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


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Supplier:  Bioss
Description:   Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the 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 family members 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 a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This kinase has been shown to be involved in many different cellular functions, such as neuron channel activation, apoptosis, cardioprotection from ischemia, heat shock response, as well as insulin exocytosis. Knockout studies in mice suggest that this kinase is important for lipopolysaccharide (LPS)-mediated signaling in activated macrophages and may also play a role in controlling anxiety-like behavior. [provided by RefSeq, Jul 2008].
Supplier:  Bioss
Description:   C2orf50 (chromosome 2 open reading frame 50), also known as FLJ25143 or MGC149401, is a 162 amino acid protein that is encoded by a gene located on human chromosome 2p25.1. The second largest human chromosome, chromosome 2 consists of 237 million bases, encodes over 1,400 genes and makes up approximately 8% of the human genome. A number of genetic diseases are linked to genes on chromosome 2. Harlequin icthyosis, a rare and morbid skin deformity, is associated with mutations in the ABCA12 gene. The lipid metabolic disorder sitosterolemia is associated with ABCG5 and ABCG8. An extremely rare recessive genetic disorder, Alstr syndrome is due to mutations in the ALMS1 gene. Interestingly, chromosome 2 contains what appears to be a vestigial second centromere and vestigial telomeres which gives credence to the hypothesis that human chromosome 2 is the result of an ancient fusion of two ancestral chromosomes seen in modern form today in apes.
Supplier:  Bioss
Description:   This gene encodes a member of the estrogen receptor-related receptor (ESRR) family, which belongs to the nuclear hormone receptor superfamily. All members of the ESRR family share an almost identical DNA binding domain, which is composed of two C4-type zinc finger motifs. The ESRR members are orphan nuclear receptors; they bind to the estrogen response element and steroidogenic factor 1 response element, and activate genes controlled by both response elements in the absence of any ligands. The ESRR family is closely related to the estrogen receptor (ER) family. They share target genes, co-regulators and promoters, and by targeting the same set of genes, the ESRRs seem to interfere with the ER-mediated estrogen response in various ways. It has been reported that the family member encoded by this gene functions as a transcriptional activator of DNA cytosine-5-methyltransferases 1 (Dnmt1) expression by direct binding to its response elements in the DNMT1 promoters, modulates cell proliferation and estrogen signaling in breast cancer, and negatively regulates bone morphogenetic protein 2-induced osteoblast differentiation and bone formation. Multiple alternatively spliced transcript variants have been identified, which mainly differ at the 5' end and some of which encode protein isoforms differing in the N-terminal region.
Supplier:  Bioss
Description:   On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.Involvement in disease; Defects in BMPR1B are the cause of acromesomelic chondrodysplasia with genital anomalies (AMDGA). Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs, and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers).Defects in BMPR1B are a cause of brachydactyly type A2 (BDA2) [MIM:112600]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits. BDA2 was described first in a large Norwegian kindred. BDA2 is caused by mutations in BMPR1B gene and studies demonstrate that these mutations function as dominant negatives in vitro and in vivo.
Supplier:  Bioss
Description:   Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction.
Supplier:  Bioss
Description:   Chemoattractant active on T-lymphocytes, monocytes, but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. SDF-1-beta(3-72) and SDF-1-alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites. Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Inhibits CXCR4-mediated infection by T-cell line-adapted HIV-1. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells. Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation.
Supplier:  Bioss
Description:   In Drosophila, neuronal cell fate decisions are directed by NUMB, a signaling adapter protein with two protein-protein interaction domains, namely a phosphotyrosine-binding domain and a proline-rich SH3-binding region (PRR). The mammalian NUMB homolog plays a role in the determination of cell fate during development and binds with a variety of proteins, including Eps15, LNX1 and Notch 1. NumbL (NUMB-like protein), also known as Numb-R, NBL, CAG3A, CTG3a, NUMBLIKE or TNRC23, is a 609 amino acid cytoplasmic protein that, like NUMB, is thought to play a role in cell fate. Expressed at high levels in developing brain tissue, NumbL contains one PID (phosphotyrosine interaction domain) and plays an important role in neuronal differentiation, possibly associating with Eps15 and Notch 1. In mice, deletion of the NumbL gene is associated with early embryonic death, suggesting an essential role for NumbL in early development.
Supplier:  Bioss
Description:   Members of the C1q superfamily have diverse functions that are related to cell adhesion and basement membrane components. CTRP5 (Complement C1q tumor necrosis factor-related protein 5) is a 243 amino acid secreted and membrane-associated protein that contains a collagen-like domain and a C1q domain. CTRP5 is a short-chain collagen that is expressed in retinal pigment epithelium as well as brain, lung, liver and placenta. By forming an extracellular hexagonal lattice, CTRP5 facilitates the adhesion of basal retinal pigment epithelium to Bruch’s membrane, the innermost layer of the choroid. A mutation within the C1q domain of CTRP5 results in abnormal high molecular weight aggregate formation, which alters its structure and interactions. This mutation may result in the presentation of late-onset retinal degeneration (LORD), an autosomal dominant disorder that is characterized by punctate yellow-white deposits in the retinal fundus and night blindness.
Supplier:  Bioss
Description:   Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects golgi structure, and a group of smaller GEPs that are insenstive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.
Supplier:  Bioss
Description:   Carbonic anhydrases (CAs), also designated carbonate dehydratases or carbonate hydrolyases, form a large family of genes that encode zinc metalloenzymes of great physiologic importance. As catalysts of the reversible hydration of carbon dioxide, these enzymes participate in a variety of biologic processes, including respiration, acid-base balance, bone resorption and calcification as well as the formation of aqueous humor, cerebrospinal fluid, saliva and gastric acid. Genes in the ?carbonic anhydrase family encode either active carbonic anhydrase isozymes or 揳catalytic?(devoid of CO2 hydration activity) carbonic anhydrase-related proteins. Human CA I (CA1) is encoded by the CA1 gene, which maps to a region on chromosome 8 that harbors a cluster of CA genes. CA I localizes to the cytoplasm and research indicates that a severe deficiency of CA I does not result in any obvious hematological or renal consequences.
Supplier:  Bioss
Description:   The Hox homeobox genes encode proteins that are transcriptional regulators with an established role in embryonic development. HoxA4 (homeobox A4), also known as HOX1D or HOX1, is a 320 amino acid protein that localizes to the nucleus and contains one homeobox DNA-binding domain. Expressed in the embryonic nervous system, HoxA4 functions as a sequence-specific DNA-binding transcription factor that is part of a regulatory mechanism that provides cells with positional identities during development. Via its ability to bind DNA, HoxA4 plays an important role in the regulation of gene expression, as well as morphogenesis and differentiation. The gene encoding HoxA4 maps to human chromosome 7, which houses over 1,000 genes and comprises nearly 5% of the human genome. Defects in some of the genes localized to chromosome 7 have been linked to Osteogenesis imperfecta, Williams-Beuren syndrome, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome.
Supplier:  Bioss
Description:   ACBD3 (acyl-CoA-binding domain-containing protein 3), also known as GCP60 (Golgi resident protein GCP60), GOCAP1, PAP7 or GOLPH1, is a Golgi apparatus membrane protein that contains one ACB (acyl-CoA-binding) domain and one GOLD (Golgi dynamics) domain which is essential for its interaction with other proteins. Expressed ubiquitously with highest expression in ovary and testis, ACBD3 is responsible for maintaining Golgi structure and, through binding to Giantin (golgin subfamily B member 1), functions to mediate protein transport between the Golgi and the endoplasmic reticulum (ER). Changes in the subcellular location of ACBD3 trigger signaling cascades within the Golgi that regulate cell fate and cell cycle progression. Additionally, ACBD3 is thought to act as a peripheral-type benzodiazepine receptor-associated protein, possibly playing a role in hormonal regulation and steroid formation.
Supplier:  Bioss
Description:   MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (1–3). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).
Supplier:  Bioss
Description:   The DnaJ family is one of the largest of all the chaperone families and has evolved with diverse cellular localization and functions. The presence of the J domain defines a protein as a member of the DnaJ family. DnaJ heat shock induced proteins are from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. The DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. The proteins contain cysteine rich regions that are composed of zinc fingers that form a peptide binding domain responsible for the chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJA2 (DnaJ homolog subfamily A member 2), also known as HIRA-interacting protein 4 or cell cycle progression restoration gene 3 protein, contains one CR-type zinc finger and is a co-chaperone of HSC 70.
Supplier:  Bioss
Description:   The gamma-Tubulin complex is composed of gamma Tubulin and the gamma-Tubulin complex-associated proteins GCP2, GCP3, GCP4, GCP5 and GCP6, all of which are essential components of microtubule organizing centers. gamma-Tubulin complex components are localized to both the centrosome, where they are involved in microtubule nucleation, and to the cytoplasm, where they exist as soluble complexes that can be recruited to the centrosome as needed. Although the GCP proteins are related, they have distinct roles which contribute to the proper function of the gamma-Tubulin complex. GCP4 (gamma-tubulin complex component 4), also known as TUBGCP4, is a ubiquitously expressed 667 amino acid member of the gamma-Tubulin complex that localizes to the metaphase spindle during mitosis. In response to proteosome inhibition, GCP4 exhibits increased accumulation at the pericentiolar material where it participates in microtubule organization and nucleation.
Supplier:  Bioss
Description:   GAD-65 and GAD-67, glutamate decarboxylases, function to catalyze the production of GABA (gamma-aminobutyric acid). In the central nervous system GABA functions as the main inhibitory transmitter by increasing a Cl- conductance that inhibits neuronal firing. GABA has been shown to activate both ionotropic (GABAA) and metabotropic (GABAB) receptors as well as a third class of receptors called GABAC. Both GABAA and GABAC are ligand-gated ion channels, however, they are structurally and functionally distinct. Members of the GABAA receptor family include GABAA R Alpha 1-6, GABAA R Beta 1-3, GABAA R Gamma 1-3, GABAA R Delta, GABAA R Epsilon, GABAA R Zeta 1 and GABAA R Zeta 2. The GABAB family is composed of GABAB R1 Alpha and GABAB R1 Beta. GABA transporters have also been identified and include GABA T-1, GABA T-2 and GABA T-3 (also designated GAT-1, -2, and -3). The GABA transporters function to terminate GABA action.
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