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: Abcam

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

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: 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: Abcam

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

Supplier: Abcam

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

Supplier: ProSci Inc.

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: ProSci Inc.

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: 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 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 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.

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 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.

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.

Supplier: Brand

PP. Eight connected 0,2 ml tubes and separate domed or flat caps in strips of 8.

Supplier: Brand

PP. Eight connected 0,2 ml tubes and domed or flat caps in strips of eight.

Supplier: Brand

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

Supplier: ProSci Inc.

NOV, also called CCN3, is a secreted protein of CCN family members. CCN family members are highly conserved cysteine rich proteins sharing a common modular structure having 4 conserved domains, insulin-like growth factor-binding protein (IGFBP) domain, von Willebrand type C (VWC) domain, thrombospondin-1 (TSP-1) domain, and C-terminal (CT) domain (absent in CCN5). By specific interactions with these domains, CCN proteins modulate multiple signalling pathways including BMPs, Wnt, TGFs, Notch and integrins to regulate cell proliferation, differentiation, adhesion, migration, angiogenesis, and survival. CCN3 is firstly characterised as a promoter of progenitor activity of human hematopoietic stem cells, as knockdown of CCN3 can abrogate the function of primitive progenitors. Recent studies showed that CCN3 is also actively involved in the process of wound healing. CCN3 is highly expressed in granulation tissues of cutaneous wounds and capable of inducing synthetic responses of fibroblasts.

Supplier: Brand

PP. Eight connected 0,2 ml tubes with attached domed cap strips.

Supplier: Quantabio

Q qPCR cycler uses a patented magnetic induction technology to rapidly heat samples, coupled with fan-forced air for cooling to acquire data in only 25 minutes. Available as four channel models, the robust optical system acquires all channels simultaneously and allows for running the fastest multiplexed assays.

Supplier: Quantabio

PerfeCTa® MultiPlex qPCR ToughMix® is a 5X concentrated, ready to use reaction cocktail for Real-Time quantitative PCR (qPCR) that overcomes many known inhibitors of PCR often present in crude samples extracted from environmental specimens, plant tissues, or animal tissues. It contains all components, except primers, probes and templates. The 5X concentrated ToughMix® allows addition of higher amounts of template and improved detection sensitivity with low concentration samples. PerfeCta® MultiPlex qPCR ToughMix® has been optimised to deliver maximum PCR efficiency, sensitivity, and specificity in reduced reaction volumes with fast cycle or conventional PCR cycling protocols.

Supplier: Quantabio

This SuperMix is a 2X concentrated, ready to use reaction cocktail for Real-Time qPCR that contains all components, except primers, probes, and templates. The system transcends multiplex limitations of conventional PCR master mixes, enabling unbiased amplification of up to five target sequences in a single tube. Suppression of low copy amplicons by high copy reference targets in the amplification is a common problem in multiplex PCR. This can skew, or mask the apparent representation and quantification of low copy target sequences. PerfeCTa® MultiPlex qPCR SuperMix delivers dynamic range and sensitivity to multiplexed qPCR that is comparable to that for singleplex qPCR probe assays without the need for limiting or variable primer concentrations.

Supplier: Cytiva (Formerly Pall Lab)

Reusable TFF devices and system for bioprocessing applications that accelerates and simplifies processing of up to 1 L.

Supplier: ProSci Inc.

IKAP Antibody: IKAP was initially identified as a scaffold protein of the I kappa B kinase complex that could bind to IKK alpha , IKK beta , NF-kappa B, and the NF-kappa B-inducing kinase (NIK), although later evidence has cast doubt on this. More recent reports show that mutations in IKAP such as a frameshift leading to a truncated protein or a missense mutation that leads to defective phosphorylation are responsible for the autosomal recessive genetic disease familial dysautonomia (FD). Reports indicating that it forms part of the RNA polymerase II transcription elongation complex suggest that this disease may be due to compromised transcription elongation. More recently, it was shown that IKAP associates with c-Jun N-terminal kinase (JNK) and could specifically enhance JNK activation induced by the upstream JNK activators MEKK1 and ASK1, indicating another possible cause for FD. At least two isoforms of IKAP are known two exist.