10774 Results for: "TLC+Plates&pageNo=32&view=easy"

Supplier: LAT - Scientific Instruments

ohne Hahn 1 * 1 ST

Supplier: REITENSPIESS BUERSTEN

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

Supplier: HWS LABORTECHNIK

HWS-PS FLAT COVER DN 150 S 1 * 1 items

Supplier: Hettich

Block 192x0.2/0.4ml for A1161drum rotor for Mikro 22 1 * 1 items

Supplier: NEUBERT VOLUME GLASSWAERE

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

Supplier: NEUBERT VOLUME GLASSWAERE

DISTILLATION RETURN DIVIDER 1 * 1 items

Supplier: KARTELL

CAP RUBBER 25/32X34MM RED 1 * 1 items

Supplier: Roth Carl

Erlenmeyer flasks 1 * 6 items

Supplier: Roth Carl

DIALYSIS TUBING VISKING 1 * 152 m

Supplier: LAUDA

Integral T are process thermostats with an integrated cooling system for dynamic temperature control within external circuits.

Supplier: NEUBERT VOLUME GLASSWAERE

TUBE MEASURING WITH GLASS STOPCOCK 1 * 1 items

Supplier: NEUBERT VOLUME GLASSWAERE

FLANGE DECK PLAN DN120 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: 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: QVF LABORTECHNIK

FOUR-NECK PISTONS IN SPECIAL DESIGN 1 * 1 items

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: Roth Carl

Rotilabo-measuring beakers 1 * 1 items

Supplier: HWS LABORTECHNIK

FUNNEL POWDER Duran 1 * 1 items

Supplier: NEUBERT VOLUME GLASSWAERE

PLANT FLANGE COVER DN 200 5-SLEEVES 1 * 1 items

Supplier: Brand

These tips are manufactured under cleanroom conditions and are automatically packaged to ensure that the tips are consistently free from contamination.

Supplier: Roth Carl

DIALYSIS TUBING VISKING 1 * 152 m

Supplier: Roth Carl

Patent spanners 1 * 1 items

Supplier: Roth Carl

DIALYSIS TUBING VISKING 1 * 152 m

Supplier: Roth Carl

Drying tube 1 * 1 items

Supplier: Roth Carl

DIALYSIS TUBING VISKING 1 * 1 Roll

Supplier: Roth Carl

Vacuum adapters 1 * 1 items

Supplier: USA SCIENTIFIC PLASTICS

MULTI-RACK NEONGELB 40 STELLPLÄTZE 1 * 1 items

Supplier: Honeywell Safety

Glove Butyl Ambidex Black L 81cm S.9.75 1 Pair 1 * 2 PAIR

Supplier: VICI JOUR RESEARCH

PLUG, NYLON, COLUMN ENDSTOPPER GREEN 10 1 * 10 items