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Single-use+Temperature+Sensor
Numéro de catalogue:
(BOSSBS-1210R-A647)
Fournisseur:
Bioss
Description:
Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1210R-FITC)
Fournisseur:
Bioss
Description:
Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1922R-CY5.5)
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
Numéro de catalogue:
(BOSSBS-3271R)
Fournisseur:
Bioss
Description:
c-Met, a member of the tyrosine kinase superfamily, is the receptor for hepatocyte growth factor, also known as scatter factor (HGF/SF). The mature c-Met protein is a disulfide-linked heterodimer with Mr=190 kDa composed of a heavily glycosylated alpha subunit that is completely extracellular in localization, and a beta subunit comprising an extracellular ligand binding domain, a single transmembrane domain, and a cytoplasmic tyrosine kinase domain. Cells expressing c-Met include epithelial cells, endothelial cells, blood cells of various types, and glomerular mesenchymal cells.HGF/SF binding to c-Met stimulates receptor dimerization and the phosphorylation of numerous residues within the receptor’s cytoplasmic domain. Signaling proteins that are phosphorylated and/or localized in response to c-Met phosphorylation include: Grb2, Shc, Cbl, Crk, cortactin, paxillin, GAB1, PI3K, FAK, Src, Ras, ERK1 and 2, JNK, PLC gamma, AKT, and STAT3. HGF/SF stimulation of c-Met expressing cells enhances proliferation, migration, morphogenesis, and protease synthesis, characteristics that are associated with invasive cell phenotype. Many types of cancer exhibit sustained c-Met stimulation, overexpression, or mutation, including carcinomas of the colon, breast, ovary, lung, liver, prostate, thyroid, kidney, as well as melanomas and sarcomas. In addition to cancer studies, other research areas in which c-Met is under investigation include organogenesis, organ regeneration, angiogenesis and surgical wound healing.
UOM:
1 * 100 µl
Numéro de catalogue:
(462-0303)
Fournisseur:
VWR Collection
Description:
Kit de dérivation pour températures élevées, tubes Viton®, 1/2" DI×6" avec ressort et 2 attaches de tuyaux, –32 à 200 °C
UOM:
1 * 1 ST
Fournisseur:
Brady
Description:
Cold temperature tape permanently adheres to surfaces at temperatures as low as −10 °F.
Fournisseur:
SWANN-MORTON
Description:
These Dermatome blades are fitted into a handheld instrument which resembles an electric razor. The blade oscillates and the movement back and forth will "evenly" skim off the surface layers of skin. Electric Dermatomes are preferable for cutting thinner and longer strips of skin with a more homogeneous thickness.
Numéro de catalogue:
(BOSSBS-2927R-A488)
Fournisseur:
Bioss
Description:
OXSR1 is a serine/threonine kinase which regulates downstream kinases in response to environmental stress such as osmotic stresses, notably sorbitol and, to a lesser extent, NaCl. OXSR1 phosphorylated thr84 within the N-terminal regulatory domain of PAK1. Replacement of thr84 with gln reduced activation of PAK1 by an active form of the small G protein CDC42, suggesting that phosphorylation by OXSR1 modulates the G protein sensitivity of PAK. OXSR1 interacts with chloride channel proteins SLC12A6 isoform 2, SLC12A1 and SLC12A2 but not with SLC12A4 and SLC12A7, possibly establishing sensor/signaling modules that initiate the cellular response to environmental stress. Binds to and phosphorylates RELL1, RELL2 AND RELT. OXSR1 may have a role in regulating the actin cytoskeleton.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11623R-CY7)
Fournisseur:
Bioss
Description:
PIRT is a 137 amino acid multi-pass membrane protein. Highly conserved among vertebrates, PIRT consists of two transmembrane domains and one putative C-terminal phosphoinositide-binding domain. Although PIRT is expressed in peripheral nervous system, with highest levels in dorsal root ganglion and trigeminal neurons, and lowest levels in sympathetic and enteric neurons, it is not expressed in spinal cord. PIRT is a required component of the VR1 complex, which positively regulates VR1, a sensor of both noxious heat and capsaicin. Correspondingly, PIRT knockout results in impaired responses to noxious heat and capsaicin exposure, while VR1 remains unaltered. The gene that encodes PIRT maps to human chromosome 17p13.1.
UOM:
1 * 100 µl
Fournisseur:
SGE a Trajan company
Description:
Septa, BTO premium high-temperature septa, Ø: 9,5 mm, Temp. max.: 400 °C
Numéro de catalogue:
(444-0004)
Fournisseur:
VWR Collection
Description:
Agitateur Vortex convenant à un petit conteneur de 30 mm de diamètre maximum, par exemple des tubes à essais, tubes à centrifuger et microtubes. La partie supérieure du boîtier est en PP et la surface pour tube à essai est recouverte de plastique TPU inerte, la partie inférieure étant en zinc moulé sous pression.
UOM:
1 * 1 ST
Fournisseur:
MAXX
Description:
NTC sensor for PB150, Pour: Spare part
Numéro de catalogue:
(MEMMB04359SF110PLS)
Fournisseur:
MEMMERT
Description:
Égouttoir inférieur (peut avoir une incidence sur la répartition de la température), Pour: SF 110 Plus
UOM:
1 * 1 ST
Fournisseur:
WTW ONLINE
Description:
Exchange membrane heads for DO sensors TriOxmatic® 600, 690, 700, 700 IN, Pour: TriOxmatic®, Sonde à oxygène dissous
Fournisseur:
Binder
Description:
Calibration certificate, temperature - for temperature, measurement in center of chamber at specified temperature, Pour: KB ECO
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
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