Recombinant Human T-Complex 1

Source : Escherichia Coli. TCP1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 576 amino acids (1-556 a.a.) and having a molecular mass of 62.5kDa. The TCP1 is purified by proprietary chromatographic techniques. TCP1 is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC) . This complex consists of 2 identical stacked rings, each containing eight different proteins. Unfolded polypeptides penetrate the central cavity of the complex and are folded in an ATP-dependent manner. The TCP1 protein is found in the cytosol as a subunit of a hetero-oligomeric chaperone. TCP1 has a significant function in maintaining cellular homoeostasis by assisting the folding of many proteins such as the cytoskeletal components actin and tubulin.

Product Specifications

Product Name Alternative

T-complex protein 1 subunit alpha||TCP-1-alpha||CCT-alpha||TCP1||CCT1||CCTA||D6S230E.

Purification

Greater than 80.0% as determined by SDS-PAGE.

Components

The TCP1 solution (0.5 mg/mL) contains 20mM Tris-HCl Buffer (pH 8.0), 1mM DTT, 0.1mM PMSF and 10% Glycerol.

Storage Conditions

TCP1 should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA) . Please prevent freeze-thaw cycles.

Amino Acids

MGSSHHHHHH SSGLVPRGSH MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG YRLACKEAVR YINENLIVNT DELGRDCLIN AAKTSMSSKI IGINGDFFAN MVVDAVLAIK YTDIRGQPRY PVNSVNILKA HGRSQMESML ISGYALNCVV GSQGMPKRIV NAKIACLDFS LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF VEAGAMAVRR VLKRDLKRIA KASGATILST LANLEGEETF EAAMLGQAEE VVQERICDDE LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER KNLKWIGLDL SNGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD KHGSYEDAVH SGALND.