Proteins & Enzymes

N-terminal GST-tagged, recombinant human XIAP full length, expressed by baculovirus in Sf21 insect cells UBE1 catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation. It is responsible for the primary

N-terminal GST-tagged, recombinant human XIAP full length, expressed by baculovirus in Sf21 insect cells UBE1 catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation. It is responsible for the primary

Produced from human cDNA, expressed in E. coli .

Product Source: N-terminal 6His-tagged recombinant human full-length ULK3. Expressed by baculovirus in Sf21 insect cells.

The Universal Protease Substrate provides rapid and highly sensitive detection of trace protease activity, or determination of the effectiveness of protease inhibition. Protease activity releases resorufin-labeled peptides from the patented

Unk-D-Trp-D-Asn-Asp-Thr(1)-Gly-Orn-Asp-D-Ala-Asp-Gly-D-Ser-Glu(3R-Me)-Asp(Ph(2-NH2))-(1).

Unk-Dab-Thr-Dab-Dab(1)-D-Dab-D-Phe-Leu-Dab-Dab-Thr-(1).Unk-Dab-Thr-Dab-Dab(2)-D-Dab-D-Phe-Leu-Dab-Dab-Thr-(2).H2SO4.

Uracil-DNA Glycosylase (UNG) contains the highly active recombinant form of the equally named enzyme found in prokaryotes and eukaryotes. It hydrolyzes uracil-glycosidic bonds in single- or double-stranded DNA, excising uracil and creating

Uracil-DNA Glycosylase, heat-labile contains the equally named enzyme found in the marine bacterium BMTU 3346. Like the UNG from E.

Uracil N-glycosylase (UNG enzyme), also known as uracil DNA glycosylase (UDG enzyme), is a recombinant enzyme expressed and purified in E. coli. The protein has a molecular weight of 25 kD and can catalyze the release of free uracil from single and

Analysis Note Appearance (clearness): clear Appearance (color): red pH-value (25&#8199&#176C): 6.6 - 7.

Synthetic peptide from rat VGLUT1 protein. VGLUT1 is expressed in a subset of glutamate neurons and transports glutamate into native synaptic vesicles from the brain, exhibiting a conductance for chloride that is blocked by glutamate.