15859 Results for: "4-(Benzyloxy)benzyl+bromide&pageNo=24&view=list"
RACK FLIPPER- 4-SEITIGPPNEONORANGE 1 * 1 items
Supplier: USA SCIENTIFIC PLASTICS
RACK FLIPPER- 4-SEITIGPPNEONORANGE 1 * 1 items
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FILTER FOLDED ANALYTICAL FAST SPONGY DIAMETER-240MM 1 * 100 items
Supplier: Sartorius
FILTER FOLDED ANALYTICAL FAST SPONGY DIAMETER-240MM 1 * 100 items
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53 components mix 1 * 2 Ampoul
Supplier: CUSTOM MADE CHEMICALS LAB
53 components mix 1 * 2 Ampoul
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RACK FLIPPER- 4-SEITIG PP RED 1 * 1 items
Supplier: USA SCIENTIFIC PLASTICS
RACK FLIPPER- 4-SEITIG PP RED 1 * 1 items
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RACK FLIPPER- 4-SEITIG PP ORANGE 1 * 1 items
Supplier: USA SCIENTIFIC PLASTICS
RACK FLIPPER- 4-SEITIG PP ORANGE 1 * 1 items
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RACK FLIPPER- 4-SEITIG PP BLUE 1 * 1 items
Supplier: USA SCIENTIFIC PLASTICS
RACK FLIPPER- 4-SEITIG PP BLUE 1 * 1 items
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Rack, flipper 1, colour orange, material PP, autoclavable, temperature resistant -90C to +120C, dimension 197x95x115mm, 8 holes di ameter 30mm, 20 holes diameter 20mm. 1 * 1 items
Supplier: KOEHLER TECHNISCHE PRODUKTEN
Rack, flipper 1, colour orange, material PP, autoclavable, temperature resistant -90C to +120C, dimension 197x95x115mm, 8 holes di ameter 30mm, 20 holes diameter 20mm. 1 * 1 items
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GLOVE DEXPURE 803-81 NITRILE PF XL 1 * 200 items
Supplier: HONEYWELL SAFETY
GLOVE DEXPURE 803-81 NITRILE PF XL 1 * 200 items
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Anti-hHR23b Rabbit Polyclonal Antibody
Supplier: Bioss
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.
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Anti-hHR23b Rabbit Polyclonal Antibody (ALEXA FLUOR® 555)
Supplier: Bioss
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.
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Rack, flipper 1, colour yellow, material PP, autoclavable, temperature resistant -90C to +120C, dimension 197x95x115mm, 8 holes di ameter 30mm, 20 holes diameter 20mm. 1 * 1 items
Supplier: KOEHLER TECHNISCHE PRODUKTEN
Rack, flipper 1, colour yellow, material PP, autoclavable, temperature resistant -90C to +120C, dimension 197x95x115mm, 8 holes di ameter 30mm, 20 holes diameter 20mm. 1 * 1 items
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Refrigerators, Compact, Midi
Supplier: GRAM
The unique air distribution system combined with a finned tube evaporator results in excellent temperature consistency for biostorage: the evaporator design eliminates the risk of 'cold walls', which can damage delicate items stored touching the sides of the cabinet. Whilst the air distribution system which directs the cold air down the rear of the cabinet and back up to the evaporator fan at the top, ensures a uniform temperature throughout.
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Rack, flipper 1, colour green, material PP, autoclavable, temperature resistant -90C to +120C, dimension 197x95x115mm, 8 holes dia meter 30mm, 20 holes diameter 20mm. 1 * 1 items
Supplier: KOEHLER TECHNISCHE PRODUKTEN
Rack, flipper 1, colour green, material PP, autoclavable, temperature resistant -90C to +120C, dimension 197x95x115mm, 8 holes dia meter 30mm, 20 holes diameter 20mm. 1 * 1 items
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Rack, flipper 1, colour blue, material PP, autoclavable, temperature resistant -90C to +120C, dimension 197x95x115mm, 8 holes diam eter 30mm, 20 holes diameter 20mm. 1 * 1 items
Supplier: KOEHLER TECHNISCHE PRODUKTEN
Rack, flipper 1, colour blue, material PP, autoclavable, temperature resistant -90C to +120C, dimension 197x95x115mm, 8 holes diam eter 30mm, 20 holes diameter 20mm. 1 * 1 items
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36 COMPONENTS MIX 1 * 2 items
Supplier: CUSTOM MADE CHEMICALS LAB
36 COMPONENTS MIX 1 * 2 items
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Mag-Bind® Fit24™ Blood and Tissue DNA Kit
Supplier: OMEGA BIO-TEK
Pre-scripted solution for purification of high-quality DNA from blood, saliva, cultured cells, or fresh or frozen tissue.
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Anti-hHR23b Rabbit Polyclonal Antibody (FITC)
Supplier: Bioss
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.
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Centrifuge Tube, Screw Thread,50ml, conical shaped bottom 1 * 12 items
Supplier: DWK Life Sciences
Centrifuge Tube, Screw Thread,50ml, conical shaped bottom 1 * 12 items
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AUTOCLAVE STERILIZATION BAG 12 X 24INCH 1 * 100 items
Supplier: BELLCO GLASS
AUTOCLAVE STERILIZATION BAG 12 X 24INCH 1 * 100 items
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Anti-hHR23b Rabbit Polyclonal Antibody (ALEXA FLUOR® 680)
Supplier: Bioss
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.
Expand 1 Items
Anti-hHR23b Rabbit Polyclonal Antibody (ALEXA FLUOR® 488)
Supplier: Bioss
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.
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Mag-Bind® cfDNA kit
Supplier: OMEGA BIO-TEK
The Mag-Bind® cfDNA Kit is designed for rapid and reliable isolation of circulating DNA from 500 to 4000 µl plasma or serum samples. The Mag-Bind® cfDNA Kit can be processed manually or with automated platforms. The procedure eliminates the need for funnels and vacuum steps, providing hands-free operation in automated protocols.
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LINDNER SILIBEADS TYP S 2.00-2.40 MM 1 * 1 kg
Supplier: SIGMUND LINDNER
LINDNER SILIBEADS TYP S 2.00-2.40 MM 1 * 1 kg
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Anti-hHR23b Rabbit Polyclonal Antibody (Cy7)
Supplier: Bioss
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.
Expand 1 Items
Anti-hHR23b Rabbit Polyclonal Antibody (ALEXA FLUOR® 647)
Supplier: Bioss
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.
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Genomic RNA purification kits, Fast RNA™ Pro Red kit, MP Biomedicals
Supplier: MP Biomedicals
FastRNA® Pro Red Kit is used to isolate total RNA from yeast and fungi. Isolated RNA is suitable for RT-PCR analysis and other downstream applications
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FILTER DISC CELLULOSE PAPER MODERATELY FAST DIAMETER-240MM 1 * 100 items
Supplier: Sartorius
FILTER DISC CELLULOSE PAPER MODERATELY FAST DIAMETER-240MM 1 * 100 items
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Anti-hHR23b Rabbit Polyclonal Antibody (Cy3)
Supplier: Bioss
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.
Expand 1 Items
Anti-hHR23b Rabbit Polyclonal Antibody (ALEXA FLUOR® 350)
Supplier: Bioss
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.
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Cubis® II MCA 225P Ultra-High Resolution Semi-Micro Balances
Supplier: Sartorius Balances
The Cubis® II laboratory balances are modular, therefore they allow to choose between applications and configurations which suit the best to the needs. These balances can be configured at the level of display, draftshields, software applications and hardware functions.