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Update to Avantor’s response to the coronavirus (COVID-19) pandemic

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Pentafluorophenyl+isothiocyanate


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Supplier:  Bioss
Description:   The initiation of DNA replication is a multi-step process that depends on the formation of pre-replication complexes, which trigger initiation (1). Among the proteins required for establishing these complexes are the origin recognition complex (ORC) proteins (1). ORC proteins bind specifically to origins of replication where they serve as scaffold for the assembly of additional initiation factors (1). Human ORC subunits 1-6 are expressed in the nucleus of proliferating cells and tissues, such as the testis (2). ORC1 and ORC2 are both expressed at equivalent concentrations throughout the cell cycle; however, only ORC2 remains stably bound to chromatin (3,4). ORC4 and ORC6 are also expressed constantly throughout the cell cycle (5,6). ORC2, ORC3, ORC4 and ORC5 form a core complex upon which ORC6 and ORC1 assemble (7,8). The formation of this core complex suggests that ORC proteins play a crucial role in the G1-S transition in mammalian cells (8).
Supplier:  Bioss
Description:   Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML.
Supplier:  Bioss
Description:   Separase is a cysteine protease that is essential for mitotic progression by separating sister chromatids. Each cell must receive one chromatid of every chromosome, during mitosis. Cohesin plays an important role in cohering sister chromatids during the prophase through anaphase stages of mitosis, making certain that genomic information is replicated accurately. As the cellular division process continues, separase destroys cohesin by means of cleavage, allowing the chromatids to separate and divide with the cell. Separase activity is highly regulated. It not only cleaves cohesin at the onset of anaphase but also cleaves itself, promoting downregulation of separase after anaphase. Should a human cell become an aneuploid (one too many or too few chromatids), the embryo most likely will not survive. Should the embryo survive, it will most likely develop severe birth defects or later develop malignant cancers.
Supplier:  Bioss
Description:   G protein-coupled receptors (GPRs), also known as seven transmembrane receptors, heptahelical receptors or 7TM receptors, comprise a superfamily of proteins that play a role in many different stimulus-response pathways. GPR signaling is an evolutionarily ancient mechanism used by all eukaryotes to sense environmental stimuli and mediate cell-cell communication. G protein-coupled receptors translate extracellular signals into intracellular signals (G protein activation) and they respond to a variety of signaling molecules, such as hormones and neurotransmitters. GPR20 is a 358 amino acid membrane protein that constitutively activates G(i) proteins without ligand stimulation. Also, GPR20 may be involved in the control of intracellular cAMP levels and mitogenic signaling. Interestingly, GPR20 is expressed in liver and certain regions of the brain, including putamen, caudate and thalamus, but is not expressed in hypothalamus, pons and frontal cortex.
Supplier:  Bioss
Description:   The protein encoded by this gene belongs to a small class of the protein tyrosine phosphatase (PTP) family. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. PTPs in this class contain a protein tyrosine phosphatase catalytic domain and a characteristic C-terminal prenylation motif. This PTP has been shown to primarily associate with plasmic and endosomal membrane through its C-terminal prenylation. This PTP was found to interact with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), and thus may function as a regulator of GGT II activity. Overexpression of this gene in mammalian cells conferred a transformed phenotype, which suggested its role in tumorigenesis. Alternatively spliced transcript variants have been described. Related pseudogenes exist on chromosomes 11, 12 and 17. [provided by RefSeq, Aug 2010]
Supplier:  Bioss
Description:   Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis.
Supplier:  Bioss
Description:   The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. This cyclin forms a complex with and functions as a regulatory subunit of CDK4 or CDK6, whose activtiy is required for cell cycle G1/S transition. This protein has been shown to interact with and be involved in the phosphorylation of tumor suppressor protein Rb. The CDK4 activity associated with this cyclin was reported to be necessary for cell cycle progression through G2 phase into mitosis after UV radiation. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2008].
Supplier:  Bioss
Description:   Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, is controlled by G-proteins and is found associated with the sulfonylurea receptor SUR. Mutations in this gene are a cause of familial persistent hyperinsulinemic hypoglycemia of infancy (PHHI), an autosomal recessive disorder characterized by unregulated insulin secretion. Defects in this gene may also contribute to autosomal dominant non-insulin-dependent diabetes mellitus type II (NIDDM), transient neonatal diabetes mellitus type 3 (TNDM3), and permanent neonatal diabetes mellitus (PNDM). Multiple alternatively spliced transcript variants that encode different protein isoforms have been described for this gene. [provided by RefSeq]
Supplier:  Bioss
Description:   Apelin is a neuropeptide expressed in the supraoptic and paraventricular nuclei and is an endogenous ligand for APJ, a G protein-coupled orphan receptor which is an alternative coreceptor with CD4 for HIV-1. Apelin and APJ are ubiquitously expressed in peripheral tissues, with highest levels reported for heart and lungs, as well several regions within the central nervous system. The actions of apelin remain largely unknown: Apelin inhibits HIV-1 entry in cells coexpressing CD4 and APJ; the oral intake of Apelin in colostrum and breast milk could have a role in the modulation of the immune responses in neonates; more recent studies have also indicated a role for Apelin in the central control of body fluid homeostasis, by influencing AVP release and drinking behavior. In the cardiovascular system several actions of Apelin have been described, including endothelium-dependent vasodilatation, vasoconstriction through direct action on smooth muscle and positive inotropism.
Supplier:  Bioss
Description:   This protein belongs to a family of Zn-containing metallocarboxypeptidases specific to C-terminal lysine and arginine residues. It circulates in plasma as a zymogen with molecular weight of 55 kDa (401 amino acid residues; pI 5.0). Being activated by thrombin-thrombomodulin complex during blood coagulation, it exerts carboxypeptidase activity. Activated carboxypeptidase B2 removes C-terminal lysine residues from fibrin, which is necessary for plasminogen binding to fibrin. This prevents plasminogen from activation into plasmin and retards the lysis of a fibrin clot. The concentration in plasma of healthy people is 5-10 ug/ml. High plasma levels were found in patients with stable angina pectoris and angiographically verified coronary artery disease. Elevated concentration in blood is considered as a risk factor for venous thrombosis. A deficiency might contribute to the severity of bleeding disorders in hemophilias A and B, and decreased levels are found in chronic liver disease.
Supplier:  Bioss
Description:   Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.
Supplier:  Bioss
Description:   Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis.
Supplier:  Bioss
Description:   Prominin 2 is a 112 kDa glycoporotein structurally related to Prominin 1 (CD133) although amino acid similarity is not more than 30%, but their genomic organization is strikingly similar. Like Prominin 1, the prominin 2 exhibit similar membrane topology with 5 trans-membrane domains and two large glycosylated extracellular domains. Similar to Prominin1 localization, the Prominin 2 is also associated with membrane protrusions of the epithelial cells from adult kidney, and all along the digestive track and other epithelial tissues.Prominin 2 expression is down-regulated in aggressive prostate cancer cell lines and transient transfection of PROML2 expression vectors has been shown to induce apoptosis in cultured prostate cancer cells, suggesting a tumor suppressive role for Prominin 2. Prominin 2 expression is likely to be involved in growth suppression in the prostate, and down-regulation of Prominin 2 may disrupt normal prostatic homeostasis and lead to uncontrolled prostatic growth.
Supplier:  Bioss
Description:   The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.
Supplier:  Bioss
Description:   FBXO29, also designated F-box/WD repeat-containing protein 8 (FBXW8), is a 598 amino acid protein that contains one 40 amino acid F-box region, making it a member of the F-box family. FBXO29 also contains five WD repeats. F-box proteins are critical components of the SCF (Skp1-CUL-1-F-box protein) type E3 ubiquitin ligase complex and are involved in substrate recognition and recruitment for ubiquitination. F-box proteins are members of a large family that regulates cell cycle, immune response, signaling cascades and developmental programs by targeting proteins, such as cyclins, cyclin-dependent kinase inhibitors, IkB-Ã¥ and ∫-catenin, for degradation by the proteasome after ubiquitination. Functioning as a component of the SCF complex, FBXO29 is thought to recognize and bind to select phosphorylated proteins, thereby promoting their ubiquitination and subsequent degradation. FBXO29 exists as two isoforms as a result of alternative splicing events.
Supplier:  Bioss
Description:   Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.
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