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Masterflex+Single-use+Flow+Sensor
Numéro de catalogue:
(BOSSBS-3804R-A647)
Fournisseur:
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.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0758R-CY5.5)
Fournisseur:
Bioss
Description:
Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta 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. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0758R-A680)
Fournisseur:
Bioss
Description:
Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognises single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognises larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta 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. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1922R)
Fournisseur:
Bioss
Description:
Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.
UOM:
1 * 100 µl
Fournisseur:
VWR Collection
Description:
Ces charlottes plissées à usage unique sont fabriquées à partir d'un tissu non tissé, en polypropylène spunbond (SPP), qui protège de la saleté et de certaines particules sèches dans des environnements non dangereux.
Numéro de catalogue:
(BOSSBS-10994R-A488)
Fournisseur:
Bioss
Description:
Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA nonhomologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC6, WRN, c-myc/MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate TP53/p53 in the presence of supercoiled DNA is dependent on C1D.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11420R-CY5)
Fournisseur:
Bioss
Description:
Neuromedin U is a neuropeptide with high activity on smooth muscle. It is widely expressed in gastrointestinal systems and central nervous system (CNS). Peripheral activities of neuromedin U include smooth muscle stimulation, ion transport alterations in the gut and the regulation of local blood flow and adrenocortical function. Neuromedin U receptors 1 and 2 (NMUR1 and NMUR2) are multi-pass membrane proteins that belong to the G-protein coupled receptor 1 family of proteins. Both NMUR1 and NMUR2 act as receptors for the neuromedin U neuropeptide. NMUR1 is detected in peripheral organs, particularly in urogenital and gastrointestinal systems, with highest levels in testis. It’s expression in CNS is low, but the protein has been detected in cerebellum, hippocampus, dorsal root ganglia and spinal cord. NMUR2 is predominantly detected in central nervous system with highest levels detected in medulla oblongata, spinal cord and thalamus. It may also be detected in testis but has low levels of expression in peripheral tissues.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-10994R-CY7)
Fournisseur:
Bioss
Description:
Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA nonhomologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC6, WRN, c-myc/MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate TP53/p53 in the presence of supercoiled DNA is dependent on C1D.
UOM:
1 * 100 µl
Fournisseur:
HAMILTON BONADUZ
Description:
Sensor cable, K8/DIN (for sensors with K8 connector), length 1 m, Pour: Hamilton pH Electrodes
Numéro de catalogue:
(BOSSBS-2097R-A750)
Fournisseur:
Bioss
Description:
Angiotensin II is a potent vasopressor hormone and a primary regulator of aldosterone secretion. It is an important effector controlling blood pressure and volume in the cardiovascular system. It acts through at least two types of receptors. This gene encodes the type 1 receptor which is thought to mediate the major cardiovascular effects of angiotensin II. This gene may play a role in the generation of reperfusion arrhythmias following restoration of blood flow to ischemic or infarcted myocardium. It was previously thought that a related gene, denoted as AGTR1B, existed; however, it is now believed that there is only one type 1 receptor gene in humans. At least five transcript variants have been described for this gene. Additional variants have been described but their full-length nature has not been determined. The entire coding sequence is contained in the terminal exon and is present in all transcript variants.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2097R-A647)
Fournisseur:
Bioss
Description:
Angiotensin II is a potent vasopressor hormone and a primary regulator of aldosterone secretion. It is an important effector controlling blood pressure and volume in the cardiovascular system. It acts through at least two types of receptors. This gene encodes the type 1 receptor which is thought to mediate the major cardiovascular effects of angiotensin II. This gene may play a role in the generation of reperfusion arrhythmias following restoration of blood flow to ischemic or infarcted myocardium. It was previously thought that a related gene, denoted as AGTR1B, existed; however, it is now believed that there is only one type 1 receptor gene in humans. At least five transcript variants have been described for this gene. Additional variants have been described but their full-length nature has not been determined. The entire coding sequence is contained in the terminal exon and is present in all transcript variants. [provided by RefSeq].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11062R-A750)
Fournisseur:
Bioss
Description:
CYTIP is a cytoplasmic protein that is involved in lymphocytic cell adhesion. Expressed primarily in hematopoetic cells, CYTIP regulates the activity of cytohesin-1 (an integrin-activating protein involved in cell adhesion) by mediating its recruitment to the leukocyte membrane. Through its ability to bind cytohesin-1, CYTIP is able to sequester it to the cytoplasm, thereby preventing cytohesin-1 translocation to lymphocytes and interrupting the flow of information in the cell adhesion pathway. CYTIP can be recruited from the cytoplasm to the membrane by leukocyte integrins which interact with CYTIP through its PDZ domain. After membrane translocation, CYTIP can be re-located to the cytoplasm via exposure to a phorbol ester. Additionally, CYTIP associates with SNX27 (sorting nexin 27) and helps to coordinate trafficking and Signalling complexes. Up-regulation of CYTIP is observed in maturing dendritic cells, suggesting a possible role in developmentally-controlled cell adhesion.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11062R-A680)
Fournisseur:
Bioss
Description:
CYTIP is a cytoplasmic protein that is involved in lymphocytic cell adhesion. Expressed primarily in hematopoetic cells, CYTIP regulates the activity of cytohesin-1 (an integrin-activating protein involved in cell adhesion) by mediating its recruitment to the leukocyte membrane. Through its ability to bind cytohesin-1, CYTIP is able to sequester it to the cytoplasm, thereby preventing cytohesin-1 translocation to lymphocytes and interrupting the flow of information in the cell adhesion pathway. CYTIP can be recruited from the cytoplasm to the membrane by leukocyte integrins which interact with CYTIP through its PDZ domain. After membrane translocation, CYTIP can be re-located to the cytoplasm via exposure to a phorbol ester. Additionally, CYTIP associates with SNX27 (sorting nexin 27) and helps to coordinate trafficking and Signalling complexes. Up-regulation of CYTIP is observed in maturing dendritic cells, suggesting a possible role in developmentally-controlled cell adhesion.
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-11948R-CY7)
Fournisseur:
Bioss
Description:
Three mammalian fringe family members, Manic, Radical and Lunatic Fringe, have been identified as proteins related to Drosophila Fringe, a protein involved in development. Fringe proteins act upstream of the Notch signaling pathway and are involved in boundary determination during segmentation. Each mammalian Fringe displays different patterns of expression, though all are expressed in the mouse embryo as well as in many adult tissues. Radical Fringe, also known as Beta-1,3-N-acetylglucosaminyltransferase Radical Fringe, is a 331 amino acid single-pass type II membrane protein that localizes to the membrane of the Golgi apparatus. Playing a key role in the development of the limb bud, Radical Fringe transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor. Lunatic Fringe is required for normal somite segmentation and patterning and is thought to be a target of the molecular clock. Manic Fringe, also involved in somatic development, has been shown to render mouse NIH/3T3 cells tumorigenic in SCID mice.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7545R-FITC)
Fournisseur:
Bioss
Description:
High density lipoproteins (HDLs) play a critical role in cholesterol metabolism and their plasma concentrations are inversely correlated with risk for atherosclerosis. SR-BI and SR-BII (previously known as SR-BI.2) are the alternatively spliced products of a single gene. SR-BII and SR-BI are identical except for the encoded c-terminal cytoplasmic domain. Both SR-BI and SR-BII bind HDL and mediates selective uptake of HDL cholesteryl ester, but with SR-BII having an approximately 4-fold lower efficiency than SR-BI. SR-BI and SR-BII are expressed primarily in liver and non-placental steroidgenic tissues. Although the role of these scavenger receptors is not completely clear, SR-BII mRNA results from the alternative splicing of SR-BI precursor transcripts with both isoforms mediating selective transfer of lipid between HDL and cells. Therefore, the relative expression and functional activities of these two isoforms create a potential means of regulating selective lipid transfer between HDL and cells.
UOM:
1 * 100 µl
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