Procurou por: Transiluminadores+UV

Código de Artigo: (BOSSBS-6634R-CY5.5)

Fornecedor: Bioss

Descrição: 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

Promoção

Código de Artigo: (ORIOAQ8100)

Fornecedor: Thermo Orion

Descrição: Thermo Scientific™ Orion™ AquaMate UV-Vis spectrophotometers include over 260 preprogramed methods, and are designed to meet the needs of water and wastewater analysis laboratories. AquaMate UV-Vis and Visible-only spectrophotometers incorporate advanced features and functions for ultimate flexibility in operation.

UOM: 1 * 1 unid.

Promoção

Fornecedor: 3M

Descrição: SecureFit™ 400X safety glasses feature 3M™ Pressure Diffusion Temple Technology, wide flexible temple arms, and a combined soft nose bridge and brow guard. These lightweight safety glasses feature a clear, anti-scratch and superior anti-fog, rimless polycarbonate lenses.

Código de Artigo: (UVPA95-0253-02)

Fornecedor: UVP ULTRA VIOLET PRODUCTS

Descrição: Câmaras para visualização UV, Com dois tubos UV, Chromato-Vue®, C-75, 2×15 W, 254/365 nm

UOM: 1 * 1 unid.

Promoção

Código de Artigo: (BOSSBS-0527R-A555)

Fornecedor: Bioss

Descrição: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 3 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-0527R-FITC)

Fornecedor: Bioss

Descrição: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 3 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-6421R-FITC)

Fornecedor: Bioss

Descrição: This gene encodes one member of a family of translation repressor proteins. The protein directly interacts with eukaryotic translation initiation factor 4E (eIF4E), which is a limiting component of the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs. Interaction of this protein with eIF4E inhibits complex assembly and represses translation. This protein is phosphorylated in response to various signals including UV irradiation and insulin signaling, resulting in its dissociation from eIF4E and activation of mRNA translation. [provided by RefSeq, Jul 2008].

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-13016R)

Fornecedor: Bioss

Descrição: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-13016R-CY7)

Fornecedor: Bioss

Descrição: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-13016R-CY3)

Fornecedor: Bioss

Descrição: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-13016R-FITC)

Fornecedor: Bioss

Descrição: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-13016R-A680)

Fornecedor: Bioss

Descrição: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci.

UOM: 1 * 100 µl

Promoção

Fornecedor: Merck

Descrição: Placas TLC, sem modificação, sílica gel 60
Sílica gel 60 da Merck, com um ligante polimérico ímpar, que dá azo a uma superfície uniforme e dura que não se quebra nem empola com facilidade. O revestimento macio e extremamente denso da placa assegura bandas estreitas e uma eficiência de separação máxima, com o ruído de fundo mais baixo possível. Espessura da camada de 250 µm, partículas de 10 a 12 µm. Dois indicadores fluorescentes inorgânicos para detecção por UV de substâncias incolores.

MSDS

Código de Artigo: (BOSSBS-15482R-A750)

Fornecedor: Bioss

Descrição: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilise XPC. May protect XPC from proteasomal degradation. 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 recognises a wide spectrum of damaged DNA characterised 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 recognise 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

Promoção

Código de Artigo: (BOSSBS-15482R-CY5)

Fornecedor: Bioss

Descrição: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilise XPC. May protect XPC from proteasomal degradation. 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 recognises a wide spectrum of damaged DNA characterised 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 recognise 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

Promoção

Fornecedor: Thermo Fisher Scientific

Descrição: Accessory for UV/Visible spectrophotometers, Kit de tubos sobressalente para MiniSipper