TCP1 Human

T-Complex 1 Human Recombinant
Cat. No.
BT23485
Source
Escherichia Coli.
Synonyms
T-complex protein 1 subunit alpha, TCP-1-alpha, CCT-alpha, TCP1, CCT1, CCTA, D6S230E.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

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.

Product Specs

Introduction
TCP1, a member of the chaperonin containing TCP1 complex (CCT), also called the TCP1 ring complex (TRiC), functions as a molecular chaperone. This complex comprises two identical stacked rings, each containing eight distinct proteins. Unfolded polypeptides enter the complex's central cavity, where they undergo ATP-dependent folding. Found in the cytosol, TCP1 exists as a subunit of a hetero-oligomeric chaperone. It plays a crucial role in cellular homeostasis by assisting the folding of numerous proteins, including cytoskeletal components like actin and tubulin.
Description
Recombinant human TCP1, with a 20 amino acid His tag at the N-terminus, is produced in E. coli. This single, non-glycosylated polypeptide chain consists of 576 amino acids (1-556 a.a.) and has a molecular weight of 62.5 kDa. Purification of TCP1 is achieved using proprietary chromatographic techniques.
Physical Appearance
Sterile, colorless solution.
Formulation
The TCP1 solution (0.5 mg/ml) is supplied in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 0.1mM PMSF, and 10% glycerol.
Stability
For optimal storage, keep the vial at 4°C if using within 2-4 weeks. For extended periods, store frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 80.0%, as determined by SDS-PAGE analysis.
Synonyms
T-complex protein 1 subunit alpha, TCP-1-alpha, CCT-alpha, TCP1, CCT1, CCTA, D6S230E.
Source
Escherichia Coli.
Amino Acid Sequence

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.

Product Science Overview

Structure and Function

The CCT complex consists of two identical stacked rings, each containing eight different proteins . Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner . The complex is essential for the proper folding of various proteins, including actin and tubulin .

Gene and Expression

The gene encoding T-Complex 1 is located on chromosome 6 in humans . It is expressed in various tissues, with high expression levels in the testis, ovary, and other reproductive tissues . The protein is involved in several cellular processes, including protein folding, stabilization, and regulation of protein localization .

Recombinant T-Complex 1

Recombinant T-Complex 1 is produced using various expression systems, including Escherichia coli (E. coli), yeast, and wheat germ . The recombinant protein is often tagged with a GST tag for purification purposes . It is used in various research applications, including Western Blotting (WB), ELISA, and Affinity Purification (AP) .

Applications and Research

Recombinant T-Complex 1 is widely used in research to study protein folding mechanisms and interactions with other proteins . It has been shown to interact with several proteins, including PPP4C and HDAC3 . The protein is also involved in the regulation of macrophage apoptotic processes and telomere maintenance .

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