Recombinant humaan TCP1-eiwit

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 protein is found in the cytosol as a subunit of a hetero-oligomeric chaperone. It has an important function in maintaining cellular homoeostasis by assisting the folding of many proteins, including the cytoskeletal components actin and tubulin. Recombinant human TCP1 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography.

T-complex protein 1 subunit alpha, CCT-alpha, CCT1, CCT, TCP-1-alpha

E.coli

Human

His-Tag

SDS-PAGE

0.5 mg/mL (determined by Bradford assay)

> 85% by SDS-PAGE

62.5 kDa (576aa) confirmed by MALDI-TOF

TCP1, T-complex protein 1 subunit alpha, CCT-alpha, CCT1, CCT, TCP-1-alpha, ATGP0768-10 µg, ATGP0768-20 µg, ATGP0768-50 µg, ATGP0768-100 µg, ATGP0768-250 µg, ATGP0768-500 µg, ATGP0768-1 mg, ATGP0768-10, ATGP0768-20, ATGP0768-50, ATGP0768-100, ATGP0768-250, ATGP0768-500, ATGP0768-1

Willison KR., et al. (2008) EMBO J. 27 (13) :1827-39; ; Kubota H., et al (2001) Eur J Biochem. 268 (17) :4664-73.;

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 0.1mM PMSF,10% glycerol

Heat Shock Proteins

NP_110379

P17987

Human

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