-B proteins (NFKBIA, MIM 164008, 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, MIM 600664 or IKBKB, MIM 603258) 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: ProSci Inc.

NFKB1 (MIM 164011) or NFKB2 (MIM 164012) is bound to REL (MIM 164910), RELA (MIM 164014), or RELB (MIM 604758) to form the NFKB complex. The NFKB complex is inhibited by I-kappa-B proteins (NFKBIA, MIM 164008, 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, MIM 600664 or IKBKB, MIM 603258) 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).

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Ferritin heavy polypeptide 1(FTH1), is a ubiquitous intracellular protein which stores iron in a soluble, non-toxic, readily available form. FTH1 has ferroxidase activity and is important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Ferritin is composed of 24 subunits of the light and heavy ferritin chains. It plays a role in delivery of iron to cells and mediates iron uptake in capsule cells of the developing kidney. Variation of ferritin subunit composition may affect iron absorption and release in different tissues. Deficiency of ferritin proteins may cause several neurodegenerative diseases. Almost all living organisms can produce this protein, including algae, bacteria, higher plants, and animals.

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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: Abcam

An Sandwich ELISA kit to quantify human TNFSF10 in human serum, plasma, culture supernatants.

Supplier: Bioss

The transcription factor NFkB is retained in the cytoplasm in an inactive form by the inhibitory protein IkB. Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in the targeted degradation of IkB (1). IkB kinase alpha (IKK alpha), previously designated CHUK (2), interacts with IkB-alpha and specifically phosphorylates IkB-alpha on the sites that trigger its degradation, serines 32 and 36 (3). IKKalpha appears to be critical for NFkB activation in response to proinflammatory cytokines (4). Phosphorylation of the IkB by IKK alpha is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation in response to TNF and IL-1 (5). The functional IKK complex contains three subunits, IKK alpha, IKK beta and IKK gamma (also designated NEMO), and each appears to make essential contributions to IkB phosphorylation (6). IKAP (IKK-complex-associated protein) is a protein that acts as a scaffold, interacting with NIK, IKK alpha and IKK beta and assembling them into an active kinase complex (7,8)

Supplier: Abcam

An Sandwich ELISA kit to quantify human ER-alpha in human serum, plasma and other biological fluids.

Supplier: Bioss

The transcription factor NFkB is retained in the cytoplasm in an inactive form by the inhibitory protein IkB. Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in the targeted degradation of IkB (1). IkB kinase alpha (IKK alpha), previously designated CHUK (2), interacts with IkB-alpha and specifically phosphorylates IkB-alpha on the sites that trigger its degradation, serines 32 and 36 (3). IKKalpha appears to be critical for NFkB activation in response to proinflammatory cytokines (4). Phosphorylation of the IkB by IKK alpha is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation in response to TNF and IL-1 (5). The functional IKK complex contains three subunits, IKK alpha, IKK beta and IKK gamma (also designated NEMO), and each appears to make essential contributions to IkB phosphorylation (6). IKAP (IKK-complex-associated protein) is a protein that acts as a scaffold, interacting with NIK, IKK alpha and IKK beta and assembling them into an active kinase complex (7,8)

Supplier: Bioss

The transcription factor NFkB is retained in the cytoplasm in an inactive form by the inhibitory protein IkB. Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in the targeted degradation of IkB (1). IkB kinase alpha (IKK alpha), previously designated CHUK (2), interacts with IkB-alpha and specifically phosphorylates IkB-alpha on the sites that trigger its degradation, serines 32 and 36 (3). IKKalpha appears to be critical for NFkB activation in response to proinflammatory cytokines (4). Phosphorylation of the IkB by IKK alpha is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation in response to TNF and IL-1 (5). The functional IKK complex contains three subunits, IKK alpha, IKK beta and IKK gamma (also designated NEMO), and each appears to make essential contributions to IkB phosphorylation (6). IKAP (IKK-complex-associated protein) is a protein that acts as a scaffold, interacting with NIK, IKK alpha and IKK beta and assembling them into an active kinase complex (7,8)

Supplier: Abcam

A sandwich ELISA kit for the quantitative measurement of collagen type I in biological fluids.

Supplier: Bioss

The transcription factor NFkB is retained in the cytoplasm in an inactive form by the inhibitory protein IkB. Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in the targeted degradation of IkB (1). IkB kinase alpha (IKK alpha), previously designated CHUK (2), interacts with IkB-alpha and specifically phosphorylates IkB-alpha on the sites that trigger its degradation, serines 32 and 36 (3). IKKalpha appears to be critical for NFkB activation in response to proinflammatory cytokines (4). Phosphorylation of the IkB by IKK alpha is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation in response to TNF and IL-1 (5). The functional IKK complex contains three subunits, IKK alpha, IKK beta and IKK gamma (also designated NEMO), and each appears to make essential contributions to IkB phosphorylation (6). IKAP (IKK-complex-associated protein) is a protein that acts as a scaffold, interacting with NIK, IKK alpha and IKK beta and assembling them into an active kinase complex (7,8)

Supplier: Bioss

The transcription factor NFkB is retained in the cytoplasm in an inactive form by the inhibitory protein IkB. Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in the targeted degradation of IkB (1). IkB kinase alpha (IKK alpha), previously designated CHUK (2), interacts with IkB-alpha and specifically phosphorylates IkB-alpha on the sites that trigger its degradation, serines 32 and 36 (3). IKKalpha appears to be critical for NFkB activation in response to proinflammatory cytokines (4). Phosphorylation of the IkB by IKK alpha is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation in response to TNF and IL-1 (5). The functional IKK complex contains three subunits, IKK alpha, IKK beta and IKK gamma (also designated NEMO), and each appears to make essential contributions to IkB phosphorylation (6). IKAP (IKK-complex-associated protein) is a protein that acts as a scaffold, interacting with NIK, IKK alpha and IKK beta and assembling them into an active kinase complex (7,8)

Supplier: Bioss

The transcription factor NFkB is retained in the cytoplasm in an inactive form by the inhibitory protein IkB. Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in the targeted degradation of IkB (1). IkB kinase alpha (IKK alpha), previously designated CHUK (2), interacts with IkB-alpha and specifically phosphorylates IkB-alpha on the sites that trigger its degradation, serines 32 and 36 (3). IKKalpha appears to be critical for NFkB activation in response to proinflammatory cytokines (4). Phosphorylation of the IkB by IKK alpha is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation in response to TNF and IL-1 (5). The functional IKK complex contains three subunits, IKK alpha, IKK beta and IKK gamma (also designated NEMO), and each appears to make essential contributions to IkB phosphorylation (6). IKAP (IKK-complex-associated protein) is a protein that acts as a scaffold, interacting with NIK, IKK alpha and IKK beta and assembling them into an active kinase complex (7,8)

Supplier: Bioss

The transcription factor NFkB is retained in the cytoplasm in an inactive form by the inhibitory protein IkB. Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in the targeted degradation of IkB (1). IkB kinase alpha (IKK alpha), previously designated CHUK (2), interacts with IkB-alpha and specifically phosphorylates IkB-alpha on the sites that trigger its degradation, serines 32 and 36 (3). IKKalpha appears to be critical for NFkB activation in response to proinflammatory cytokines (4). Phosphorylation of the IkB by IKK alpha is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation in response to TNF and IL-1 (5). The functional IKK complex contains three subunits, IKK alpha, IKK beta and IKK gamma (also designated NEMO), and each appears to make essential contributions to IkB phosphorylation (6). IKAP (IKK-complex-associated protein) is a protein that acts as a scaffold, interacting with NIK, IKK alpha and IKK beta and assembling them into an active kinase complex (7,8)

Supplier: Bioss

The transcription factor NFkB is retained in the cytoplasm in an inactive form by the inhibitory protein IkB. Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in the targeted degradation of IkB (1). IkB kinase alpha (IKK alpha), previously designated CHUK (2), interacts with IkB-alpha and specifically phosphorylates IkB-alpha on the sites that trigger its degradation, serines 32 and 36 (3). IKKalpha appears to be critical for NFkB activation in response to proinflammatory cytokines (4). Phosphorylation of the IkB by IKK alpha is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation in response to TNF and IL-1 (5). The functional IKK complex contains three subunits, IKK alpha, IKK beta and IKK gamma (also designated NEMO), and each appears to make essential contributions to IkB phosphorylation (6). IKAP (IKK-complex-associated protein) is a protein that acts as a scaffold, interacting with NIK, IKK alpha and IKK beta and assembling them into an active kinase complex (7,8)

Supplier: Brand

PP. These 0,2 and 0,5 ml PCR tubes with attached caps are compatible with leading thermal cyclers with heated lids.

Supplier: Bioss

The transcription factor NFkB is retained in the cytoplasm in an inactive form by the inhibitory protein IkB. Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in the targeted degradation of IkB (1). IkB kinase alpha (IKK alpha), previously designated CHUK (2), interacts with IkB-alpha and specifically phosphorylates IkB-alpha on the sites that trigger its degradation, serines 32 and 36 (3). IKKalpha appears to be critical for NFkB activation in response to proinflammatory cytokines (4). Phosphorylation of the IkB by IKK alpha is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation in response to TNF and IL-1 (5). The functional IKK complex contains three subunits, IKK alpha, IKK beta and IKK gamma (also designated NEMO), and each appears to make essential contributions to IkB phosphorylation (6). IKAP (IKK-complex-associated protein) is a protein that acts as a scaffold, interacting with NIK, IKK alpha and IKK beta and assembling them into an active kinase complex (7,8)

Supplier: Bioss

The transcription factor NFkB is retained in the cytoplasm in an inactive form by the inhibitory protein IkB. Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in the targeted degradation of IkB (1). IkB kinase alpha (IKK alpha), previously designated CHUK (2), interacts with IkB-alpha and specifically phosphorylates IkB-alpha on the sites that trigger its degradation, serines 32 and 36 (3). IKKalpha appears to be critical for NFkB activation in response to proinflammatory cytokines (4). Phosphorylation of the IkB by IKK alpha is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation in response to TNF and IL-1 (5). The functional IKK complex contains three subunits, IKK alpha, IKK beta and IKK gamma (also designated NEMO), and each appears to make essential contributions to IkB phosphorylation (6). IKAP (IKK-complex-associated protein) is a protein that acts as a scaffold, interacting with NIK, IKK alpha and IKK beta and assembling them into an active kinase complex (7,8)

Supplier: ProSci Inc.

PIWI-L1 Antibody: PIWI-L1 is a member of the PIWI subfamily of Argonaute proteins, evolutionarily conserved proteins containing both PAZ and Piwi motifs that are crucial for the biogenesis and function of small non-coding RNAs and play important roles in stem cell self-renewal, RNA silencing, and translational regulation in diverse organisms. PIWI-L1 is thought to play a role as an intrinsic regulator of the self-renewal capacity of germline and hematopoietic stem cells as removing PIWI-L1 protein from single germline stem cells significantly decreases the rate of their division. Recent studies have shown that overexpression of PIWI-L1 (as well as other PIWI-like proteins) are potential biomarkers for colon and other cancers.

Supplier: ProSci Inc.

Adiponectin is a secreted protein. It is Synthesised exclusively by adipocytes and secreted into plasma. Adiponectin is an important adipokine that is involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Adiponectin Stimulates AMPK phosphorylation and activates in the liver and the skeletal muscle, enhancing glucose utilisation and fatty-acid combustion. Adiponectin also antagonises TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. It inhibits endothelial NF-kappa-B signalling through a cAMP-dependent pathway. Adiponectin may play a role in cell growth, angiogenesis and tissue remodelling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex: LMW, MMW or HMW.

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PIWI-L2 Antibody: PIWI-L2 is a member of the PIWI subfamily of Argonaute proteins, evolutionarily conserved proteins containing both PAZ and Piwi motifs that are crucial for the biogenesis and function of small non-coding RNAs and play important roles in stem cell self-renewal, RNA silencing, and translational regulation in diverse organisms. PIWI-L2 has been implicated in multiple roles including stem cell self-renewal and is highly expressed in many breast cancers. In these tumors, PIWI-L2 silences the expression of STAT3, a regulator of Bcl-XL and cyclin D1, allowing the proliferation and survival of breast cancer stem cells. Recent studies have shown that overexpression of PIWI-like proteins are potential biomarkers for colon and other cancers.

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Adiponectin is a secreted protein. It is synthesised exclusively by adipocytes and secreted into plasma. Adiponectin is an important adipokine that is involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Adiponectin Stimulates AMPK phosphorylation and activates in the liver and the skeletal muscle, enhancing glucose utilisation and fatty-acid combustion. Adiponectin also antagonises TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. It inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. Adiponectin may play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex: LMW, MMW or HMW.

Supplier: ProSci Inc.

Adiponectin is a secreted protein. It is synthesized exclusively by adipocytes and secreted into plasma. Adiponectin is an important adipokine that is involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Adiponectin Stimulates AMPK phosphorylation and activates in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Adiponectin also antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. It inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. Adiponectin may play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex: LMW, MMW or HMW.

Supplier: ProSci Inc.

Peroxiredoxin-1(PRDX1) contains 1 thioredoxin domain and belongs to the AhpC/TSA family. PRDX1 constitutively expressed in most human cells and it is induced to higher levels upon serum stimulation in untransformed and transformed cells. PRDX1 is involved in redox regulation of the cell. It reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin and play an important role in eliminating peroxides generated during metabolism. PRDX1 might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. It reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation. It may contribute to the antiviral activity of CD8(+) T-cells and have a proliferative effect in cancer development or progression.

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PIWI-L2 Antibody: PIWI-L2 is a member of the PIWI subfamily of Argonaute proteins, evolutionarily conserved proteins containing both PAZ and Piwi motifs that are crucial for the biogenesis and function of small non-coding RNAs and play important roles in stem cell self-renewal, RNA silencing, and translational regulation in diverse organisms. PIWI-L2 has been implicated in multiple roles including stem cell self-renewal and is highly expressed in many breast cancers. In these tumors, PIWI-L2 silences the expression of STAT3, a regulator of Bcl-XL and cyclin D1, allowing the proliferation and survival of breast cancer stem cells. Recent studies have shown that overexpression of PIWI-like proteins are potential biomarkers for colon and other cancers.

Supplier: Brand

PP. Eight connected 0,2 or 0,15 ml PCR tubes with attached, flat individual caps.

Supplier: Brand

PP. Eight connected 0,2 or 0,15 ml PCR tubes with attached flat individual caps. The tubes are held together by three connectors for increased rigidity.

Supplier: ProSci Inc.

Serpin F1 is a secreted glycoprotein that belongs to the noninhibitory serpin. It has an alpha/beta core serine-protease inhibitor domain, three major beta-sheets, and ten alpha-helices. As protease inhibitors, serpins have an array of functions including regulating blood clotting, the complement pathway, extracellular matrix remodeling, and cell motility. They are also involved in activities that extend beyond their ability to inhibit proteases. For instance, they may also regulate blood pressure, angiogenesis, or act as storage/transport proteins. Serpin F1 is a new promising approach for the treatment of osteosarcoma and has been described as a natural angiogenesis inhibitor with neurotrophic and immune-modulation properties. The human serpin superfamily consists of at least 35 members that target not only serine proteases, but also selected cysteine proteases and non-protease proteins. Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.