10875 Results for: "Perfluoro(2-butyltetrahydrofuran)&pageNo=32&view=list"

Supplier: MORGAN ADVANCED MATERIALS HALD

L 600 R10PYT 400 320 06000 1 * 1 items

Supplier: NEUBERT VOLUME GLASSWAERE

with 5mm bore 1 * 1 items

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: witeg Labortechnik

Flask for collecting 500ml, with cylindrical needle valve,st29/32,250x70mmmm, acc. to schlenk, null

Supplier: witeg Labortechnik

Flask for collecting 2l, with cylindrical hook,st29/32,300x100mmmm, acc. to schlenk, null

Supplier: Ahlstrom-Munksjö

General purpose Filter Paper, N°5H/N, 320 mm, discs 1 * 100 items

Supplier: Sartorius

FILTER FOLDED QAL/TECL GRADE 3MN 320MM 1 * 100 items

Supplier: witeg Labortechnik

Flask for collecting 100ml, with cylindrical needle valve,st29/32,165x40mmmm, acc. to schlenk, null

Supplier: witeg Labortechnik

WITO-REX-STIRRER-GUIDES, DGBM, CPL. 1 * 1 items

Supplier: VICI JOUR RESEARCH

S/Steel Nut Packed 5,Jour 1 * 5 items

Supplier: Aesculap

KNOCHENHALTEZANGE, SELBSTZENTR., 280 MM 1 * 1 ST

Supplier: Thermo Scientific

1-bromo-5,8,8-trimethyl-3-oxabicyclo[3.2.1]octane-2,4-dione, TECH 1 * 250 mg

Supplier: VARIAN

CPSIL 13 30M X 0.32MM 1UM GC COLUMN 1 * 1 items

Supplier: witeg Labortechnik

WITO-REX-STIRRER-GUIDES DGBM, COMPLETE, 1 * 1 items

Supplier: HWS LABORTECHNIK

PS-DECKEL DN150S 1 * 1 items

Supplier: Aesculap

KNOCHENHALTEZANGE N.LANE,320MM, M.SPERRE 1 * 1 ST

Supplier: Aesculap

OHRSPEKULUM N.TUMARKIN, D: 3,2MM,GESCHL. 1 * 1 ST

Supplier: NEUBERT VOLUME GLASSWAERE

tap NS 14,5 Bohr.4 mm + GL 14 1 * 1 items

Supplier: NEUBERT VOLUME GLASSWAERE

Doppelkugel, Tropfspitze ca. 200mm lang, Schenkelbreite 180-200mm 1 * 1 items

Supplier: NEUBERT VOLUME GLASSWAERE

COLUMN HEAD WITH REFLUX ADJUSTMENT 1 * 1 items

Supplier: VICI JOUR RESEARCH

Union,PEEK,hex-head nut short,1/16 1 * 6 items

Supplier: Thermo Orion

The Thermo Scientific™ Orion Star™ T910 pH titrators are designed to increase your laboratory productivity by automating titrations. Our core electrochemistry technology is integrated with a state-of-the-art reagent dispensing system to create modern, simplified automated titrators designed to make performing titrations easier, more reliable and more reproducible than manual titrations.

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: Ahlstrom-Munksjö

Micro-Glass Fiber Filters, MG 550 HA, 320 mm, discs 1 * 100 items

Supplier: BUCHI

Spider SJ29732 12xSJ14.5 1 * 1 items

Supplier: HWS LABORTECHNIK

HWS PLANSCHLIFFDECKEL, NW 100 1 * 1 items

Supplier: VITLAB

Volumetric flask, PFA, class A, with screw cap, PFA, 10 mL 1 * 2 items

Supplier: NEUBERT VOLUME GLASSWAERE

CENTR TUBE130ML 44X150MM GL32 W/O SC/CAP 1 * 1 items

Supplier: NEUBERT VOLUME GLASSWAERE

Boro 3.3,Trichter Kern mit Verlängerung oben mit Trichter 1 * 1 items