5787 Results for: "extraction"

Supplier: Rockland Immunochemical

NOX1(NADPH OXIDASE 1), also known as NOH1, MOX1 or GP91-2, is an enzyme that in humans is encoded by the NOX1 gene. It is also a homolog of the catalytic subunit of the superoxide-generating NADPH oxidase of phagocytes, gp91phox. The NOX1 gene is mapped to Xq22.1. NOX1 was expressed in colon, prostate, uterus, and vascular smooth muscle, but not in peripheral blood leukocytes. The deduced 564-amino acid NOX1 protein, which is 58% identical to CYBB, contains 6 membrane-spanning regions, conserved flavin and pyridine nucleotide-binding sites, and histidines possibly involved in heme ligation. Overexpression of MOX1 in NIH 3T3 cells increased superoxide generation and cell growth. Cells expressing MOX1 had a transformed appearance, showed anchorage-independent growth, and produced tumors in athymic mice. Disruption of either Nox1 or Nox2 significantly delayed progression of motor neuron disease in these mice. However, 50% survival rates were enhanced significantly more by Nox2 deletion than Nox1 deletion. This antibody is suitable for researchers interested in epigenetic antibodies and cancer research.

Supplier: Rockland Immunochemical

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the telomeric copy. Anti-Histone H3 are ideal for researchers interested in Chromatin Modifiers, Chromatin Research, Histones and Modified Histones, and Epigenetics Research.

Supplier: Rockland Immunochemical

SLC22A6(Solute carrier family 22 (organic anion transporter), member 6), also called OAT1 or PAHT, is a protein that in humans is encoded by the SLC22A6 gene, which is also a member of the organic anion transporter (OAT) family of proteins. OAT1 is a transmembrane protein that is expressed in the brain, the placenta, the eyes, smooth muscles, and the basolateral membrane of proximal tubular cells of the kidneys. The SLC22A6 gene is mapped on 11q12.3. It plays a central role in renal organic anion transport. Along with OAT3, OAT1 mediates the uptake of a wide range of relatively small and hydrophilic organic anions from plasma into the cytoplasm of the proximal tubular cells of the kidneys. The SLC22A6 gene contains 10 exons and spans 8.2 kb. OAT1 functions as organic anion exchanger. When the uptake of one molecule of an organic anion is transported into a cell by an OAT1 exchanger, one molecule of an endogenous dicarboxylic acid (such as glutarate, ketoglutarate, etc) is simultaneously transported out of the cell. PAH uptake in Xenopus oocytes injected with OAT1 mRNA was demonstrated by Race et al. This antibody is suitable for researchers interested in cancer research.

Supplier: Rockland Immunochemical

Signal transducer and activator of transcription 3 (Stat3) belongs to a family of cytoplasmic transcription factors that can be activated by phosphorylation by its cell surface receptor. Stat3 plays a key role in many cellular processes such as cell growth and apoptosis. It also mediates cellular responses to interleukins, KITLG/SCF,EGF, IFN-alpha and other growth factors and may mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Stat3 forms a homodimer or a heterodimer with a related family member (e.g. STAT1). Activation occurs through phosphorylation of tyrosine 705 and serine 727. Phosphorylation of Stat3 at Tyr705 induces Stat3 dimerization and nuclear translocation. Serine phosphorylation is important for stable DNA-binding of Stat3 homodimers and maximal transcriptional activity. Stat3 can have a dual role in cancer, it has been found that Stat3 protein can promote oncogenesis and have a tumor suppressor role depending upon the mutational background of the tumor.

Supplier: Rockland Immunochemical

ITGA3(INTEGRIN, ALPHA-3), also called CD49C, VLA3 or GAPB3, is a protein that in humans is encoded by the ITGA3 gene. ITGA3 is an integrin alpha subunit which is also a member of the family of cell surface adhesion molecules. ITGA3 is mapped to chromosome 17 and its exact cytogenetic location is 17q21.33. ITGA3 makes up half of the alpha3beta1 integrin duplex that plays a role in neural migration and corticogenesis together with beta-1 subunit.A functional link between DAB1 phosphorylation and ITGA3 signaling drives the timely detachment of migrating neurons from radial glial fibers. Expression of human ITGA3 increased the infectivity of virus for Chinese hamster ovary cells. ITGA3 also contains 13 potential N-glycosylation sites, 2 potential cleavage sites, and the 7 N-terminal repeating units characteristic of ITGAs. Recombinant ITGA3 is expressed as a 150-kD protein as the same size as the native protein by the western blot analysis. This antibody is suitable for researchers interested in cancer research.

Supplier: Rockland Immunochemical

NOX2(NADPH OXIDASE 2), also called CYBB(CYTOCHROME b(-245), BETA SUBUNIT), p91-PHOX or GP91-1, is a human gene encoding a glycoprotein.NOX2 is an essential component of phagocytic NADPH-oxidase, a membrane-bound enzyme complex that generates large quantities of microbicidal superoxide and other oxidants upon activation. It is mapped on Xp11.4. NOX2 is a heterodimer composed of an alpha chain of relative molecular mass 23 kD and a beta chain of 76 to 82 kD. NOX2 assembled on DC phagosomes in a gp91-phox subunit-dependent manner, and that reactive oxygen species were produced in a more sustained manner in immature DC phagosomes than in macrophage phagosomes .As a major player in innate immune responses in neutrophils,NOX2 is also involved in adaptive immunity through its activity in DCs. In heart cells, physiologic stretch rapidly activates reduced-form NOX2 to produce reactive oxygen species (ROS) in a process dependent on microtubules (X-ROS signaling). This antibody is suitable for researchers interested in cancer research.

Supplier: Rockland Immunochemical

MUC1 is a large cell surface mucin glycoprotein expressed by most glandular and ductal epithelial cells and some hematopoietic cell lineages. It is expressed on most secretory epithelium, including mammary gland and some hematopoietic cells. It is expressed abundantly in lactating mammary glands and overexpressed abundantly in >90% breast carcinomas and metastases. Transgenic MUC1 has been shown to associate with all four cebB receptors and localize with erbB1 (EGFR) in lactating glands. The MUC1 gene contains seven exons and produces several different alternatively spliced variants. The major expressed form of MUC1 uses all seven exons and is a type 1 transmembrane protein with a large extracellular tandem repeat domain. The tandem repeat domain is highly O glycosylated and alterations in glycosylation have been shown in epithelial cancer cells. This antibody is suitable for researchers interested in neuroscience research, developmental signaling, and cell adheshion.

Supplier: Rockland Immunochemical

Anti-NEMO antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Anti-NEMO antibody detects recombinant and endogenous NEMO. NEMO, the regulatory subunit of the IKK core complex, phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. Nemo is also considered to be a mediator for TAX activation of NF-kappa-B and may be implicated in NF-kappa-B-mediated protection from cytokine toxicity. NEMO is essential for viral activation of IRF3 and involved in TLR3- and IFIH1-mediated antiviral innate response. The innate antivaral response from NEMO requires 'Lys-27'-linked polyubiquitination. Anti-NEMO is ideal for researchers interested in Immunology and Cancer research.

Supplier: Biosensis

FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include SYT11, CCNE1, GPR37, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP and SEPT5. May play a more general role in the ubiquitin proteasomal pathway by participating in the removal and/or detoxification of abnormally folded or damaged protein. Loss of this ubiquitin ligase activity appears to be the mechanism underlying pathogenesis of PARK2. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. Regulates cyclin E during neuronal apoptosis. May represent a tumor suppressor gene. SUBCELLULAR LOCATION: Cytoplasm. Co-localizes with STY11 in neutrites. Co-localizes with SNCAIP in brainstem Lewy bodies. TISSUE SPECIFICITY: Highly expressed in the brain including the substantia nigra. Expressed in heart, testis and skeletal muscle. Expression is down-regulated or absent in tumor biopsies, and absent in the brain of PARK2 patients. Overexpression protects dopamine neurons from kainate-mediated apoptosis.

Supplier: Rockland Immunochemical

TP53 (tumor suppressor gene p53) is one of the most well-studied genes that suppresses tumor formation and renders protection against DNA damage by inducing cell cycle arrest, DNA repair, or apoptosis. TP53 signaling is triggered through numerous cellular events ranging from DNA damage to hypoxia, stress and a plethora of other causes. Upon activation, p53 acts as zinc-containing transcriptional regulator and initiates a cascade of events that determines the cellular outcome including cell cycle arrest, apoptosis, senescence, DNA repair, development, differentiation and tissue homeostasis. Cell cycle arrest is induced by p53 via trans-activating genes such as p21 (CDK-inhibitor 1, cyclin dependent kinase) and others. Interestingly, p53 itself is capable of triggering cellular responses (survival or induced cell death) as well. Mutations or deletions in the TP53 gene are present in nearly 50% of human cancers, and primarily results in impaired tumor suppressor function. Anti-p53 (ac Lys292) antibody is ideal for researchers interested in developmental biology, cell growth and cancer research.

Supplier: Rockland Immunochemical

SIRT1 antibody detects human SIRT1 protein. SIRT1 is a member of the sirtuin family of protein-modifying enzymes. SIRT1 is a NAD+-dependent deacetylase that plays an important role in many cellular processes. SIRT1 protein is known to regulate epigenetic gene silencing and suppress recombination of rDNA. SIRT1 deacetylates a wide range of substrates, including p53, NF-kB, FOXO transcription factors, and PGC-1 alpha, with roles in cellular processes such as muscle differentiation, adipogenesis, protection from axonal degeneration, and life span extension. SIRT1 is downregulated in cells that have high insulin resistance and inducing its expression increases insulin sensitivity, suggesting the molecule is associated with improving insulin sensitivity. Furthermore, SIRT1 de-acetylates and affects the activity of both members of the PGC1-alpha/ERR-alpha complex, which are essential metabolic regulatory transcription factors. Anti-SIRT1 Antibody is useful for researcher involved in research areas including cancer, diabetes, aging, neurodegenerative, metabolic or cardiovascular diseases.

Supplier: Rockland Immunochemical

TP53 (tumor suppressor gene p53) is one of the most well-studied genes that suppresses tumor formation and renders protection against DNA damage by inducing cell cycle arrest, DNA repair, or apoptosis. TP53 signaling is triggered through numerous cellular events ranging from DNA damage to hypoxia, stress and a plethora of other causes. Upon activation, p53 acts as zinc-containing transcriptional regulator and initiates a cascade of events that determines the cellular outcome including cell cycle arrest, apoptosis, senescence, DNA repair, development, differentiation and tissue homeostasis. Cell cycle arrest is induced by p53 via trans-activating genes such as p21 (CDK-inhibitor 1, cyclin dependent kinase) and others. Interestingly, p53 itself is capable of triggering cellular responses (survival or induced cell death) as well. Mutations or deletions in the TP53 gene are present in nearly 50% of human cancers, and primarily results in impaired tumor suppressor function. Anti-p53 (ac Lys305) antibody is ideal for researchers interested in developmental biology, cell growth and cancer research.

Supplier: Rockland Immunochemical

Histones are the main constituents of the protein part of chromosomes of eukaryotic cells. They are rich in the amino acids arginine and lysine and have been greatly conserved during evolution. Histones pack the DNA into tight masses of chromatin. Two core histones of each class H2A, H2B, H3 and H4 assemble and are wrapped by 146 base pairs of DNA to form one octameric nucleosome. Histone tails undergo numerous post-translational modifications, which either directly or indirectly alter chromatin structure to facilitate transcriptional activation or repression or other nuclear processes. In addition to the genetic code, combinations of the different histone modifications reveal the so-called “histone code”. Histone methylation and demethylation is dynamically regulated by respectively histone methyl transferases and histone demethylases. Levels of H3K27 dimethylation are higher in silent genes than in active genes suggesting that this histone modification is associated with transcriptional repression. Anti-H3K27me2 Antibody is ideal for research in Chromatin Remodeling, Epigenetics and Gene Expression.

Supplier: Rockland Immunochemical

Anti-HSF1 Antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Heat shock factor 1 (HSF1) is a highly conserved transcription factor that coordinates stress-induced transcription and directs versatile physiological processes in eukaryotes. Upon stress, HSF1 is the key transcriptional activator of chaperones, co-chaperones and ubiquitin, and also coordinates the expression of many transcriptional and translational regulators, signaling molecules and mitotic determinants. HSF1 is involved in balancing core cellular processes during stress and enables their rapid re-establishment once conditions suitable for proliferation have been restored. Importantly, HSF1 controls a distinct set of target genes in cell stress, development and cancer progression. The central role of HSF1 in diverse cellular functions is reflected in pathologies, such as neurodegenerative diseases and cancer, where an imbalance in HSF1 activity facilitates disease onset. The ability of cancer cells to harness HSF1 for metastatic progression highlights the plasticity of HSF1 in rewiring transcription and coordinating cellular processes. Anti-HSF1 antibody is thus ideal for investigators involved in cancer research and neurodegenerative diseases.

Supplier: Genetex

Histone proteins H3, H4, H2A, and H2B function as building blocks to package eukaryotic DNA into repeating nucleosome units that are folded in higher order chromatin fibers. The nucleosome is composed of an octamer containing a H3/H4 tetramer and two H2A/H2B dimers, surrounded by approximately 146 base pairs of DNA. A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation occurs on the N-terminal tail domains of histones. Acetylation of lysine residues within these N-terminal domains by histone acetyl-transferases (HATs), including Gcn5p, P/CAF, p300/CBP, and TAFII250, is associated with transcriptional activation. This modification results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. Conversely, histone deacetylation by histone deacetylases (HDACs) is associated with transcription repression reversing the chromatin remodeling process. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms.

Supplier: Rockland Immunochemical

Peripherin Antibody detects Peripherin. Peripherin is a ~57kDa intermediate filament subunit found initially in sensory neurons of the peripheral nervous systems, which gives the protein its name. Subsequently, peripherin was found in some sensory and other neurons of the central nervous system and also in PC12 cells. Peripherin is also expressed in certain neuroendocrine tumors and in the insulin producing cells of the pancreas. Peripherin belongs to the Class III family of intermediate filament subunits which also includes vimentin, glial fibrillary acidic protein (GFAP) and desmin. In contrast to the neurofilaments, peripherin is strongly up-regulated after nerve injury. Antibodies to peripherin can be used in identifying, classifying, and studying neurons throughout the nervous system. Peripherin is also a good diagnostic marker for ballooned axons seen in Lou Gehrig's disease (Amyotrophic lateral sclerosis) and some neuronally derived tumors. Autoantibodies to peripherin are frequently seen in the sera of patients with diabetes. Peripherin is not related to peripherin/RDS, a protein of the photoreceptor outer membrane mutations of which are causative of certain forms of slow retinal degeneration. Anti-Peripherin Antibody is ideal for investigators involved in Neuroscience and Cancer research.

Supplier: Genetex

Histone proteins H3, H4, H2A, and H2B function as building blocks to package eukaryotic DNA into repeating nucleosome units that are folded in higher order chromatin fibers. The nucleosome is composed of an octamer containing a H3/H4 tetramer and two H2A/H2B dimers, surrounded by approximately 146 base pairs of DNA. A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation occurs on the N-terminal tail domains of histones. Acetylation of lysine residues within these N-terminal domains by histone acetyl-transferases (HATs), including Gcn5p, P/CAF, p300/CBP, and TAFII250, is associated with transcriptional activation. This modification results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. Conversely, histone deacetylation by histone deacetylases (HDACs) is associated with transcription repression reversing the chromatin remodeling process. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms.

Supplier: Genetex

Arginine methylation is an irreversible post translational modification which has only recently been linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These protein include nuclear proteins (Histone 2A, 3, 4), IL enhancer binding factor, nuclear factors (NF45, 90, ILF3, Nucleolin, STAT1, Poly(A) binding protein II), cell cycle proteins (phosphoprotein phosphatase 2A), signal transduction proteins (FGF2, Fibrillarin, FN, INFAR1, Jak, MBP, Src-adaptor Sam68), apoptosis proteins (FADD, ICE-like protease), and viral proteins (Hepatitis C NS3 RNA Helicase, HIV TAR). The mammalian PRMT family currently consists of 5 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all five PRMT members have been developed. These antibodies can be utilized to explore arginine methylation and its regulatory functions.

Supplier: Eagle Biosciences

Mouse Urocortin 2 ELISA is used to detect urocortin 2 in mouse plasma & serum samples.

Supplier: MP Biomedicals

MP Biomedicals' FastPrep-96™ is a versatile high-speed homogenizer offering the ultimate in high-throughput sample preparation. FastPrep-96™ is used to homogenize biological samples. FastPrep-96 Instrument lyses thoroughly and quickly any tissues and cells and thus allows easy and reproducible isolation of stable RNA, active proteins, and full-length genomic DNA. This high-performance system saves hours of work during the sample preparation stage. The FastPrep-96™ instrument features high-throughput processing of up to 192 samples simultaneously in 2×96 deep well plates. Versatile interchangeable adapters are available for 2×96 deep well plates, 96×2 ml tubes, 48×4.5 ml tubes, 24×15 ml tubes, 8×50 ml tubes, and 1×250 ml flasks.

Supplier: Genetex

SIR2, one of the silent information regulator genes, encodes a protein that promotes a compact chromatin structure, thereby preventing or silencing gene transcription at selected loci. SIR2 belongs to a family of proteins that is found in organisms ranging from bacteria to complex eukaryotes. Members of this family contain a 250 amino acid core domain that shares about 25-60% sequence identity. Silencing occurs as a series of events initiated by formation of Sir complexes (Sir2, Sir3, Sir4). The complexes are recruited to their chromosome targets via interactions with DNA-binding proteins, followed by deacetylation of histones H3 and H4. A final step required for telomeric silencing is binding of the complex to the deacetylated histones and recruitment of the telosome to the nuclear periphery. Sir2 protein is an NAD-dependent histone deacetylase, an enzyme that removes acetyl groups from lysine residues of histone proteins and possibly other substrates. Sir2 transfers acetyl groups from its protein substrates to ADP-ribose and synthesizes o-acetyl-ADP-ribose. Through histone deacetylation, Sir2 may silence chromatin. The maintenance or silencing of chromatin may be at the center of processes leading to aging of cells and development of cancer.

Supplier: Genetex

Syntaxin 1, also known as HPC1, is a 35 kDa integral membrane protein which along with SNAP25, and VAMP/synaptobrevin plays a role in vesicular trafficking and membrane fusion. Two Syntaxin 1 isoforms have been identified, Syntaxin 1A which is localized to nerve terminals of sensory neurons and nerve fibers reaching small blood vessels, and Syntaxin 1B which is localized to motor end plates and muscle spindles. The SNARE (soluble N-ethylmaleimide sensitive fusion protein [NSF] attachment protein [SNAPs] receptors)hypothesis of membrane fusion proposes that Syntaxin 1A and SNAP25 (target membrane SNAREs, t-SNAREs) and VAMP/synaptobrevin (vesicular SNAREs, vSNAREs) bind together to form a tripartite structure that along with soluble cytosolic proteins allows for close membrane apposition of donor and target membranes thereby facilitating membrane fusion. The interaction of Syntaxin 1A with vSNAREs is thought to be negatively regulated by the binding of Munc18 to Syntaxin 1A and this interaction is controlled by Cdk5 phosphorylation of Munc18. Syntaxin 1A can be phosphorylated by casein kinase II and phosphorylation of Syntaxin enhances its interaction with Synaptotagmin.

Supplier: Rockland Immunochemical

TP53 (tumor suppressor gene p53) is one of the most well-studied genes that suppresses tumor formation and renders protection against DNA damage by inducing cell cycle arrest, DNA repair, or apoptosis. TP53 signaling is triggered through numerous cellular events ranging from DNA damage to hypoxia, stress and a plethora of other causes. Upon activation, p53 acts as zinc-containing transcriptional regulator and initiates a cascade of events that determines the cellular outcome including cell cycle arrest, apoptosis, senescence, DNA repair, development, differentiation and tissue homeostasis. Cell cycle arrest is induced by p53 via trans-activating genes such as p21 (CDK-inhibitor 1, cyclin dependent kinase) and others. Interestingly, p53 itself is capable of triggering cellular responses (survival or induced cell death) as well. Mutations or deletions in the TP53 gene are present in nearly 50% of human cancers, and primarily results in impaired tumor suppressor function. Anti-p53 (ac Lys305) antibody is ideal for researchers interested in developmental biology, cell growth and cancer research.

Supplier: Rockland Immunochemical

Anti-HSF1 Antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Heat shock factor 1 (HSF1) is a highly conserved transcription factor that coordinates stress-induced transcription and directs versatile physiological processes in eukaryotes. Upon stress, HSF1 is the key transcriptional activator of chaperones, co-chaperones and ubiquitin, and also coordinates the expression of many transcriptional and translational regulators, signaling molecules and mitotic determinants. HSF1 is involved in balancing core cellular processes during stress and enables their rapid re-establishment once conditions suitable for proliferation have been restored. Importantly, HSF1 controls a distinct set of target genes in cell stress, development and cancer progression. The central role of HSF1 in diverse cellular functions is reflected in pathologies, such as neurodegenerative diseases and cancer, where an imbalance in HSF1 activity facilitates disease onset. The ability of cancer cells to harness HSF1 for metastatic progression highlights the plasticity of HSF1 in rewiring transcription and coordinating cellular processes. Anti-HSF1 antibody is thus ideal for investigators involved in cancer research and neurodegenerative diseases.

Supplier: Rockland Immunochemical

STAT2 is a member of the STAT family of transcription factors. Unlike other STATs, STAT2 is unique as it can only be activated by interferons (IFNs). STAT2 is a critical component in mediating many IFN-stimulated biological activities including antiproliferation and antiviral responses. Upon IFN treatment, STAT1 and STAT2 become tyrosine phosphorylated, assemble as heterodimers that bind IRF9 to form the ISGF3 complex. This complex translocates to the nucleus, binds to promoters of IFN-stimulated genes and mediates gene transcription. Consequently, mutations in STAT2 or loss of STAT2 expression leads to impairment in IFN signal transduction and gene activation. IFN-alpha is an approved drug for the treatment of several forms of cancer. Yet only a subset of patients who receive IFN-alpha therapy benefit from the treatment. Given that STAT2 is activated by IFNs, it is important to define if the reduced or lack of antitumor effects seen in cancer patients on IFN therapy is due to in defects in STAT2 function. STAT2 pS734 antibody is ideal for researchers focused in cancer and transcripton factor research.

Supplier: Rockland Immunochemical

SIRT1 antibody detects human SIRT1 protein. SIRT1 is a member of the sirtuin family of protein-modifying enzymes. SIRT1 is a NAD+-dependent deacetylase that plays an important role in many cellular processes. SIRT1 protein is known to regulate epigenetic gene silencing and suppress recombination of rDNA. SIRT1 deacetylates a wide range of substrates, including p53, NF-kB, FOXO transcription factors, and PGC-1 alpha, with roles in cellular processes such as muscle differentiation, adipogenesis, protection from axonal degeneration, and life span extension. SIRT1 is downregulated in cells that have high insulin resistance and inducing its expression increases insulin sensitivity, suggesting the molecule is associated with improving insulin sensitivity. Furthermore, SIRT1 de-acetylates and affects the activity of both members of the PGC1-alpha/ERR-alpha complex, which are essential metabolic regulatory transcription factors. Anti-SIRT1 Antibody is significant for researchers involved in research areas including cancer, diabetes, aging, neurodegenerative, metabolic and cardiovascular diseases.

Supplier: Rockland Immunochemical

UCHL1 antibody recognizes Ubiquitin C-terminal hydrolase 1 (UCHL1) which is also known as ubiquitin carboxyl esterase L1, ubiquitin thiolesterase, neuron-specific protein PGP9.5 and Park5. It was originally identified as a major component of the neuronal cytoplasm from 2-dimensional gel analysis of brain tissues, and was given the name PGP9.5. It was later found that ubiquitin C-terminal hydrolase enzyme activity was associated with the PGP9.5 protein. The ubiquitin C-terminal hydrolases cleave ubiquitin from other molecules. Regulation of the ubiquitin pathway is very important and many disease states are associated with defects in this pathway. Genetic knockout of UCHL1 in mice results in a motor neuron degeneration similar to the spontaneous gracile axonal dystrophy (gad) mutant mice. Point mutations in the UCHL1 gene are associated with some forms of human Parkinson's disease. Since UCHL1 is heavily expressed in neurons, it is released in large amounts following injury or degeneration, so the detection of UCHL1 in CSF and other bodily fluids can be used as a biomarker.
Therefore, UCHL1 monoclonal antibody is ideal for investigators involved in Neuroscience.

Supplier: Rockland Immunochemical

NLRP3(NLR FAMILY, PYRIN DOMAIN-CONTAINING 3),also known as CIAS1, CRYOPYRIN, NALP3 or PYPAF1, is a protein that in humans is encoded by the NLRP3 (NOD-like receptor family, pryin domain containing 3) gene. The NLRP3 gene encodes a pyrin-like protein expressed predominantly in peripheral blood leukocytes. And the NLRP3 gene is mapped on 1q44. NLRP3 interacts with apoptosis-associated speck-like protein containing a CARD (ASC). The encoded protein may play a role in the regulation of inflammation and apoptosis. Mutation of the NALP3 nucleotide-binding domain reduced ATP binding, CASP1 activation, IL1B production, cell death, macromolecular complex formation, self-association, and association with ASC. Consistent with an essential role for Nlrp3 inflammasomes in antifungal immunity, Gross et al.showed that Nlrp3-deficient mice are hypersusceptible to C. albicans infection. Activation of the NLRP3 inflammasome in response to virus or to RNA was dependent upon lysosomal maturation and reactive oxygen species production in human cells. The NLRP3 inflammasome senses obesity-associated danger signals and contributes to obesity-induced inflammation and insulin resistance. This antibody is suitable for researchers interested in cancer research.

Supplier: Rockland Immunochemical

Smad2 is designed, produced, and validated as part of a collaboration between Rockland and the National Cancer Institute (NCI). Smad2 (Mothers against decapentaplegic homolog 2) is a member of the Smad family of proteins which are similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signal of the transforming growth factor (TGF)-beta, and thus regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. This protein is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors. The phosphorylation induces the dissociation of this protein with SARA and the association with the family member SMAD4. The association with SMAD4 is important for the translocation of this protein into the nucleus, where it binds to target promoters and forms a transcription repressor complex with other cofactors. Anti-SMAD2 pS465 pS467 antibody is ideal for researchers interested in Cancer, Immunology and Nuclear Signaling research.

Supplier: Rockland Immunochemical

STAT2 is a member of the STAT family of transcription factors. Unlike other STATs, STAT2 is unique as it can only be activated by interferons (IFNs). STAT2 is a critical component in mediating many IFN-stimulated biological activities including antiproliferation and antiviral responses. Upon IFN treatment, STAT1 and STAT2 become tyrosine phosphorylated, assemble as heterodimers that bind IRF9 to form the ISGF3 complex. This complex translocates to the nucleus, binds to promoters of IFN-stimulated genes and mediates gene transcription. Consequently, mutations in STAT2 or loss of STAT2 expression leads to impairment in IFN signal transduction and gene activation. IFN-alpha is an approved drug for the treatment of several forms of cancer. Yet only a subset of patients who receive IFN-alpha therapy benefit from the treatment. Given that STAT2 is activated by IFNs, it is important to define if the reduced or lack of antitumor effects seen in cancer patients on IFN therapy is due to in defects in STAT2 function. STAT2pS734 antibody is ideal for researchers focused in cancer and transcripton factor research.