Supplier: Abnova

Mouse monoclonal antibody raised against partial recombinant mouse Notch1. 1 * 100 µG

Supplier: Abnova

Mouse monoclonal antibody raised against partial recombinant mouse Notch1. 1 * 100 µG

Supplier: NEUBERT VOLUME GLASSWAERE

300 mm long 1 * 1 items

Supplier: AMBEED

tert-Butyl endo-3-amino-8-azabicyclo[3.2.1]octane-8-carboxylate,96% 1 * 1 g

Supplier: Abnova

Mouse monoclonal antibody raised against partial recombinant mouse Notch1. 1 * 100 µG

Supplier: Abnova

Mouse monoclonal antibody raised against partial recombinant mouse Notch1. 1 * 100 µG

Supplier: US Biological

GRO BETA MIP-2, MACROPHAGE INF PAB RB XR 1 * 50 µG

Supplier: MORGAN ADVANCED MATERIALS HALD

L 600 R10PYT 400 320 06000 1 * 1 items

Supplier: Abnova

Mouse monoclonal antibody raised against partial recombinant mouse Notch1. 1 * 100 µG

Supplier: Abnova

Mouse monoclonal antibody raised against partial recombinant mouse Notch1. 1 * 100 µG

Supplier: Abnova

Mouse monoclonal antibody raised against partial recombinant mouse Notch1. 1 * 100 µG

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: Abnova

Mouse monoclonal antibody raised against partial recombinant rat Slc38a1. 1 * 100 µG

Supplier: Abnova

Mouse monoclonal antibody raised against partial recombinant rat Slc38a1. 1 * 100 µG

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: MEMMERT

ADDITIONAL CHIP CARD, BLANK, null

Supplier: AMBEED

9-Bromo-1,2,3,5,6,7-hexahydropyrido[3,2,1-ij]quinoline,95% 1 * 5 g

Supplier: Avantor

GC COLUMN HI-WAX 0.32MM 0.20UM 50M 1 * 1 items

Supplier: Avantor

GC COLUMN HI-WAX 0.32MM 1.20 25M 1 * 1 items

Supplier: Abnova

Mouse monoclonal antibody raised against partial recombinant rat Slc38a1. 1 * 100 µG

Supplier: Edmund Bühler GmbH

Motor MQC 847 48V DC /5,4A / 235W 3200/min for VKS 1 * 1 items

Supplier: Abnova

Mouse monoclonal antibody raised against partial recombinant rat Slc38a1. 1 * 100 µG

Supplier: witeg Labortechnik

Flask for collecting 2l, 300x100mmmm, acc. to schlenk, null

Supplier: Abnova

Mouse monoclonal antibody raised against human HLA-A/HLA-B/HLA-C. 1 * 50 µG

Supplier: witeg Labortechnik

FLASK, PEAR SHAPE, 50 ML, 1 * 10 items

Supplier: VARIAN

Cp-Sil 5-Cb,M5 Cap Col 30Mx0.32Mmx0.25Um 1 * 1 items

Supplier: Abnova

Mouse monoclonal antibody raised against partial recombinant rat Slc38a1. 1 * 100 µG

Supplier: witeg Labortechnik

FLASK, PEAR SHAPE, 250 ML, 1 * 10 items