15895 Results for: "Sodium+metatungstate+monohydrate"

Supplier: ProSci Inc.

This gene encodes tumor protein p73, which is a member of the p53 family of transcription factors involved in cellular responses to stress and development. The family members include p53, p63, and p73 and have high sequence similarity to one another, which allows p63 and p73 to transactivate p53-responsive genes causing cell cycle arrest and apoptosis. The family members can interact with each other in many ways involving direct or indirect protein interactions, resulting in regulation of the same target gene promoters or regulation of each other's promoters. The p73 protein is expressed at very low levels in normal tissues and is differentially expressed in a number of tumors. The p73 gene expresses at least 35 mRNA variants due to the use of alternate promoters, alternate translation initiation sites, and multiple splice variations. Theoretically this can account for 29 different p73 isoforms; however, the biological validity and the full-length nature of most variants have not been determined.

Supplier: ProSci Inc.

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

Supplier: ProSci Inc.

Lyn (also known as p53/56 Lyn) is a membrane-associated protein tyrosine kinase (PTK) mostly expressed in hemopoietic cells which is important in cellular signaling. It contains an SH2 and SH3 domain and has been found to be cleaved after activation of caspases in apoptosis. A member of the Src family of PTKs, there are two known isoforms for Lyn which plays an indispensable role in the Fc epsilon RI (Fcer1) and the B-cell IgM receptor signaling pathway and is essential for Syk activation and Lat phosphorylation after Fcer1 aggregation and can also phosphor-ylate Tec on multiple residues. Lyn can also be regulated by IL-2 and IL-3.Lyn is a member of the src family of non-receptor protein tyrosine kinases that is predominantly expressed in haematopoietic tissues. Like all members of the src family, lyn is thought to participate in signal transduction from cell surface receptors that lack intrinsic tyrosine kinase activity. It is associated with a number of cell surface receptors including the B cell antigen receptor and immunoglobulin E receptor (FceRI).

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Tyrosine-protein kinase (TYRO3) belongs to the Tyr protein kinase family (AXL/UFO subfamily). The UFO family of receptor tyrosine kinases is comprised of subfamily members Rse(also referred to as Tyro3 or Sky) and UFO (also called Tyro7 or Axl). Two distinct isoforms of Rse, designated Brt and Etk-2, have been described. Brt differs from Rse at its C-terminus, but more importantly lacks the N-terminal 31 amino acid signal peptide sequence present in Rse, which is replaced by a 27 amino acid Brt-specific sequence. It has been suggested that as a result of this alternative splicing event, Brt resides in the cytoplasm, unlike Rse which is expressed on the cell surface. Ekt-2 also lacks an N-terminal signal peptide which is substituted with a 45 amino acid Ekt-2-specific sequence. Protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation.

Supplier: Biosensis

Black-Gold II is a novel haloaurophosphate complex which localises myelin within the central nervous system. The Black Gold II Ready-to-Dilute (RTD) Staining Kit allows you to localise myelin, both individual fibres and tracts, along with the option of co-localising cell bodies via the Toluidine Blue counter stain. Black Gold II labelled myelinated fibres appear nearly black while the Toluidine Blue O labelled cellular Nissl bodies are blue under bright field illumination.

Supplier: ProSci Inc.

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

Supplier: Cytiva

MabSelect SuRe™ LX is a protein A affinity medium with very high dynamic binding capacity at extended residence times and is developed for high titer antibody processes.

Supplier: MP Biomedicals

The protein encoded by FGA gene is the alpha component of fibrinogen, a blood-borne glycoprotein comprised of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia, afibrinogenemia and renal amyloidosis. Alternative splicing results in two isoforms which vary in the carboxy-terminus.

The total protein is measured using the Biuret procedure with bovine albumin as the standard. To ensure that the product titer falls within the required range, antibody titer is standardized by microtiter plate ELISA with human fibrinogen. The product is tested for purity and specificity at final concentration by immunoelectrophoresis. The antibody is predominantly goat IgG; no trace of albumin is detected.

Supplier: ProSci Inc.

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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Gli-2 (also known as Zinc Finger Protein Gli-2, GLI-Kruppel family member GLI-2 or Tax helper protein) belongs to the C2H2-type zinc finger protein subclass of the Gli family. Members of this subclass are characterized as transcription factors that bind DNA through zinc finger motifs. These motifs contain conserved H-C links. Gli family zinc finger proteins are mediators of Sonic hedgehog (Shh) signaling, and they are implicated as potent oncogenes in the embryonal carcinoma cell. The protein encoded by this gene localizes to the cytoplasm and activates patched Drosophila homolog (PTCH) gene expression. Gli-2 is also thought to play a role during embryogenesis. The encoded protein is associated with several phenotypes: Greig cephalopolysyndactyly syndrome, Pallister-Hall syndrome, pre-axial polydactyly type IV, post-axial polydactyly types A1 and B. Expression has been reported for this mRNA in human testis, myometrium, kidney, lung, glioblastomas, and embryonal cell carcinomas. Multiple splice variants have been reported for this protein.

Supplier: ProSci Inc.

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

Supplier: ProSci Inc.

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

Supplier: ProSci Inc.

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

Supplier: ProSci Inc.

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

Supplier: MACHEREY-NAGEL

The high purity CHROMABOND® adsorbents can be used for a self-filling of SPE columns or further analytical applications.

Supplier: ProSci Inc.

Myeloid leukemia factor-1 (MLF1) Interacting Protein (also known as PBIP1, MLF1IP1, KLIP1 or KSHV latent nuclear antigen interacting protein 1) is a novel polo-like kinase 1 (Plk1) substrate. Plk1 phosphorylation of MLF1IP induces ubiquitination and degradation of MLF1IP prior to the metaphase/anaphase transition. Several Plk1-dependent phosphorylation sites have been identified on MLF1IP by mass spectrometry. Mutations of these sites stabilize MLF1IP and inhibit mitotic progression. Subsequent in vitro and in vivo MLF1IP phosphorylation and stability assays have revealed that phosphorylation of Thr78 is critical for triggering Plk1-dependent MLF1IP degradation. Expression of a non-degradable Thr78Ala mutant was sufficient to induce a mitotic block. Timely phosphorylation of MLF1IP on Thr78 by Plk1 is critical for eliminating the MLF1IP-imposed mitotic block prior to anaphase onset. MLF1IP is speculated to be a novel tumor suppressor, whose function is required for proper sister-chromatid separation. Loss of MLF1IP function may result in improper segregation of chromosomes and genomic instability, thus promoting tumorigenesis.

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Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger.

Supplier: ProSci Inc.

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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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

Supplier: ProSci Inc.

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.

Supplier: MP Biomedicals

Crystalline Purity: 99.5% 1 * 3 kg

Supplier: MP Biomedicals

Potency:~900 µ g/mg Crystalline Topoisomerase II inhibitor 1 * 5 g

Supplier: MP Biomedicals

Purity: >98% 1 * 1 kg

Supplier: MP Biomedicals

Cell Culture Reagent Anhydrous 1 * 500 g

Supplier: G-Biosciences

L-lactate is produced from pyruvate by the enzyme Lacate Dehydrogenase. Lactate production occurs during anaerobic glycolysis or in proliferatively active cells. S 1 * 10 g

Supplier: MP Biomedicals

Photoinitiator of polymerization useful in either acid or alkaline buffer systems. 1 * 5 g

Supplier: G-Biosciences

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: G-Biosciences

Carbonyl groups, including aldehydes, ketones and glyoxals, react with amines to form Schiff base intermediates that are in equilibr ium with their free forms. The labile Schiff’s base interaction can be stabilized by chemical reduction. 1 * 2.000 mg