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Ace+Method+Development+Kits
Fournisseur:
Thermo Scientific
Description:
Chrome (III)-potassium sulfate dodécahydraté 98.0-102.0% ACS
Numéro de catalogue:
(BOSSBS-4100R-A750)
Fournisseur:
Bioss
Description:
Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage. Required for normal brain development, including that of cerebellum. Facilitates developmentally regulated apoptosis during neural tube formation. Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues. Also required for mitochondrial fission during mitosis. Required for formation of endocytic vesicles. Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles. Required for programmed necrosis execution. Isoform 1 and isoform 4 inhibit peroxisomal division when overexpressed.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0534R-CY3)
Fournisseur:
Bioss
Description:
P19ARF Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0534R-CY5.5)
Fournisseur:
Bioss
Description:
P19ARF Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9474R-CY3)
Fournisseur:
Bioss
Description:
Members of the NFAT (nuclear factor of activated T cells) family of transcription factors are related to NFkB/Rel proteins and form cooperative complexes with the AP-1 proteins, Fos and Jun, on DNA to regulate cytokine expression in T cells. NFAT proteins are widely expressed and alternatively modified to generate splice variants, and they are localized to both the cytosol (NFATc) and to the nucleus (NFATn). NFAT1, NFAT2, and NFAT4 are predominantly expressed in immune cells, and NFAT2 and NFAT3 are expressed at high levels in cardiac tissues. In addition to activating cytokine gene transcription, NFAT2 is also implicated in cardiac valve development, and NFAT3 is involved in cardiac hypertrophy. NFAT5 is detected in both immune and nonimmune cells and, like other NFAT proteins, contains a highly conserved Rel-like binding domain that mediates NFAT proteins associating with specific consensus sequences on DNA. NFAT proteins are activated by increases in intracellular calcium, which leads to the calmodulin-dependent phosphatase, calcineurin, dephosphorylating NFAT proteins. This activating event induces a conformational change in the protein structure that exposes the nuclear localization signal and facilitates the translocation of NFAT proteins from the cytosol into the nucleus.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1779R)
Fournisseur:
Bioss
Description:
Members of the GATA family share a conserved zinc finger DNA-binding domain and are capable of binding the WGATAR consensus sequence. GATA-1 is erythroid-specific and is responsible for the regulated transcription of erythroid genes. It is an essential component in the generation of the erythroid lineage. GATA-2 is expressed in embryonic brain and liver, HeLa and endothelial cells, as well as in erythroid cells. Studies with a modified GATA consensus sequence, AGATCTTA, have shown that GATA-2 and GATA-3 recognize this mutated consensus while GATA-1 has poor recognition of this sequence. This indicates broader regulatory capabilities of GATA-2 and GATA-3 than GATA-1. GATA-3 is highly expressed in T lymphocytes. GATA-4, GATA-5 and GATA-6 comprise a subfamily of transcription factors. Both GATA-4 and GATA-6 are found in heart, pancreas and ovary; lung and liver tissues exhibit GATA-6, but not GATA-4 expression. GATA-5 expression has been observed in differentiated heart and gut tissues and is present throughout the course of development in the heart. Although expression patterns of the various GATA transcription factors may overlap, it is not yet apparent how the GATA factors are able to discriminate in binding their appropriate target sites.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0990R-CY7)
Fournisseur:
Bioss
Description:
Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6P targets several other substrates to degradation via the proteasome including host NFX1-91, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including Bak, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11104R)
Fournisseur:
Bioss
Description:
Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.
UOM:
1 * 100 µl
Fournisseur:
3M Food Safety
Description:
3M™ Petrifilm™ Enterobacteriaceae count plates provide a cost-effective, convenient and reliable method for testing equipment, raw materials, food products and manufacturing environmental samples and bottled water testing.
Numéro de catalogue:
(BOSSBS-4897R-HRP)
Fournisseur:
Bioss
Description:
Atypical chemokine receptor that controls chemokine levels and localization 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 (internalizing 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 internalization 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.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3730R-A350)
Fournisseur:
Bioss
Description:
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play distinct roles in cells. The protein encoded by this gene is one of the PKC family members. There have been at least 12 different PKC isoforms identified in humans to date including alpha, beta I, beta II, gamma, delta, epsilon, zeta, eta, theta, iota, lambda, and mu. PKC gamma is expressed solely in the brain and spinal cord and its localization is restricted to neurons. It has been demonstrated that several neuronal functions, including long term potentiation (LTP) and long term depression (LTD), specifically require this kinase. Knockout studies in mice also suggest that this kinase may be involved in neuropathic pain development. Defects in this protein have been associated with neurodegenerative disorder spinocerebellar ataxia-14 (SCA14).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5915R-CY7)
Fournisseur:
Bioss
Description:
DNA methylation, or the addition of methyl groups to cytosine bases in the dinucleotide CpG, is imperative to proper development and regulates gene expression. The methylation pattern involves the enzymatic processes of methylation and demethylation. The demethylation enzyme was recently found to be a mammalian protein, which exhibits demethylase activity associated to a methyl-CpG-binding domain (MBD). The enzyme is able to revert methylated cytosine bases to cytosines within the particular dinucleotide sequence mdCpdG by catalyzing the cleaving of the methyl group as methanol. MeCP2 and MBD1 (PCM1) are first found to repress transcription by binding specifically to methylated DNA. MBD2 and MBD4 (also known as MED1) were later found to colocalize with foci of heavily methylated satellite DNA and believed to mediate the biological functions of the methylation signal. Surprisingly, MBD3 does not bind methylated DNA both in vivo and in vitro. MBD1, MBD2, MBD3, and MBD4 are found to be expressed in somatic tissues, but the expression of MBD1 and MBD2 is reduced or absent in embryonic stem cells, which are known to be deficient in MeCP1 activity. MBD4 have homology to bacterial base excision repair DNA N-glycosylases/lyases. In some microsatellite unstable tumors MBD4 is mutated at an exonic polynucleotide tract.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11044R-CY5)
Fournisseur:
Bioss
Description:
Adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containg non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11044R-A647)
Fournisseur:
Bioss
Description:
Adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containg non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11044R-CY7)
Fournisseur:
Bioss
Description:
Adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containg non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling.
UOM:
1 * 100 µl
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