1082 Results for: "Test Lead"

Supplier: American Compliance Systems

Courses from The Interactive CD-ROM Training Library™ provide safety, health, and regulatory compliance training using a combination of audio, full-motion video, text, and colorful graphics.

Supplier: Genetex

Enzymes of the cAMP-dependent phosphodiesterase type 4 (PDE4) family are important in hydrolyzing cAMP produced by G-protein coupled receptor (GPCR) stimulated adenylyl cyclases. In brain, more than 90% of cAMP formed by the stimulation of GPCRs is hydrolyzed by PDE4 enzymes. PDE4 enzymes are also important molecular targets for a variety of therapeutic agents like antidepressants, anti-asthmatics, and anti-inflammatory drugs. PDE4 family comprises 4 genes (PDE4A, B, C and D); each exhibiting multiple isozymes due to alternate splicing that leads to a larger number of distinct PDE4 variants. Members of the PDE4 family are regulated/activated by phosphorylation/dephosphorylation by cAMP-dependent protein kinase A and phosphatases. Protein-protein interactions and cellular trafficking of PDE4A enzymes play an important role in cAMP compartmentalization and cAMP-dependent signaling. In brain members of the PDE4A, B and D family are associated with GPCRs (adrenergic and dopaminergic) signaling.

Supplier: Prosci

Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, the microtubule-associated protein MAPT, RHOH or TYROBP.

Supplier: Prosci

GPVI Antibody: Glycoprotein VI (GP6) is a 58kD platelet membrane glycoprotein that plays a crucial role in the collagen-induced activation and aggregation of platelets. It is uniquely expressed by cells of the megakaryocytic/platelet lineage, and is a member of the immunoglobulin gene superfamily, closely related to Fc receptor gamma chain (FcRgamma) and natural killer receptors. Glycoprotein VI plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcRgamma, the Src kinases (likely Fyn/Lyn), the adapter protein LAT and leads to the activation of phospholipase C gamma2. GPVI deficiency can result in bleeding disorders. Further study should reveal the extent of GPVI involvement in thrombotic disease and allow the development of alternative anti-thrombotic compounds.

Supplier: Prosci

GPVI Antibody: Glycoprotein VI (GP6) is a 58kD platelet membrane glycoprotein that plays a crucial role in the collagen-induced activation and aggregation of platelets. It is uniquely expressed by cells of the megakaryocytic/platelet lineage, and is a member of the immunoglobulin gene superfamily, closely related to Fc receptor gamma chain (FcRgamma) and natural killer receptors. Glycoprotein VI plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcRgamma, the Src kinases (likely Fyn/Lyn), the adapter protein LAT and leads to the activation of phospholipase C gamma2. GPVI deficiency can result in bleeding disorders. Further study should reveal the extent of GPVI involvement in thrombotic disease and allow the development of alternative anti-thrombotic compounds.

Supplier: Prosci

APP Antibody: Accumulation of the amyloid-beta peptide (Abeta) in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. The beta-amyloid protein precursor (APP) is cleaved by one of two beta-secretases (BACE and BACE2), producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for gamma-secretase to generate the 4 kDa amyloid-beta peptide (Abeta), which is deposited in the Alzheimer's disease patient's brains. Recently, Death Receptor 6 (DR6) was found to interact with an amino-terminal fragment of the beta-amyloid protein (N-APP) in neurons, activating a caspase 6-dependent apoptotic event leading to axonal degeneration and pruning during development, suggesting that these two proteins are involved in neural development and may possibly play a role in Alzheimer's disease.

Supplier: Tonbo Biosciences

The 53-6.7 antibody reacts with the 32-34 kDa alpha subunit of mouse CD8, known as CD8a or CD8 alpha. CD8a can form a homodimer (CD8 alpha-alpha), but is more commonly expressed as a heterodimer with a second chain known as CD8b or CD8 beta. CD8 acts as a co-receptor in antigen recognition and subsequent T cell activation that is initiated upon binding of the T cell receptor (TCR) to antigen-bearing MHC Class I molecules. The cytoplasmic domains of CD8 provide binding sites for the tyrosine kinase lck, facilitating intracellular signaling events that lead to T cell activation, development, and cytotoxic effector functions. CD8+ cytotoxic T cells (CTLs) play an important role in inducing cell death of tumor cells, as well as cells infected by virus, bacteria or parasites.

Supplier: Prosci

Signal transducer and activator of transcription that mediates signaling by interferons (IFNs). Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state.

Supplier: Tonbo Biosciences

The 53-6.7 antibody reacts with the 32-34 kDa alpha subunit of mouse CD8, known as CD8a or CD8 alpha. CD8a can form a homodimer (CD8 alpha-alpha), but is more commonly expressed as a heterodimer with a second chain known as CD8b or CD8 beta. CD8 acts as a co-receptor in antigen recognition and subsequent T cell activation that is initiated upon binding of the T cell receptor (TCR) to antigen-bearing MHC Class I molecules. The cytoplasmic domains of CD8 provide binding sites for the tyrosine kinase lck, facilitating intracellular signaling events that lead to T cell activation, development, and cytotoxic effector functions. CD8+ cytotoxic T cells (CTLs) play an important role in inducing cell death of tumor cells, as well as cells infected by virus, bacteria or parasites.

Supplier: Prosci

Acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let-7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre-let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre-let-7 in embryonic stem (ES) cells contributes to the maintenance of ES cells.

Supplier: MOUSER ELECTRONICS MS

TEST LEADS MALE BLACK 3.9IN 10CM 2MM/4MM

Supplier: Prosci

Signal transducer and activator of transcription that mediates signaling by interferons (IFNs). Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state.

Supplier: Genetex

The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane-type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimers, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.

Supplier: Prosci

L13 inhibits proinflammatory cytokine production and stimulates antibody production. It induces proliferation in the human pre myeloid cell line TF1. IL13 has multiple effects on the differentiation and functions of monocytes and macrophages. It suppresses cytotoxic functions and induces changes in the morphology of human monocytes and in the phenotype of human monocytes and B cells by upregulating MHC class II expression. IL13 will also decrease the production of nitric oxide by activated murine macrophages, leading to impaired parasiticidal activity. Human and mouse interleukin 13 share approximately 58% amino acid sequence identity. Although human and mouse IL13 are equally active on human cells, human IL13 is much less active than mouse IL13 on mouse cells. Human IL13 and human IL4 also share approximately 30% sequence homology and have similar biological functions.

Supplier: Prosci

GOLPH1 Antibody: GOLPH1, also known as GCP60, was initially identified as a Golgi protein that can interact with the integral membrane protein giantin and is thought to be involved in the maintenance of the Golgi structure. GOLPH1 has also been shown to interact with other Golgi proteins such as Golgin-160, a Golgi protein that can be cleaved by caspases-2, -3, and -7, leading to the nuclear localization of Golgin-160. GOLPH1 interaction with the Golgin-160 fragments is stronger than that with the intact Golgin-160, with its interaction regulated by the oxidation state of Cys-463 within GOLPH1, suggesting that the nuclear localization of the caspase-cleaved Golgin-160 fragments is a highly coordinated event. GOLPH1 has also been found to interact with Numb, a cytosolic signaling protein that mediates asymetric cell division of neural progenitor cells to a daughter progenitor cell and a neuron, suggesting that Golgi fragmentation and reconstitution during the cell cycle differentially regulate Numb signaling through changes in GOLPH1 subcellular distribution and may couple cell fate with cell cycle progression.

Supplier: Prosci

Vimentin is the major subunit protein of the intermediate filaments of mesenchymal cells. It is believed to be involved with the intracellular transport of proteins between the nucleus and plasma membrane. Vimentin has been implicated to be involved in the rate of steroid synthesis via its role as a storage network for steroidogenic cholesterol containing lipid droplets. Vimentin phosphorylation by a protein kinase causes the breakdown of intermediate filaments and activation of an ATP and myosin light chain dependent contractile event. This results in cytoskeletal changes that facilitate the interaction of the lipid droplets within mitochondria, and subsequent transport of cholesterol to the organelles leading to an increase in steroid synthesis. Immunohistochemical staining for Vimentin is characteristic of sarcomas (of neural, muscle and fibroblast origin) compared to carcinomas which are generally negative. Melanomas, lymphomas and vascular tumors may all stain for Vimentin. Vimentin antibodies are thus of value in the differential diagnosis of undifferentiated neoplasms and malignant tumors. They are generally used with a panel of other antibodies including those recognising cytokeratins, lymphoid markers, S100, desmin and neurofilaments.

Supplier: Genetex

Lens proteins consist almost entirely of Crystallins (about 95%). Crystallins are also found in vertebrate skeletal muscle tissue. In the lens, their structural function is to assist in maintaining the proper refractive index of the lens. The mammalian lens contains 3 major classes of crystallins: alpha, beta, and gamma. Alpha Crystallin is the largest of the crystallins and is composed of 2 primary gene products; alpha A and alpha B. There are at least 5 different proteins comprising the beta Crystallins. The gamma Crystallins are monomeric, but there are at least 5 gamma Crystallins identified in bovine and rat lens. Alpha Crystallin comprises 40% of total lens protein composition. In addition to maintaining proper refractive index, it also functions in a chaperone like manner by preventing the formation of aggregates possibly leading to cataract formation. It is believed that the phosphorylated states of the alpha Crystallin occur in response to cellular stress and may serve a structural control function and play a role in protein maintenance. Alpha B Crystallin has been linked to Alexander's disease where it accumulates in brain cells of those afflicted.

Supplier: Prosci

L13 inhibits proinflammatory cytokine production and stimulates antibody production. It induces proliferation in the human pre myeloid cell line TF1. IL13 has multiple effects on the differentiation and functions of monocytes and macrophages. It suppresses cytotoxic functions and induces changes in the morphology of human monocytes and in the phenotype of human monocytes and B cells by upregulating MHC class II expression. IL13 will also decrease the production of nitric oxide by activated murine macrophages, leading to impaired parasiticidal activity. Human and mouse interleukin 13 share approximately 58% amino acid sequence identity. Although human and mouse IL13 are equally active on human cells, human IL13 is much less active than mouse IL13 on mouse cells. Human IL13 and human IL4 also share approximately 30% sequence homology and have similar biological functions.

Supplier: Genetex

Brutons tyrosine kinase (Btk) is a member of the Btk/Tec family of cytoplasmic tyrosine kinases. Like other Btk family members, it contains a pleckstrin homology (PH) domain, Src homology SH3 and SH2 domains. Btk plays an important role in B cell development. Activation of B cells by various ligands is accompanied by Btk membrane translocation mediated by its PH domain binding to phosphatidylinositol-3,4,5-trisphosphate. The membrane-located Btk is active and associated with transient phosphorylation of two tyrosine residues, Tyr551 and Tyr223. Tyr551 in the activation loop is transphosphorylated by the Src family tyrosine kinase, leading to autophosphorylation at Tyr223 within the SH3 domain, which is necessary for full activation. The activation of Btk is negatively regulated by PKCbeta through phosphorylation of Btk at Ser180, which results in reduced membrane recruitment, transphosphorylation and subsequent activation. The PKC/Btk inhibitory signal is likely to be a key determinant of the B-cell receptor signaling threshold to maintain optimal Btk activity.

Supplier: Genetex

Vimentin is the major subunit protein of the intermediate filaments of mesenchymal cells. It is believed to be involved with the intracellular transport of proteins between the nucleus and plasma membrane. Vimentin has been implicated to be involved in the rate of steroid synthesis via its role as a storage network for steroidogenic cholesterol containing lipid droplets. Vimentin phosphorylation by a protein kinase causes the breakdown of intermediate filaments and activation of an ATP and myosin light chain dependent contractile event. This results in cytoskeletal changes that facilitate the interaction of the lipid droplets within mitochondria, and subsequent transport of cholesterol to the organelles leading to an increase in steroid synthesis. Immunohistochemical staining for Vimentin is characteristic of sarcomas (of neural, muscle and fibroblast origin) compared to carcinomas which are generally negative. Melanomas, lymphomas and vascular tumors may all stain for Vimentin. Vimentin antibodies are thus of value in the differential diagnosis of malignant tumors, generally used with a panel of other antibodies including those recognising cytokeratins, lymphoid markers, S100, desmin and neurofilaments.

Supplier: Adipogen

IL-36alpha (IL-1F6), IL-36beta (IL-1F8) and IL-36gamma (IL-1F9) bind to IL-36R (IL-1Rrp2) and IL-1RAcP, activating similar intracellular signals as IL-1 and are inhibited by IL-36Ra. The expression of IL-36 cytokines has been shown to occur at different sites including the lung and skin and can be derived from diverse cell types including keratinocytes, bronchial epithelium as well as macrophages, monocytes and different T cell subsets. IL-36 family members induce the production of proinflammatory cytokines, including IL-12, IL-1beta, IL-6, TNF-alpha and IL-23 in BMDC and CD4 T cells. Skin and dendritic cells are targets of the IL-36 interleukins leading to a Th1 response. These cytokines may represent potential targets for immune-mediated inflammatory conditions or, alternatively, could be used as adjuvants in vaccination. Recently a novel role for IL-36alpha in the pathogenesis of intestinal inflammation has been reported.

Supplier: Genetex

The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zinc-endopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. In addition, fibronectin-like repeats, a hinge region, and a C-terminal hemopexin-like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane-type MMP subfamilies. MMPs contain the motif His-Glu-X-X-His (X represents any amino acid) that binds zinc in the catalytic site, as well as another zinc molecule and two calcium molecules structurally. They fall within the matrixin subfamily and are EC designated 3.4.24.x. This group also contains astacin, reprolysin, and serralysin, as well as other more divergent metalloproteinases. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown.

Supplier: Bel-Art Products, a Part of SP

Thermometers contain black, non-toxic, biodegradable, EnviroKleen™ certified, Enviro-Safe® liquid against lead-free, yellow back glass for easy readability and fewer reading errors.

Supplier: Adipogen

BAFF is mainly produced by innate immune cells such as neutrophils, monocytes, macrophages, dendritic cells, follicular dendritic cells. T cells, activated B cells, some malignant B cells and also non-lymphoid cells like astrocytes, synoviocytes and epithelial cells can also produce BAFF. BAFF binds three distinct receptors (BAFF-R, TACI and BCMA) expressed predominantly on B cells, although activated T cells also express BAFF-R. BAFF is a master regulator of peripheral B cell survival, and together with IL-6, promotes Ig class-switching and plasma cell differentiation. Besides its major role in B cell biology, BAFF co-stimulates activated T cells. Deregulated expression of BAFF leads to autoimmune disorders in mice. In humans, elevated levels of soluble BAFF have been detected in the serum of patients with various autoimmune diseases such as Sjoegren syndrome, Rheumatoid arthritis (RA), Multiple sclerosis (MS) and Systemic Lupus Erythematosus (SLE). BAFF has also increased levels in some lymphoid cancers.

Supplier: Prosci

Tumor necrosis factor receptor superfamily, member 6 isoform 1; apoptosis antigen 1; Fas antigen; APO-1 cell surface antigen. This protein is a member of the TNF-receptor superfamily. This receptor contains a death domain. It has been shown to play a central role in the physiological regulation of programmed cell death, and has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The interaction of this receptor with its ligand allows the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10. The autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, and leads to apoptosis. This receptor has been also shown to activate NF-κB, MAPK3/ERK1, and MAPK8/JNK, and is found to be involved in transducing the proliferating signals in normal diploid fibroblast and T cells. At least eight alternatively spliced transcript variants encoding seven distinct isoforms have been described. The isoforms lacking the transmembrane domain may negatively regulate the apoptosis mediated by the full length isoform. ** Cat.N

Supplier: Bel-Art Products, a Part of SP

These calibrated thermometers are EnviroKleen™ certified and feature green, non-toxic, biodegradable, Enviro-Safe® liquid against lead-free, white back glass.

Supplier: Bel-Art Products, a Part of SP

EnviroKleen™ certified thermometers feature black, non-toxic, biodegradable, Enviro-Safe® liquid against lead-free, yellow back glass for easy readability and fewer reading errors.

Supplier: NEWARK IN ONE MS

SET TEST LEAD TIP PROBE 4MM 1KV 3A 2LEAD

Supplier: Genetex

Structural Maintenance of Chromosomes (SMC) family proteins play critical roles in various nuclear events that require structural changes of chromosomes, including mitotic chromosome organization, DNA recombination and repair and global transcriptional repression. The chromosome proteins are conserved in eukaryotes lead to mitotic chromosome segregation defects, suggesting a critical function of SMC family proteins in mitotic chromosome dynamics. SMC1 and SMC3 form a heterodimeric complex required for metaphase progression in mitotic cells. Specifically this SMC1/SMC3 complex is responsible for sister chromatid cohesion during metaphase. A number of cellular factors interact with hSMC1/hSMC3 during cell cycle. The major population of hSMC1/hSMC3 is in a compex with hRAD21 forming the human cohesion complex. Human cohesion associates with chromosomes which peaks at S phase and dissociates from chromosomes during G2/M transition. In addition, a subpopulation of hSMC1/hSMC3 associates tightly with nuclear matrix and centrosomes during interphase. A subset of hSMC1/hSMC3 is localized to spindle poles, spindles and kinetochores during mitosis when cohesin is in the cytoplasm. hSMC1/hSMC3 is required for spindle aster formation in vitro and reacts with nuclear mitotic apparatus protein in vivo.

Supplier: Genetex

Polo-like kinases are a family of serine/threonine protein kinases, named after the prototypic founding member of the family, the polo gene product of Drosophila melanogaster. The polo kinase was originally identified in mutants that display abnormal mitotic spindle organization. Subsequently, potential homologues of Drosophila polo have been identified in yeasts (Cdc5p in Saccharomyces cerevisiae; plo1+ in Schizosaccharmoyces pombe) and in mammals (polo-like kinase 1; Plk1). Genetic and biochemical studies suggest that polo, Cdc5p and plo1+ may be required for mitotic spindle organization and, possibly, for cytokinesis. Likewise, the patterns of expression, activity and subcellular localization of Plk1 suggest that Plk12 may function during mitosis in spindle assembly and function. Recent studies have demonstrated that mammalian Plks regulate the function of the Golgi complex, a cellular organelle closely associated with the centrosome and also have microtubule organization activity. Furthermore, deregulated expression of human PLK1 and PLK3 is strongly correlated with the development of many types of malignancies, and ectopic expression of kinase-active Plk3 or Plk1 dominant negative protein leads to rapid cell death.