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Masterflex+Single-use
Numéro de catalogue:
(BOSSBS-6634R-CY7)
Fournisseur:
Bioss
Description:
Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6634R-A488)
Fournisseur:
Bioss
Description:
Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.
UOM:
1 * 100 µl
Numéro de catalogue:
(COPA414C)
Fournisseur:
Copan
Description:
The M40 Transystem line is the latest generation of traditional bacteriology transport swabs. It was designed to provide the ultimate performance capability with the most diverse range of fastidious aerobic and anaerobic bacteria including Neisseria gonorrhoeae, sustaining viability during transit or storage at room temperature and refrigerator temperatures for up to 48 hours (at least 24 hours for Neisseria gonorrhoeae).
UOM:
1 * 50 ST
Numéro de catalogue:
(115-2051)
Fournisseur:
KIMBERLY CLARK
Description:
These single ply wipes are made from AIRFLEX* material, a specialised fabric with a perfect balance of softness and strength, that is also thick and absorbent. Ideal for industrial tasks such as cleaning, process line wiping, soaking up large spills.
UOM:
1 * 1 ROU
Numéro de catalogue:
(BOSSBS-6737R-HRP)
Fournisseur:
Bioss
Description:
SVH may play a role in cell survival and cell growth and may suppress the transcriptional activity of p53/TP53. Cellular localization Endoplasmic; reticulum membrane; Single-pass membrane protein.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6737R-A647)
Fournisseur:
Bioss
Description:
SVH may play a role in cell survival and cell growth and may suppress the transcriptional activity of p53/TP53. Cellular localization Endoplasmic; reticulum membrane; Single-pass membrane protein.
UOM:
1 * 100 µl
Numéro de catalogue:
(444-2301)
Fournisseur:
IKA
Description:
Plateau (135×130 mm), Pour: 1 flacon non attaché 1 - 250 ml
UOM:
1 * 1 ST
Numéro de catalogue:
(SYNOGGNOME-XRQ-NPC)
Fournisseur:
Syngene (a division of the Synoptics group)
Description:
The Syngene GeneGnome XRQ is dedicated to chemiluminescence imaging. The system is built for high performance and automation and features a next generation high quantum efficiency CCD camera for even greater sensitivity. A very simple set-up process means a single click will automatically capture a quality image of any Western blot.
UOM:
1 * 1 ST
Numéro de catalogue:
(BOSSBS-5453R-HRP)
Fournisseur:
Bioss
Description:
The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.
UOM:
1 * 100 µl
Fournisseur:
Avantor
Description:
Prevail™ HPLC columns exhibit long column lifetime in both highly aqueous and highly organic mobile phases. All phases, apart from Prevail™ Carbohydrate ES are silica-based. The stability of these phases is such that a single column can be switched between highly aqueous for analysis of highly polar analytes and highly organic for strong retention of hydrophobic analytes.
Numéro de catalogue:
(BOSSBS-5150R-HRP)
Fournisseur:
Bioss
Description:
Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1545R-A750)
Fournisseur:
Bioss
Description:
Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodelling and degradation, in cell migration and many other physiopathological events. Plays a direct role in facilitating neuronal migration.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1545R-A350)
Fournisseur:
Bioss
Description:
Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodelling and degradation, in cell migration and many other physiopathological events. Plays a direct role in facilitating neuronal migration.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5009R-CY7)
Fournisseur:
Bioss
Description:
Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. Polymer of 16 chains, four each of alpha, beta, gamma, and delta. Alpha and beta are regulatory chains, gamma is the catalytic chain, and delta is calmodulin. The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5009R-A680)
Fournisseur:
Bioss
Description:
Phosphorylase b kinase catalyses the phosphorylation of serine in certain substrates, including troponin I. Polymer of 16 chains, four each of alpha, beta, gamma, and delta. Alpha and beta are regulatory chains, gamma is the catalytic chain, and delta is calmodulin. The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5009R-A647)
Fournisseur:
Bioss
Description:
Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. Polymer of 16 chains, four each of alpha, beta, gamma, and delta. Alpha and beta are regulatory chains, gamma is the catalytic chain, and delta is calmodulin. The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains.
UOM:
1 * 100 µl
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est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
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