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Product Image-VERN760520

Versilic™ Tubings, Silicone

Producent: Saint Gobain Life Sciences
Opis: This tubing meets European Pharmacopoeia requirements for silicone elastomer for closures and tubing, USP Class VI biological tests and ISO 10993 biocompatibility (systemic toxicity, irritation, sensitisation, citotoxicity, hemocompatibility and Ames test).

Product Image-SCTS2011200

Hełmy ochronne, typ 300

Numer katalogowy: (SCTS2011200)
Producent: SCOTT SAFETY
Opis: The Style 300 is a stylish, lightweight and comfortable safety helmet design. Manufactured from UV stabilised, high density polyethylene and available in either an eight-point terylene or four-point plastic head gear, Style 300 is a durable, well balanced safety helmet for all day comfort.
j.m.: 1 * 1 SZT
Image Unavailable-UVPA34-0016-01

Akcesoria do lamp akumulatorowych UV

Producent: UVP ULTRA VIOLET PRODUCTS
Opis: Replacement filter, Do: Rechargeable UV lamp, UVS-26P

Image Unavailable-BOSSBS-15482R-HRP

Anti-hHR23b Rabbit Polyclonal Antibody (HRP)

Numer katalogowy: (BOSSBS-15482R-HRP)
Producent: Bioss
Opis: 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.
j.m.: 1 * 100 µl
Image Unavailable-BOSSBS-15482R-CY3

Anti-hHR23b Rabbit Polyclonal Antibody (Cy3)

Numer katalogowy: (BOSSBS-15482R-CY3)
Producent: Bioss
Opis: 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.
j.m.: 1 * 100 µl
Image Unavailable-BOSSBS-15482R-A350

Anti-hHR23b Rabbit Polyclonal Antibody (ALEXA FLUOR® 350)

Numer katalogowy: (BOSSBS-15482R-A350)
Producent: Bioss
Opis: 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.
j.m.: 1 * 100 µl
Image Unavailable-BOSSBS-6634R-A488

Anti-XPC Rabbit Polyclonal Antibody (Alexa Fluor® 488)

Numer katalogowy: (BOSSBS-6634R-A488)
Producent: Bioss
Opis: 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.
j.m.: 1 * 100 µl
Image Unavailable-BOSSBS-6634R-CY7

Anti-XPC Rabbit Polyclonal Antibody (Cy7®)

Numer katalogowy: (BOSSBS-6634R-CY7)
Producent: Bioss
Opis: 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.
j.m.: 1 * 100 µl
Product Image-MMMASF403SGAF-YEL

Okulary ochronne, seria SecureFit™ 400

Producent: 3M
Opis: SecureFit™ safety glasses feature 3M™ Pressure Diffusion Temple Technology, wide flexible temple arms, soft adjustable nose pads, and a grey anti-scratch and superior anti-fog, rimless polycarbonate lenses. These lightweight glasses are suitable for indoor or outdoor use.

Image Unavailable-13051.36

Calcium wolframate ≥98%

Producent: Thermo Fisher Scientific
Opis: Calcium wolframate ≥98%

MSDS Certyfikaty

Product Image-UVPA95-0020-05

Szafki z podglądem, Chromato-Vue®, C-70G, UVP

Numer katalogowy: (UVPA95-0020-05)
Producent: UVP ULTRA VIOLET PRODUCTS
Opis: The large, lightweight plastic UV Chromato-Vue® viewing cabinet C-70G is designed for examining fluorescent samples in a fully lit environment.
j.m.: 1 * 1 SZT
Product Image-630-3175

Mikroskopy pionowe, DM 1000 LED

Producent: LEICA MICROSYSTEMS
Opis: The DM1000 LED laboratory microscope is perfect for clinical laboratory applications; histology, cytology, haematology and pathology.

Product Image-216-0980

Pojemniki na próbki z zakrętką, Bijou, WHEATON®

Producent: DWK Life Sciences
Opis: PS clear, with PE screw cap.

Image Unavailable-BOSSBS-15482R

Anti-hHR23b Rabbit Polyclonal Antibody

Numer katalogowy: (BOSSBS-15482R)
Producent: Bioss
Opis: 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.
j.m.: 1 * 100 µl
Image Unavailable-BOSSBS-15482R-A555

Anti-hHR23b Rabbit Polyclonal Antibody (ALEXA FLUOR® 555)

Numer katalogowy: (BOSSBS-15482R-A555)
Producent: Bioss
Opis: 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.
j.m.: 1 * 100 µl
Image Unavailable-BOSSBS-6634R-A350

Anti-XPC Rabbit Polyclonal Antibody (Alexa Fluor® 350)

Numer katalogowy: (BOSSBS-6634R-A350)
Producent: Bioss
Opis: 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.
j.m.: 1 * 100 µl
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Zapasy tego artykułu są ograniczone, ale możliwe, że jest on dostępny w pobliskim magazynie. Upewnij się, że jesteś zalogowany na stronie, aby móc sprawdzić dostępność zapasów. Jeśli call ciągle się wyświetla i potrzebujesz pomocy, zadzwoń na 58 323 82 00.
Ten produkt jest ograniczony w dostępie i można go zamówić tylko przy użyciu zaaprobowanego konta. Jeśli potrzebujesz pomocy, napisz do Działu Prawnego VWR na tomasz.chrobak@pl.vwr.com
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Produkt oryginalny został wycofany. Dostępny jest wskazny zamiennik .
Wybrany produkt został wycofany - sprzedaż do wyczerpania zapasów. Dostępne zamienniki można znaleźć poprzez wpisanie powyższego numeru katalogowego VWR w okno wyszukiwarki. Jeśli potrzebujesz dalszej pomocy, prosimy o kontakt z Działem Doradztwa Produktowego pod numerem telefonu 58 3238 220.
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