26679 Results for: "Ferrozine+mono-sodium+salt+hydrate"

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p53 is a nuclear protein which plays an essential role in the regulation of cell cycle specifically in the transition from G0 to G1. It is found in very low levels in normal cells however in a variety of transformed cell lines in high amounts and believed to contribute to transformation and malignancy. The open reading frame of p53 is 393 amino acids long, with the central region (consisting of amino acids from about 100 to 300) containing the DNA-binding domain. This proteolysis-resistant core is flanked by a C-terminal end mediating oligomerization and an N-terminal end containing a strong transcription activation signal. p53 binds as a tetramer to a PBS (p53-Binding Site) and activates the expression of downstream genes that inhibit growth and/or invasion. p53 binds as a tetramer to a p53-binding site (PBS) and to activate the expression of adjacent genes that inhibit growth and/or invasion. Deletion of one or both p53 alleles reduces the expression of tetramers, resulting in decreased expression of the growth inhibitory genes

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Rb operates in the midst of the cell cycle clock apparatus. Its main role is to act as a signal transducer connecting the cell cycle clock with the transcriptional machinery. It plays an important role in the Rb/ E2F pathway in cell proliferation, cell fate determination, and cancer. Cellular senescence is a stable form of cell cycle arrest that limits proliferation of damaged cells and act as a natural barrier to cancer progression. A distinct heterochromatic structure that accumulates in senescent human fibroblasts, designated as SAHF (Senescence-Associated Heterochromatic Foci). SAHF formation coincides with recruitment of heterochromatin proteins and the Rb protein to E2F-responsive promoters and is associated with the stable repression of E2F target genes. Both SAHF formation and the silencing of E2F target genes depended on the integrity of the Rb pathway and do not occur in reversibly arrested cells. Rb activates transcription of the c-Jun gene through the SP1-binding site within the c-Jun promoter

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Cell Culture Reagent Anhydrous 1 * 100 g

Supplier: LGC Standards PROMOCHEM

5-(Difluoromethoxy)-2-[[(3 ,4-dimethoxypyridin-2-yl)methyl]sulphanyl]-1H-benzimidazole 1 * 100 mg

Supplier: MP Biomedicals

Purity: 99% Anionic detergent used to solubilize proteins prior to electrophoresis. 1 * 25 g

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L-lactate is produced from pyruvate by the enzyme Lacate Dehydrogenase. Lactate production occurs during anaerobic glycolysis or in proliferatively active cells. S 1 * 50 g

Supplier: PanReac AppliChem

SDS, ACS 1 * 5 kg

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SDS, ACS 1 * 250 g

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eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. Interacts with eIF3, mutually exclusive with EIF4A1 or EIFA2, EIF4E and through its N-terminus with PAPBC1. Interacts through its C-terminus with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding these enzymes in place to phosphorylate EIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. EIF4G1/EIF4G3 interacts with PABPC1 to bring about circularization of the mRNA. Rapamycin can attenuate insulin stimulation mediated by FKBPs. Interacts with EIF4E3. Interacts with MIF4GD. Interacts with rotavirus A NSP3; in this interaction, NSP3 takes the place of PABPC1 thereby inducing shutoff of host protein synthesis

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DDR2 (discoidin domain receptor family, member 2) is one of the largest families of proteins in eukaryotes. The family has been classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/ threonine (STK) kinase catalytic domains. Receptor tyrosine kinases (RTKs) play a key role in the communication of cells with their microenvironment. These molecules are involved in the regulation of cell growth, differentiation, and metabolism. In several cases the biochemical mechanism by which RTKs transduce signals across the membrane has been shown to be ligand induced receptor oligomerization and subsequent intracellular phosphorylation. This autophosphorylation leads to phosphorylation of cytosolic targets as well as association with other molecules, which are involved in pleiotropic effects of signal transduction. RTKs have a tripartite structure with extracellular, transmembrane, and cytoplasmic regions. This gene encodes a member of a novel subclass of RTKs and contains a distinct extracellular region encompassing a factor VIII-like domain. Alternative splicing in the 5' UTR results in multiple transcript variants encoding the same protein.

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Calcium-activated and phospholipid-dependent serine/threonine-protein kinase involved in various processes such as regulation of the B-cell receptor (BCR) signalosome, apoptosis and transcription regulation. Plays a key role in B-cell activation and function by regulating BCR-induced NF-κ-B activation and B-cell suvival. Required for recruitment and activation of the IKK kinase to lipid rafts and mediates phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652', leading to activate the NF-κ-B signaling. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. Also involved in triglyceride homeostasis. Serves as the receptor for phorbol esters, a class of tumor promoters.

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SLIT-1 (also known as KIAA0813, MEGF4, multiple epidermal growth factor-like domains 4 and Slit homolog 1 protein) is a Slit protein. This protein is a ligand for the Roundabout (Robo) receptors and acts as guidance cues in axonal migration/navigation during neural development, at the ventral midline of the neural tube. Slit1 and Slit2 are essential for midline guidance in the forebrain by acting as repulsive signals preventing inappropriate midline crossing by axons projecting from the olfactory bulb. Each SLIT gene encodes a putative secreted protein, which contains conserved protein-protein interaction domains including leucine-rich repeats and epidermal growth factor-like motifs, similar to those of the Drosophila protein. In situ hybridization studies indicated that the rat SLIT-1 mRNA was specifically expressed in the neurons of fetal and adult forebrains. This data suggests that the SLIT genes form an evolutionarily conserved group in vertebrates and invertebrates, and that the mammalian SLIT proteins may participate in the formation and maintenance of the nervous and endocrine systems by protein-protein interactions. Alternative splicing isoforms have been identified for Slit1 protein.

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Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3'. In embryonic development is required for notochord formation. Involved in the development of multiple endoderm-derived organ systems such as the liver, pancreas and lungs; FOXA1 and FOXA2 seem to have at least in part redundant roles. Originally discribed as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis; regulates the expression of genes important for glucose sensing in pancreatic beta-cells and glucose homeostasis. Involved in regulation of fat metabolism. Binds to fibrinogen beta promoter and is involved in IL6-induced fibrinogen beta transcriptional activation.

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Principal Names: SnoN; SNO; SKI-like; Ski-related Oncogene; SnoA; SKIL Official Gene Symbol- SKIL Gen Bank Accession Number- NP_005405 Gene ID- 6498(Human) 20482 (mouse)Gene Map Locus- 3q26 (human) SnoN, an 80 kDa protein, is a member of ski family of nuclear proto-oncogenes involved in regulation of cellular transformation and differentiation. Primarily expressed in two isoforms, SnoN is localized in cytoplasm in normal tissues and non-tumorigenic primary epithelial cells. In cancer tissues or cells, SnoN is exclusively localized in the nucleus. It plays a vital role in inhibition of cell cycle arrest induced by TGF-. Upon morphological differentiation or cell-cycle arrest, SnoN translocates into the nucleus, binds to Smad2, Smad3, and Smad4 on TGF- -responsive promoters and represses their ability to activate expression of TGF- target genes. It has also been found to mediate transcriptional repression of thyroid hormone receptor, Mad and pRb. Increased expression of SnoN has been detected in many human tumor cell lines suggesting a clinical significance.

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General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase. /General protein kinase capable of phosphorylating several known proteins. /IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival. Capable of phosphorylating several known proteins. Truncated isoform 2/PKB gamma 1 without the second serine phosphorylation site could still be stimulated but to a lesser extent.

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8-[N-(2-DIPHENYLMETHOXYETHYL)-N,N-DIMETH 1 * 100 mg

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Myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila).Eukaryotic RNA polymerase II mediates the synthesis of mature and functional messenger RNA. This is a multistep process, called the transcription cycle,that includes five stages: preinitiation, promoter, clearance, elongation and termination. Elongation is thought to be a critical stage for the regulation of gene expression. ELL (11-19 lysine-rich leukemia protein, also designated MEN)
functions as an RNA polymerase II elongation factor that increases the rateof transcription by suppressing transient pausing by RNA polymerase II. Also, ELL is thought to regulate cellular proliferation. ELL is abundantly expressed in peripheral blood leukocytes, skeletal muscle, placenta and testis, and has lower expression in spleen, thymus, heart, brain, lung, kidney, liver and ovary.The gene encoding human ELL, which maps to chromosome 19p13.1, is one of several genes which undergo translocation with the MLL gene on chromo-some 11q23 in acute myeloid leukemia. MLL (myeloid/lymphoid leukemia,also designated ALL-1 and HRX) is a 430 kDa protein that regulates embryonal and hematopoietic development.

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General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase. /General protein kinase capable of phosphorylating several known proteins. IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival. Capable of phosphorylating several known proteins. Truncated isoform 2/PKB gamma 1 without the second serine phosphorylation site could still be stimulated but to a lesser extent.

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Chek1 is a protein kinase that inhibits mitotic entry after DNA damage, required for the DNA damage checkpoint and is strongly similar to murine Chek1. Checkpoint pathways control the order and timing of cell cycle transitions and ensure that critical events, such as DNA replication and chromosome segregation, are completed with high fidelity. The mouse and human proteins share 90% sequence identity through the protein kinase domains. The sequence of the 476-amino acid human Chek1 protein is 29%, 40%, and 44% identical to those of the fission yeast Chek1, C. elegans Chek1, and Drosophila 'grapes' (Grp) proteins, respectively. Chek1 is expressed ubiquitously as an approximately 2.4-kb mRNA, with the most abundant expression in thymus, testis, small intestine, and colon. The protein has altered mobility when isolated from cells treated with ionizing radiation, indicating that Chek1 is modified in response to DNA damage. In vitro, Chek1 directly phosphorylates a regulator of CDC2 tyrosine phosphorylation, CDC25C. In response to DNA damage, Chek1 phosphorylates and inhibits CDC25C, thus preventing activation of the CDC2-Cyclin-B complex and mitotic entry

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Histone deacetylase (HDAC) and histone acetyltransferase (HAT) are enzymes that regulate transcription by selectively deacetylating or acetylating the eta-amino groups of lysines located near the amino termini of core histone proteins. Eight members of HDAC family have been identified in the past several years. These HDAC family members are divided into two classes, I and II. Class I of the HDAC family comprises four members, HDAC-1, 2, 3, and 8, each of which contains a deacetylase domain exhibiting from 45 to 93% identity in amino acid sequence. Class II of the HDAC family comprises HDAC-4, 5, 6, and 7, the molecular weights of which are all about twofold larger than those of the class I members, and the deacetylase domains are present within the C-terminal regions, except that HDAC-6 contains two copies of the domain, one within each of the N-terminal and C-terminal regions. Human HDAC-1, 2 and 3 were expressed in various tissues, but the others (HDAC-4, 5, 6, and 7) showed tissue-specific expression patterns. These results suggested that each member of the HDAC family exhibits a different, individual substrate specificity and function in vivo.

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Progesterone receptors (PRs) are nuclear hormone receptors of the NR3C class, which also includes mineralocorticoid, glucocorticoid and androgen receptors. They exist as homodimers coupled to Hsp90 or HMGB proteins, which are shed upon activation. The major signaling pathway used by progesterone receptors is via direct DNA binding and transcriptional regulation of target genes. They can also signal by binding to other proteins, mainly with transcription factors such as NF-κB, AP-1 or STAT. Progesterone receptors are found in the female reproductive tract, mammary glands, brain and pituitary gland and receptor expression is induced by estrogen. Well established functions of progesterone receptors include ovulation, implantation, mammary gland development and maintenance of pregnancy. In addition, progesterone, signaling through the progesterone receptor, increases the ventilatory response of the respiratory centers to carbon dioxide and decreases arterial and alveolar PCO2 in the luteal phase of the menstrual cycle and during pregnancy. The human gene encoding the progesterone receptor has been localized to 11q22.

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rProtein A Sepharose™ 4 Fast Flow is a well established antibody affinity medium is designed for the purification of monoclonal and polyclonal antibodies based on Sepharose™ Fast Flow platform. The recombinant protein A is produced in E.coli and engineered for an oriented coupling to giving a matrix with enhanced binding capacity. The epoxy-based coupling ensures low ligand leakage. The specificity of the recombinant protein A for the Fc region of IgG is similar to native protein A and provides excellent purification in one step. The high capacity, low ligand leakage and a well established base matrix makes rProtein A Sepharose™ Fast Flow ideal for purification of monoclonal antibodies at both laboratory and process scale.

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FANCA (also called Protein FACA or Fanconi anemia group A protein) is involved in DNA repair, perhaps specifically with post-replication repair or a cell cycle checkpoint function. FANCA may also be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. The Fanconi anemia complementation group (FANC) currently includes FANCA, FANCB, FANCC, FANCD1 (also called BRCA2), FANCD2, FANCE, FANCF, FANCG, and FANCL. The previously defined group FANCH is the same as FANCA. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA crosslinking agents, increased chromosomal breakage, and defective DNA repair. The members of the Fanconi anemia complementation group do not share sequence similarity; they are related by their assembly into a common nuclear protein complex. This gene encodes the protein for complementation group A. Alternative splicing results in multiple transcript variants encoding different isoforms. Variant 1 (isoform a) encodes the longest transcript. Variant 2 (isoform b) contains an alternate exon, which results in an early stop codon, compared to variant 1. Isoform b has a shorter C-terminus when compared to isoform a. Mutations in this gene are the most common cause of Fanconi anemia.

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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.

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Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) and involved in initiation of primary immune response. Thought to mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. The receptor returns to the cell membrane surface and the pathogen-derived antigens are presented to resting T-cells via MHC class II proteins to initiate the adaptive immune response. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, cytomegalovirus gB, HCV E2, dengue virus gE, Leishmania pifanoi LPG, Lewis-x antigen in Helicobacter pylori LPS, mannose in Klebsiella pneumonae LPS, di-mannose and tri-mannose in Mycobacterium tuberculosis ManLAM and Lewis-x antigen in Schistosoma mansoni SEA. On DCs it is a high affinity receptor for ICAM2 and ICAM3 by binding to mannose-like carbohydrates. May act as a DC rolling receptor that mediates transendothelial migration of DC presursors from blood to tissues by binding endothelial ICAM2. Seems to regulate DC-induced T-cell proliferation by binding to ICAM3 on T-cells in the immunological synapse formed between DC and T-cells.

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The RNaid® Kit is designed to isolate and purify RNA (75 bases to 10 kb) from native and denaturing agarose and polyacrylamide gels.

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MicroElute® Clean Up system, designed for rapid DNA clean up.

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MabSelect SuRe™ is composed of a rigid, high-flow agarose matrix and alkali-tolerant rProtein A ligand. The ligand has been engineered to provide greater stability than conventional protein A-based media in the alkaline conditions used in CIP protocols. This enhanced alkali stability improves process economy and product quality.

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CLOXACILIN 1 * 200 mg

Supplier: MP Biomedicals

The RNaid® Spin Kit is designed to isolate and purify RNA (75 bases to 10 kb) from native and denaturing agarose and polyacrylamide gels. The kit includes spin filters which prevent silica particle carry-over into cleaned RNA.