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PS-DECKEL DN150S 1 * 1 items

Supplier: NEUBERT VOLUME GLASSWAERE

FLAT FLANGE LID DN 150 1 * 1 items

Supplier: NEUBERT VOLUME GLASSWAERE

COLUMN HEAD WITH REFLUX ADJUSTMENT 1 * 1 items

Supplier: Bohlender

Ground Joint glAdaptors, Black screw cap made of PPS with gl45 thread, movable insert with ground joint made of PTFE. Transition fro m a ground joint to a glass thread. The body can be turned independently from the screw cap. The completely assembled 1 * 1 items

Supplier: VICI JOUR RESEARCH

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

Supplier: HWS LABORTECHNIK

DISTILLATION OF DURAN LENGTH 115 MM 1 * 1 items

Supplier: Ahlstrom-Munksjö

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

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[EN]STUTZER SPLASH HEADS STRAIGHT C+H29/ 1 * 1 ST

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400X100XØ32 PIG BR., BUNDLE, PLASTIC HOSE 1 * 10 items

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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

Supplier: LAT - Scientific Instruments

ohne Hahn 1 * 1 ST

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: APG Europe

BOTTLE INFUSION 500ML TYPE1 32MM BROWN 1 * 35 items

Supplier: WATSON MARLOW

[EN]HOSE PUMP 205U/CA32 SERIES200 MAX RP 1 * 1 ST

Supplier: Hettich

Block 192x0.2/0.4ml for A1161drum rotor for Mikro 22 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: NEUBERT VOLUME GLASSWAERE

DISTILLATION RETURN DIVIDER 1 * 1 items

Supplier: KARTELL

CAP RUBBER 25/32X34MM RED 1 * 1 items

Supplier: NEUBERT VOLUME GLASSWAERE

TUBE MEASURING WITH GLASS STOPCOCK 1 * 1 items

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FOUR-NECK PISTONS IN SPECIAL DESIGN 1 * 1 items

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FOR-MET-ALA-SER-OH,,C12H21N3O6S,17351-3 1 * 250 mg

Supplier: BACHEM BIOCHEMICA

FOR-MET-ALA-SER-OH,,C12H21N3O6S,17351-3 1 * 50 mg

Supplier: Roth Carl

Erlenmeyer flasks 1 * 6 items

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DIALYSIS TUBING VISKING 1 * 152 m

Supplier: Roth Carl

Discharge pipes 1 * 1 items

Supplier: Thermo Scientific

1,8,8-trimethyl-3-oxabicyclo[3.2.1]octane-2,4-dione, TECH 1 * 1 g

Supplier: NEUBERT VOLUME GLASSWAERE

PLANT FLANGE COVER DN 200 5-SLEEVES 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.