1082 Results for: "Test Lead"

Supplier: Prosci

MFNG is one of the evolutionarily conserved secreted proteins that act in the Notch receptor pathway to demarcate boundaries during embryonic development. Western blots using two different antibodies against two unique regions of this protein target confirm the same apparent molecular weight in our tests.This gene is a member of the fringe gene family which also includes Radical and Lunatic fringe. They all encode evolutionarily conserved secreted proteins that act in the Notch receptor pathway to demarcate boundaries during embryonic development. While their genomic structure is distinct from other glycosyltransferases, fringe proteins have a fucose-specific beta1,3 N-acetylglucosaminyltransferase activity that leads to elongation of O-linked fucose residues on Notch, which alters Notch signaling. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Prosci

RNAse H2A Antibody: Ribonucleases (RNAses) H are enzymes that hydrolyze the RNA strands of RNA/DNA hybrids. The major role of these enzymes is to remove the RNA strand from the RNA/DNA hybrids that form during DNA replication and repair. RNAse H2 is made up of three subunits; all three are required for RNAse activity. Recent evidence has demonstrated that mutations in RNAse H2A or any of the other subunits result in Aicardi-Goutieres syndrome (AGS), a neurological disorder with similar symptoms to viral brain infections including high levels of IFN-alpha in the cerebral spinal fluid. Similar conditions are observed with mutations in TREX1, a single-stranded DNA exonuclease, suggesting that RNAse H2 and TREX1 may have similar roles, and that mutations in any of these genes lead to an accumulation of intracellular nucleic acids, triggering an inflammatory response through activation of the innate immune system.

Supplier: Prosci

ALKBH2 Antibody: The E. coli AlkB protein protects against the cytotoxicity of methylating agents by repair of the specific DNA lesions generated in single-stranded DNA; ALKBH2 and ALKBH3 are mammalian homologs of AlkB that catalyze the removal of 1-methyladenine and 3-methylcytosine, modifications that left unchecked could lead to cancerous cells. Mutations in both ALKBH2 and ALKBH3 have been observed in pediatric brain tumors indicating that these proteins are important in the prevention of cancer formation. Like the histone demethylase JMJD1A, ALKBH2 is a non-heme iron enzyme that is inhibited by Nickel ions, suggesting that inhibition of ALKBH2 by Nickel ions may play a role in the development of cancer. Conversely, ALKBH2 mRNA and protein levels are increased glioma cells following Photofrin-mediated photodynamic therapy, an adjuvant therapy in cancer treatment, suggesting that down-regulating ALKBH2 expression in cancer cells may enhance the anti-cancer effectiveness of this treatment.

Supplier: Prosci

Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is a member of the hnRNP A/B family of related RNA binding proteins that bind pre-mRNA and are involved in the processing, metabolism and transport of nuclear pre-mRNA transcripts. hnRNP A1 regulates the alternative splicing of c-Src, c-H-Ras and modifies initiation of translation of the fibroblast growth factor 2 mRNA. hnRNP A1 expression level is elevated in many cancers; knockdown of hnRNP A1 leads to apoptosis in various cancer cells. Although predominantly nuclear, hnRNP A1 is continually transported from the nucleus to the cytoplasm where it disassociates from mRNA and is rapidly re-imported into the nucleus. hnRNP A1 binds to cis-acting repressive sequences (CRS) of HIV-1 to influence HIV-1 production. HIV-1 enhances hnRNP A1 expression and promotes the relocalization of hnRNP A1 to the cytoplasm ,

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: Prosci

CD85 antigen-like family member J (CD85J) is also known as Leukocyte immunoglobulin-like receptor subfamily B member 1 (LILRB1 or LIR-1), Immunoglobulin-like transcript 2 (ILT-2), Monocyte/macrophage immunoglobulin-like receptor 7 (MIR7), which belongs to leukocyte immunoglobulin-like receptor (LIR) family. CD85J / LILRB1 Contains 4 Ig-like C2-type (immunoglobulin-like) domains. CD85J / LIR-1 is expressed predominantly on B-cells and monocytes. CD85J is receptor for class I MHC antigens and recognizes a broad spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles and is also receptor for H301/UL18, a human cytomegalovirus class I MHC homolog. Ligand binding results in inhibitory signals and down-regulation of the immune response. CD85J / LILRB1 interaction with HLA-B or HLA-E leads to inhibition of the signal triggered by FCER1A and inhibits serotonin release. CD85J / LILRB1 inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions.

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

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: MOUSER ELECTRONICS MS

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

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: 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: 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: 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: 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: 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

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: 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

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: 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

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

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: 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

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

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: Prosci

In response to DNA damage and replication blocks, cell cycle progression is halted through the control of critical cell cycle regulators. The protein encoded by Chk2 gene is a cell cycle checkpoint regulator and putative tumor suppressor. It contains a forkhead-associated protein interaction domain essential for activation in response to DNA damage and is rapidly phosphorylated in response to replication blocks and DNA damage. When activated, the encoded protein is known to inhibit CDC25C phosphatase, preventing entry into mitosis, and has been shown to stabilize the tumor suppressor protein p53, leading to cell cycle arrest in G1. In addition, this protein interacts with and phosphorylates BRCA1, allowing BRCA1 to restore survival after DNA damage. Mutations in this gene have been linked with Li-Fraumeni syndrome, a highly penetrant familial cancer phenotype usually associated with inherited mutations in TP53. Also, mutations in this gene are thought to confer a predisposition to sarcomas, breast cancer, and brain tumors. This nuclear protein is a member of the CDS1 subfamily of serine/threonine protein kinases. Three transcript variants encoding different isoforms have been found for this gene.

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

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: 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.