10780 Results for: "2-Fluorophenyl+isocyanate&pageNo=32&view=list"

Supplier: witeg Labortechnik

Tubing threaded 46x130x3.2mm gl50 with screw threaded, straight,acc. to din 12216, with iso screw thread,made of borosilicate glass , available with screw thread gl, rd or svl null

Supplier: witeg Labortechnik

SQUIBB COUNTER BORO 500 ML NS 1 * 2 items

Supplier: asecos

drum pump, pp with hose and tap immersion depth 800 1 * 1 items

Supplier: asecos

drum pump, pp with hose and tap immersion depth 650 1 * 1 items

Supplier: Beckman Coulter

48-WELL FLOWERPLATE MF MTP 1 * 1 SET

Supplier: MACHEREY-NAGEL

Filter paper circles MN 85/90 32cm diameter, pack of 100. 1 * 100 items

Supplier: asecos

drum pump, pp with hose and tap immersion depth 500 1 * 1 items

Supplier: witeg Labortechnik

Tubing threaded 28x150x2.0mm gl32 with screw, straight,acc. to din 12216, with iso screw thread,made of borosilicate glass, availab le with screw thread gl, rd or svl null

Supplier: witeg Labortechnik

Tubing threaded 65x130x3.2mm gl70 with screw threaded, straight,acc. to din 12216, with iso screw thread,made of borosilicate glass , available with screw thread gl, rd or svl null

Supplier: witeg Labortechnik

Tubing threaded 40x150x3.2mm gl45 with screw threaded, straight,acc. to din 12216, with iso screw thread,made of borosilicate glass , available with screw thread gl, rd or svl null

Supplier: MACHEREY-NAGEL

Filter paper circles MN 85/70 32cm diameter, pack of 100. 1 * 100 items

Supplier: Hach

Robust and intuitive portable meters, instilling confidence in reporting and managing your results.

Supplier: GLASWARENFABRIK KARL HECHT

CENTRIFUGE TUBE 108MM 1 * 50 items

Supplier: NEXOPART

Test Sieve for cereals with stainless steel frame 200x32 mm, stainless steel-perforated plate with slot holes according to ISO 5223 1 * 1 items

Supplier: witeg Labortechnik

Tubing threaded 40x300x3.2mm gl45 with screw threaded, straight,acc. to din 12216, with iso screw thread,made of borosilicate glass , available with screw thread gl, rd or svl null

Supplier: VICI JOUR RESEARCH

TUBING, FEP, 1/8'' OD X 1.59 MM ID 1 * 3 m

Supplier: witeg Labortechnik

Tubing threaded 32x150x2.0mm svl30 with screw threaded straight,acc. to din 12216, with iso screw thread,made of borosilicate glass, available with screw thread gl, rd or svl 1 * 1 items

Supplier: Heidolph Instruments GmbH & Co.KG

Powerful electronic stirrers that feature a smooth start operation which prevents spills and splashing media. The speed ramps up slowly until set speed has been reached. Both models feature safe start and stop of operation via an intuitive glass slide touch panel to avoid accidental start-up. An overtemperature sensor shuts off the unit in dangerous heat-up situations, ideal for unattended continuous operation. All units are designed for continuous 24-hour operation, including challenging high viscosity applications in polymer research. High torque levels give better mixing results in less time, maintenance-free motors reduce repairs and down time. Hei-TORQUE Value 400 and Hei-TORQUE Precision 400 units have two speed gears.

Supplier: Thermo Scientific

The Heracell™ VIOS series has been designed for sensitive cultures like stem and primary cells in leading research, pharmaceutical and clinical applications. The units are available with either electropolished stainless steel or 100% pure copper interiors and have adjustable, perforated shelving, easy to clean corners with convenient access port and a reversible exterior door for added flexibility.

Supplier: Bioss

ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.

Supplier: Bioss

ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.

Supplier: Heidolph Instruments GmbH & Co.KG

Hei-VAP Expert Control rotary evaporators allow central control of all process parameters: Vacuum, cooling temperature, rotation and heating bath temperature. The units have separate knobs for quick access: Right for direct vacuum control, the left one for rotation has a lock function to prevent accidental adjustment

Supplier: GETINGE LIFE SCIENCES

RUBBER CAP D32MM 1 * 1 items

Supplier: Lenz Laborglas GmbH & CO.KG

TUBE CAPILLARY TYPE A NS29/32C 1 * 1 items

Supplier: MEMMERT

The range of cooled incubators have a temperature range from below zero up to 60 °C, units ensure rapid and precise heating up and cooling down times without energy intensive power bursts. All models have stainless steel inner chamber and housing, ensuring long working life and easy cleaning. These compressor cooled incubators have an integrated data logger and digital timer which is adjustable from one minute to 99 days and 23 hours.

Supplier: MEMMERT

The ICO series of CO₂ incubators has seamlessly welded, corrosion-resistant stainless steel chambers with rounded edges and no further installations, ensuring easy and thorough cleaning. Models have TwinDISPLAY with a USB port for uploading programs, reading out logs or protecting appliances via the user ID function, and an Ethernet interface as well as a data logger with a 10 year storage capacity. All parameters can be set directly in the ControlCOCKPIT or the AtmoCONTROL software, which uses drag and drop symbols to input values. Battery-buffered ControlCOCKPIT (optional): Operating display, logging and CO₂ control are fully functional even during a power failure.

Supplier: Bioss

ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.

Supplier: Bioss

ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.

Supplier: Bioss

ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.

Supplier: Bioss

ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.