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Solid+Phase+Extraction
Numéro de catalogue:
(BOSSBS-7782R-A350)
Fournisseur:
Bioss
Description:
This gene encodes for a coiled coil domain containing 16 protein and is located on chromosome 17. The protein may act as a regulator of the cell cycle in embryos by participating in control of M phase.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9249R-HRP)
Fournisseur:
Bioss
Description:
Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7615R-A488)
Fournisseur:
Bioss
Description:
The death domain (DD) containing protein PIDD is a p53 target gene in an erythroleukemia cell line that undergoes G1 phase arrest and subsequent apoptosis after p53 expression. Independently, PIDD was also described as a DD-containing protein with unknown function. The N-terminal region of PIDD contains seven leucine-rich repeats (LRRs), a protein interaction motif found in various proteins with diverse functions, followed by two ZU-5 domains and a C-terminal DD. PIDD forms a complex with caspase-2 and the adaptor protein RAIDD. Increased PIDD expression results in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli, via interaction with caspase-2 and CRADD/RAIDD. PIDD also promotes apoptosis downstream of p53 as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. PIDD has also been shown to interact with NEMO/IKBKG and RIP1 and enhance sumoylation and ubiquitination of NEMO/IKBKG, an important component for activation of the transcription factor NF-kappa-B.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7615R-FITC)
Fournisseur:
Bioss
Description:
The death domain (DD) containing protein PIDD is a p53 target gene in an erythroleukemia cell line that undergoes G1 phase arrest and subsequent apoptosis after p53 expression. Independently, PIDD was also described as a DD-containing protein with unknown function. The N-terminal region of PIDD contains seven leucine-rich repeats (LRRs), a protein interaction motif found in various proteins with diverse functions, followed by two ZU-5 domains and a C-terminal DD. PIDD forms a complex with caspase-2 and the adaptor protein RAIDD. Increased PIDD expression results in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli, via interaction with caspase-2 and CRADD/RAIDD. PIDD also promotes apoptosis downstream of p53 as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. PIDD has also been shown to interact with NEMO/IKBKG and RIP1 and enhance sumoylation and ubiquitination of NEMO/IKBKG, an important component for activation of the transcription factor NF-kappa-B.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7615R-CY3)
Fournisseur:
Bioss
Description:
The death domain (DD) containing protein PIDD is a p53 target gene in an erythroleukemia cell line that undergoes G1 phase arrest and subsequent apoptosis after p53 expression. Independently, PIDD was also described as a DD-containing protein with unknown function. The N-terminal region of PIDD contains seven leucine-rich repeats (LRRs), a protein interaction motif found in various proteins with diverse functions, followed by two ZU-5 domains and a C-terminal DD. PIDD forms a complex with caspase-2 and the adaptor protein RAIDD. Increased PIDD expression results in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli, via interaction with caspase-2 and CRADD/RAIDD. PIDD also promotes apoptosis downstream of p53 as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. PIDD has also been shown to interact with NEMO/IKBKG and RIP1 and enhance sumoylation and ubiquitination of NEMO/IKBKG, an important component for activation of the transcription factor NF-kappa-B.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7615R-HRP)
Fournisseur:
Bioss
Description:
The death domain (DD) containing protein PIDD is a p53 target gene in an erythroleukemia cell line that undergoes G1 phase arrest and subsequent apoptosis after p53 expression. Independently, PIDD was also described as a DD-containing protein with unknown function. The N-terminal region of PIDD contains seven leucine-rich repeats (LRRs), a protein interaction motif found in various proteins with diverse functions, followed by two ZU-5 domains and a C-terminal DD. PIDD forms a complex with caspase-2 and the adaptor protein RAIDD. Increased PIDD expression results in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli, via interaction with caspase-2 and CRADD/RAIDD. PIDD also promotes apoptosis downstream of p53 as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. PIDD has also been shown to interact with NEMO/IKBKG and RIP1 and enhance sumoylation and ubiquitination of NEMO/IKBKG, an important component for activation of the transcription factor NF-kappa-B.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11224R-A488)
Fournisseur:
Bioss
Description:
DNA damage or incomplete replication of DNA results in the inhibition of cell cycle progression at the G1 to S or the G2 to M phase transition by conserved regulatory mechanisms known as cell cycle checkpoints. Checkpoint proteins include Rad17, which is involved in regulating cell cycle progression at the G1 checkpoint as well as Chk1, Chk2, Rad1, Rad9 and Hus1, which are involved in regulating cell cycle arrest at the G2 checkpoint. In response to DNA damage, ATM and ATR kinases are important for cell cycle checkpoint response signalling. ATR-interacting protein (ATRIP), also designated ATM and Rad3-related-interacting protein, is required for checkpoint signaling after DNA damage. It is also important for ATR expression, which regulates DNA replication and damage checkpoint responses. ATRIP is a ubiquitously expressed protein that can form heterodimers with ATR. After dimerization they bind the RPA complex and are recruited to single stranded DNA. ATRIP is a nuclear protein that may also play a role in protein stabilization.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9301R-HRP)
Fournisseur:
Bioss
Description:
SAS-6 (spindle assembly abnormal protein 6 homolog, HsSAS-6) is a 657 amino acid protein encoded by the human gene SAS6. SAS-6 is a component of the centrosome that contains one PISA (present in SAS-6) domain. LK4, SAS-6, CPAP and other centriole related proteins are required at different stages of procentriole formation and were associated with different centriolar structures. SAS-6 associates only transiently with nascent procentrioles, whereas CEP135 and CPAP form a core structure within the proximal lumen of both parental and nascent centrioles. SAS-6 is necessary for procentriole formation in human cell lines and is localized asymmetrically next to the centriole at the onset of procentriole formation. SAS-6 levels oscillate during the cell cycle; it is degraded in mitosis starting at anaphase, and it accumulates again at the end of the following G1 phase. The anaphase-promoting complex targets SAS-6 for degradation by the 26S Proteasome, and a KEN box in the C-terminus of SAS-6 is necessary for its degradation. Increased SAS-6 levels promoted the formation of multiple procentrioles forming next to a single centriole.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11224R-A680)
Fournisseur:
Bioss
Description:
DNA damage or incomplete replication of DNA results in the inhibition of cell cycle progression at the G1 to S or the G2 to M phase transition by conserved regulatory mechanisms known as cell cycle checkpoints. Checkpoint proteins include Rad17, which is involved in regulating cell cycle progression at the G1 checkpoint as well as Chk1, Chk2, Rad1, Rad9 and Hus1, which are involved in regulating cell cycle arrest at the G2 checkpoint. In response to DNA damage, ATM and ATR kinases are important for cell cycle checkpoint response Signalling. ATR-interacting protein (ATRIP), also designated ATM and Rad3-related-interacting protein, is required for checkpoint Signalling after DNA damage. It is also important for ATR expression, which regulates DNA replication and damage checkpoint responses. ATRIP is a ubiquitously expressed protein that can form heterodimers with ATR. After dimerization they bind the RPA complex and are recruited to single stranded DNA. ATRIP is a nuclear protein that may also play a role in protein stabilisation.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2993R-CY5)
Fournisseur:
Bioss
Description:
Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.
UOM:
1 * 100 µl
Fournisseur:
Thermo Fisher Scientific
Description:
Choose Thermo Scientific™ SureSTART™ 2 ml glass screw top vials, performance level 2, to ensure high quality data with an uninterrupted workflow in high-throughput applications using GC, HPLC/UHPLC, and single or triple quadrupole MS systems. Use level 2 vials for routine QA/QC applications, where the analyte levels are achievable or close to the method detection level. Available in clear and amber glass, these 2 ml screw top vials have very low metal content, extractables, and leachables and conform to high standards so that you can to meet your regulatory requirements. They are specification certified to ensure their physical dimensions and autosampler compatibility.
Numéro de catalogue:
(BOSSBS-6085R)
Fournisseur:
Bioss
Description:
Plays a role in the regulation of the circadian clock. Modulates the period length and phase of circadian gene expression and also regulates expression and interaction of the core clock components PER1/2 and CRY1/2. Seems to have an immune potentiation function.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11267R-CY5)
Fournisseur:
Bioss
Description:
CCT2 is one of eight largely unrelated subunit proteins found in a protein chaperone complex known as the chaperonin-containing TCP-1 (CCT) or TRiC complex. The CCT complex is an abundanct cytoslic component that is credited with helping newly synthesized polypeptides adopt the correct conformation (1). Proteins that fold and assemble with the help of CCT include the cytoskeletal proteins actin and tubulin as well as up to 15% of newly synthesized eukaryotic proteins (2). CCT2 is the β-subunit of the chaperone complex and is one of several CCT proteins that exhibit increased expression in response to stress. This implies that the CCT complex helps cells recover from protein damage by assisting in protein folding and assembly (3). CCT subunit levels also change throughout the cell cycle, with lower proteins levels (and reduced chaperone activity) found during induced cell cycle arrest during at M phase (4). Each CCT subunit is thought to perform a specific function during protein folding and assembly (5); CCT2 exhibits both actin and tubulin binding activities (6,3) but the exact molecular function on this subunit remains uncertain.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2993R-CY5.5)
Fournisseur:
Bioss
Description:
Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6377R-A750)
Fournisseur:
Bioss
Description:
Suppressin, also known as DEAF1 is a transcription factor required for embryonic development. Suppressin contains one SAND domain and one C-terminal MYND-type zinc finger. It interacts with LMO4 and CLIM-2, suggesting that it plays a role mediating cell fate and embryonic pattern formation. Suppressin is expressed in a variety of tissues and localises to the nucleus. Several isoforms exist due to alternative splicing and, depending on the isoform, Suppressin is secreted in some cell types. Secreted Suppressin can function to inhibit cell proliferation, arresting cells in the G0 or G1 phase. Mutations in the gene encoding Suppressin may result in a growth advantage leading to the development and progression of neoplasia. This suggest that Supressin is a potential target for cancer therapy.
UOM:
1 * 100 µl
Numéro de catalogue:
(BNUM1098-50)
Fournisseur:
Biotium
Description:
This antibody recognizes a protein of 55-62 kDa, identified as cyclin B1. In mammals, cyclin B associates with inactive p34cdc2, which facilitates phosphorylation of p34cdc2 at aa 14Thr and 15Tyr. This maintains the inactive state until the end of G2-phase. The inactive cyclin B-p34cdc2 complex continues to accumulate in the cytoplasm until the completion of DNA synthesis, when Cdc25, a specific protein phosphatase, dephosphorylates aa 14Thr and 15Tyr of p34cdc2 rendering the complex active at the G2/M boundary. This mitotic kinase complex remains active until the metaphase/anaphase transition when cyclin B is degraded. This degradation process is ubiquitin-dependent and is necessary for the cell to exit mitosis. So, cyclin B-p34cdc2 plays a critical role in G2 to M transition.
UOM:
1 * 50 µl
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