p-18

CYP11B2 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli.

Syntaxin-binding protein 1, also known as N-Sec1, Protein unc-18 homolog 1, MUNC18-1 and STXBP1, is a peripheral membrane protein that belongs to the STXBP / unc-18 / SEC1 family. STXBP1 is an evolutionally conserved neuronal Sec1/Munc-18 (SM) protein that is essential in synaptic vesicle release in several species. It may participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. STXBP1 is essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. It can interact with syntaxins 1, 2, and 3 but not syntaxin 4. STXBP1 may also play a role in determining the specificity of intracellular fusion reactions. Defects in STXBP1 are the cause of epileptic encephalopathy early infantile type 4 (EIEE4). Affected individuals have neonatal or infantile onset of seizures, suppression-burst pattern on EEG, profound mental retardation, and MRI evidence of hypomyelination.

EEF1E1, also known as AIMP3 and p18, is a multifunctional protein that localizes to both the cytoplasm and nucleus. In the cytoplasm, EEF1E1 is an auxiliary component of the macromolecular aminoacyl-tRNA synthase complex. It is comprised of a bifunctional glutamyl-prolyl-tRNA synthase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl and aspartyl-tRNA synthases, and three auxiliary proteins, EEF1E1/p18, AIMP2/p38 and AIMP1/p43. EEF1E1 also plays a positive role in ATM/ATR-mediated p53 activation.

TPPP2 Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 20.3 kDa and the accession number is AAH38970.1.

UBE2I is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation, ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction, and thereby the fate of the substrate, is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space, a highly sophisticated conjugation machinery has been developed. In a sequential manner, ubiquitin becomes activated by a ubiquitin-activating enzyme (E1), which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next, ubiquitin-loaded E2s are interacting with ubiquitin-protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system, wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans.

CTLA-4 Protein, Cavia porcellus, Recombinant (His) is expressed in P. pastoris yeast expression system with C-6xHis tag. The predicted molecular weight is 18-40 KDa and the accession number is H0VUB1.