299 Results for: "assay 11-55"

Supplier: Genetex

Lymphoid enhancer factor, LEF1, is a transcription factor of the High Mobility Group of DNA binding proteins. It is one member of a family of four proteins referred to as LEF/TCF transcription factors (LEF1, TCF1, TCF3 and TCF4). These factors play crucial roles in WNT/Wingless signaling, a signal transduction cascade that directs cell differentiation. Aberrant activation of the WNT/Wingless pathway is also a root cause in the genesis of certain cancers such as colon cancer, melanoma and breast cancer.

Supplier: Thermo Scientific

Kit has been optimized to incorporate 1-3 biotinylated ribonucleotides (biotin-N4-CTP) onto the 3' end of DNA strands where the label will be less likely to interfere with hybridization or sequence-specific binding of proteins.

Supplier: Genetex

Psoriasin/HID-5 was originally identified as an up-regulated protein in psoriatic keratinocytes. Subsequently, this protein was found to have elevated expression in abnormally differentiating primary keratinocytes and in various carcinomas, including ductal carcinoma in situ. Psoriasin/HID-5 may play a role in the establishment or maintenance of these pathologies, and may serve as a diagnostic marker of particular tumour types or abnormally proliferative epithelia.

Supplier: Genetex

This chemotactic factor attracts monocytes and basophils but not neutrophils or eosinophils and augments monocyte anti-tumor activity. It has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis or atherosclerosis. It may be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis.

Supplier: Cayman Chemical Company

A sensitive detection method for measuring both the free acid and ethyl amide forms of 17-phenyl trinor PGF_2α.

Supplier: Biosensis

Biosensis is proud to offer the first commercially available ApoE/β-amyloid (ApoE/Aβ) complex ELISA kit. As a result of extensive collaboration with Dr. LaDu’s laboratory at UIC and validation by Biosensis, this ELISA can be used to accurately and consistently measure the extent of ApoE/Aβ complex in tissue extracts and other samples.

Supplier: Genetex

Mouse monoclonal [6217] to IL8

Supplier: MOLECULAR DEVICES LLC. CA

Unparalleled performance on a personalized platform. The SpectraMax® iD3 Multi-Mode Microplate Reader is the cornerstone of a complete laboratory solution designed to expand the boundaries of research capabilities. With optimized reagents and the industry-leading data acquisition and analysis tool, SoftMax Pro® 7 Software, the SpectraMax® iD3 allows users to customize workflow to perfectly match their needs.

Supplier: Biosensis

The Mature BDNF Rapid^TM ELISA Kit is a sandwich ELISA that allows the quantification of mature BDNF in less than 3 hours in cell culture supernatants, serum, plasma (citrate and EDTA), pig serum, cell lysates, brain extracts, human milk and sheep CSF only if used as directed, with a simplified protocol and no loss of sensitivity or specificity.

Supplier: Biosensis

The Biosensis proBDNF RapidTM ELISA Kit is a sandwich ELISA that allows the specific, fast and reliable quantification of proBDNF in less than 4 hours in cell culture supernatants, cell lysates, serum, citrate-plasma and tissue extracts only if used as directed. Please refer to the kit protocol for specific use instructions for each substrate application, in particular human blood samples.

Supplier: Thermo Scientific

Empower the analysis and bring versatility and productivity to your lab with the Evolution UV-Vis spectrophotometers. With next-generation INSIGHT™ PRO software, the instrument is always up to date and ready for the next sample challenge.

Supplier: IMPLEN, INC. CA

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: IMPLEN, INC. CA

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: Quantabio

The qScript™ XLT One-Step RT-PCR Kit is a convenient and highly sensitive system for amplification of RNA templates up to 2 kb

Supplier: IMPLEN, INC. CA

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: Genetex

The basic repeating unit of chromatin is the nucleosome, which is composed of a protein octamer containing two each of the core histones H2A, H2B, H3, and H4, surrounded by approximately 146 base pairs of DNA. Reversible acetylation of highly conserved lysine residues in the N-terminal tail domains of core histones plays an important role in transcriptional regulation, cell cycle progression, and development events. Several histone acetyltransferases (HATs) catalyze this acetylation reaction (e.g. GCN5, PCAF, p300/CBP, TAFII250, P/CAF, SRC-1, BRCA-2). Acetylation of the core histones is generally considered to be associated with gene activation, probably through maintenance of the unfolded structure of transcribing nucleosomes. Histone acetylation is a dynamic process in which levels are determined by the net activities of HATs and the competing enzymes histone deacetylases (HDACs). Both activities are associated with the nuclear matrix. Eleven different mammalian HDACs have been described. HDACs 1-3 & 8 (Class I) are similar to yeast Rpd3 protein, while HDACs 4-7, 9 & 10 (Class II) are similar to yeast Hda1 protein. The activities of the histone deacetylases are often, but not always, associated with transcriptional repression and nucleosome condensation. HDAC1, HDAC2 and several others are the catalytic subunits of different multiprotein regulatory complexes. Other components of such complexes may include: corepressors such as mSin3, N-CoR, SMRT, associated proteins such as SAP18, SAP30, RbAp46, RbAp48, and c-Ski oncogenic protein (involved in DNA methylation). Nucleosome remodeling and deacetylation (NRD) complexes containing HDAC1, HDAC2, Mi-2 (CH3, CH4) dermatomyositis specific autoantigen, and MAT2 (metastasis-associated protein) (related to MAT1) have been described. It is therefore assumed that ATP-dependent nucleosome remodeling activity and histone deacetylation may be interconnected or interdependent. Recruitment of the multiprotein complexes to promoter sites occurs by many sequence specific DNA-binding proteins such as unliganded nuclear hormone receptors, DP1-E2F, YY1, and Rb family of transcription factors, transcriptional repressors, and tumor suppressors (e.g. BRCA1). Aberrant recruitment of HDACs by various oncoproteins may occur in certain neoplastic diseases. It has been found that inhibition ofHDAC2 activity by valporic acid induces proteosomal degradation of HDAC2.

Supplier: Prosci

CD254, also known as RANKL, TNFSF11, TRANCE, OPGL and ODF, is a type II membrane protein of the tumor necrosis factor (TNF) superfamily, and affects the immune system and control bone regeneration and remodeling. RANKL is the ligand of nuclear factor (NF)-κB (RANK). When RANKL binds to RANK, it will undergo trimerization and then bind to an adaptor molecule TNF receptor-associated factor 6 (TRAF6). This results in the activation of several downstream signaling cascades, including the NFκB, mitogen-activated protein kinases (MAPK), activating protein 1 (AP-1), and nuclear factor of activated T cells (NFATc1), resulting in the formation of multinucleated bone-resorbing osteoclasts. RANKL is widely expressed in skeletal muscle, thymus, liver, colon, small intestine, adrenal gland, osteoblast, mammary gland epithelial cells, prostate and pancreas.

Supplier: IMPLEN, INC. CA

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: IMPLEN, INC. CA

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: Prosci

Interleukin-33 (IL-33) is a recently identified member of the IL-1 family of cytokines whose other members include IL-1, IL-1Ra and IL-18 (1,2). Its receptor has been shown to be ST2, an IL-1 receptor family member that also acts as a negative regulator of TLR-IL-1R signaling (1,3) and IL-1R accessory protein (IL-1RAcP) (4). Receptor binding of IL-33 activates NF-B and MAP kinases and induces the expression of TH2-associated cytokines such as IL-4, IL-5 and IL-6. Prolonged IL-33 treatment of mice led to the development of eosinophilia, splenomegaly, and severe pathological changes in mucosal organs such as lungs, esophagus and small intestine (2). Recent experiments have shown that IL-33 can also co-localize with heterochromatin and possesses transcriptional repressor activities, indicating that IL-33 may function as both a proinflammatory cytokine and an intracellular nuclear factor with transcriptional regulatory properties (5).

Supplier: IMPLEN, INC. CA

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: MP Biomedicals

For the extraction and purification of high quality viral DNA and RNA from serum, plasma or cell-free body fluids of 1 to 2 mL using magnetic particle separation technolog and the MPure-12 NA purification system.

Supplier: IMPLEN, INC. CA

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: Genetex

Myosin is the major component of thick muscle filaments, and is a long asymmetric molecule containing a globular head and a long tail. The molecule consists of two heavy chains each ~200,000 daltons, and four light chains each ~16,000 - 21,000 daltons. Activation of smooth and cardiac muscle primarily involves pathways that increase calcium levels and myosin phosphorylation, resulting in contraction. Myosin light chain phosphatase acts to regulate muscle contraction by dephosphorylating activated myosin light chain. This antibody is specific for the phosphorylated form of myosin light chain. The selected peptide sequence used to generate the polyclonal antibody is located near the amino terminal end of the polypeptide corresponding to the smooth/non-muscle form of myosin regulatory light chain found in cardiac myocytes in addition to smooth and non-muscle cells. This sequence differs from that of the sarcomeric/cardiac form of myosin regulatory light chain that has a different sequence around the phosphorylation site. Human and mouse have almost identical sequences. In human the phosphorylation site is pS19, while in mouse the site maps to pS20.

Supplier: MP Biomedicals

MPure Bacterial DNA Extraction Kit is used with the MPure-12 Nucleic Acid Purification System for extraction and purification of genomic DNA from both Gram-positive and Gram-negative bacteria.

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: Genetex

The serum amyloid A (SAA) family comprises a number of differentially expressed lipoproteins, acute-phase SAA1 and SAA2, the former being a major component in plasma, and constitutive SAA's (C-SAAs). Although the liver is the primary site of synthesis of both SAA types, extrhepatic production has been reported. The in-vivo concentrations increase by as much as 1000 fold during inflammation. Several studies have expressed it's importance in the diagnosis and monitoring of various diseases. Pathological SAA values are often detected in association with normal CRP concentrations. SAA rises earlier and more sharply than CRP.SAA enhances the binding of HDL's to macrophages and thus helps the delivery of lipid to sites of injury for use in tissue repair. It is thus thought to be an integral part of the disease process. In addition, recent experiments suggest that SAA may play a "houekeeping" role in normal human tissues.Elevated levels of SAA over time predispose secondary amyloidosis, extracellular accumulation of amyloid fibrils, derived from a circulating precursor, in various tissues and organs. The most common form of amyloidosis occurs secondary to chronic inflammatory disease, particularly rheumatoid artheritis.