128771 Results for: "Isothiocyanate+de+m-tolyle"

Supplier: Bioss

Hypermethylated in cancer (HIC-1) was originally identified as a target of p53-induced gene expression. HIC-1 is deleted in the genetic disorder Miller-Dieker syndrome (MDS), and the expression of HIC-1 is also frequently suppressed in leukemia and various cancers due to the hypermethylation of specific DNA regions and the resulting transcriptional silencing. These and other studies indicate that HIC-1 acts as a putative tumor suppressor protein that mediates transcriptional repression. HIC-1 is ubiquitously expressed in adult tissues and its structure is defined by five Zinc fingers and an N-terminal broad complex POZ (or BTB) domain. In several BTB/POZ containing proteins, including BCL-6 and the promyelocytic leukemia Zinc-finger (PLZF) oncoprotein, this domain interacts with the SMRT/N-CoR-mSin3A HDAC complex and is directly involved in repressing and silencing gene transcription. When this domain is deleted, as with the oncogenic PLZF-RAR chimera of promyelocytic leukemias, this transcriptional repression is attenuated. Conversely, HIC-1 does not interact with components of the HDAC complex, suggesting that HIC-1-induced transcriptional repression is unassociated with the POZ/BTB domain.

Supplier: Bioss

Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of Zinc-finger proteins contain a Kr_ppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. HIC-2 (hypermethylated in cancer 2) possesses Zinc finger motifs that are thought to be important for DNA-binding and also has a BTB/POZ domain at the N-terminus, which is thought to be important for protein-protein binding, as well as for the binding of transcription factors. HIC-2 is also known as Hic-3, HIC1-related gene on chromosome 22 or Zinc finger and BTB domain-containing protein 30, and is a 615 amino acid protein that is expressed as two isoforms produced by alternative splicing. HIC-2 is highly expressed in cerebellum and is localised to the nucleus in cells. HIC-2 contains a short amino acid sequence that is thought to interact with CtBP, a transcriptional repressor. The gene sequence associated with HIC-2 is thought to be a target for miRNAs (microRNAs) which are expressed in many cancers, suggesting that HIC-2 could possess tumor suppressor capabilities.

Supplier: Tonbo Biosciences

The incorporation of BrdU into newly synthesized DNA by actively cycling cells is one method for measuring the changing amount of cellular DNA during cell proliferation through each of the cell cycle phases. As a thymidine analog, BrdU is preferentially incorporated into newly replicated DNA which can then be subsequently labeled and analyzed to determine relative DNA content and cell cycle position. Incorporation of BrdU is most commonly detected using anti-BrdU antibodies. A BrdU solution is provided for exposure of actively cycling cells to incorporate BrdU. The EZ-BrdU Kit employs an acid denaturation step. The mild acid method used helps reduce damage to other cellular proteins. After the denaturation step, cells are stained with a FITC anti-BrdU antibody and total DNA is counterstained with a PI/RNase A solution. Two color flow cytometry can then be used to analyze cells that have incorporated BrdU (proliferating cells) in terms of their cell cycle position (G0/1, S, or G2/M phase). The EZ-BrdU Kit is shipped in one container and consists of two packages. Upon arrival one should be stored at 2-8°C and the other at -20°C.

Supplier: Bioss

Transmembrane adapter protein which associates with KLRK1 to form an activation receptor KLRK1-HCST in lymphoid and myeloid cells; this receptor plays a major role in triggering cytotoxicity against target cells expressing cell surface ligands such as MHC class I chain-related MICA and MICB, and UL16-binding proteins (ULBPs); these ligands are up-regulated by stress conditions and pathological state such as viral infection and tumor transformation. Functions as docking site for PI3-kinase PIK3R1 and GRB2. Interaction of ULBPs with KLRK1-HCST triggers calcium mobilisation and activation of the PIK3R1, MAP2K/ERK, and JAK2/STAT5 signaling pathways. Both PIK3R1 and GRB2 are required for full KLRK1-HCST-mediated activation and ultimate killing of target cells. In NK cells, KLRK1-HCST signaling directly induces cytotoxicity and enhances cytokine production initiated via DAP12/TYROBP-associated receptors. In T-cells, it provides primarily costimulation for TCR-induced signals. KLRK1-HCST receptor plays a role in immune surveillance against tumors and is required for cytolysis of tumors cells; indeed, melanoma cells that do not express KLRK1 ligands escape from immune surveillance mediated by NK cells.

Supplier: Tonbo Biosciences

The FITC Mouse Lineage Cocktail contains a combination of pre-diluted antibodies that identify lineage committed cells by flow cytometry and facilitate their exclusion from hematopoietic progenitor cells in mouse bone marrow. The antibodies in the cocktail react with cells from major hematopoietic lineages including T, B and NK cells, monocytes/macrophages, granulocytes and erythrocytes. The Lineage Cocktail contains the following FITC conjugated antibodies: anti-mouse CD3 (17A2), anti-mouse CD11b (M1/70), anti-mouse CD45/B220 (RA3-6B2), anti-mouse Ly-6G (Gr-1) (RB6-8C5) and anti-mouse TER-119 (TER-119). An Isotype Control Cocktail consisting of FITC conjugated isotype-matched control antibodies (Rat IgG2a, kappa; Rat IgG2b, kappa) is also provided in a separate vial.

Supplier: Bioss

Atypical chemokine receptor that controls chemokine levels and localisation via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalising receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalisation and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.

Supplier: Abcam

A sandwich ELISA kit for the quantitative measurement of NOS2 in biological fluids.

Supplier: Abcam

A sandwich ELISA kit for the quantitative measurement of NOS2 in biological fluids.

Supplier: Tonbo Biosciences

The fragmentation of genomic DNA by cellular nucleases during the later stages of apoptosis is also one of the most easily measured features of apoptotic cells. Nuclease activity generates DNA fragments ranging from ~300 bp to 50 bp in length, resulting in a typical DNA ‘laddering’ appearance when analyzed by agarose gel electrophoresis. These fragments have exposed 3’-hydroxyl (OH) ends which can be labeled with bromolated deoxyuridine triphosphates (Br-dUTP). An enzyme, terminal deoxynucleotidyl transferase (TdT), is used to catalyze the template-independent addition of Br-dUTP to the 3’-OH ends of double or single stranded DNA. This method is often called TUNEL (terminal deoxynucleotidyl transferase dUTP nick end labeling) or end labeling. Sites where the Br-dUTP is incorporated can then be detected with an antibody specific to BrdU. With the APO-BrdUTM Kit cells are first labeled with Br-dUTP, and then sites of incorporation are detected through staining with a FITC anti-BrdU antibody. Samples can then be analyzed via flow cytometry. Samples that are apoptotic will stain brightly with the anti-BrdU antibody due to the substantial number of exposed 3’-OH sites, while cells that are non-apoptotic will not have incorporated significant amounts of Br-dUTP and will stain dimly. The APO-BrdU Kit is shipped in one container and consists of two packages. Upon arrival one should be stored at 2-8°C and the other at -20°C.

Supplier: Bioss

Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Zince lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30 to 40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.

Supplier: Bioss

Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilise XPC. May protect XPC from proteasomal degradation. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognises a wide spectrum of damaged DNA characterised by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognise and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.