TCP1 recombinant protein

TCP1, 1-556aa, Human, His tag, E Coli

Cat. Num. AAA203928

• Gene Names: TCP1; CCT1; CCTa; D6S230E; CCT-alpha; TCP-1-alpha
• Applications: SDS-Page
• Purity: > 80% by SDS-PAGE
• Synonyms: TCP1; 1-556aa; Human; His tag; E Coli; T-complex protein 1 subunit alpha; CCT-alpha; CCT1; CCT; TCP-1-alpha; TCP1 recombinant protein

• Host: E Coli
• Purity/Purification: > 80% by SDS-PAGE
• Form/Format: Liquid. In 20 mM Tris-HCl Buffer (pH 8.0) containing 1 mM DTT, 0.1 mM PMSF, 10% glycerol
• Concentration: 0.5 mg/ml (determined by Bradford assay) (varies by lot)
• 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
• Sequence Length: 556

• Applicable Applications for TCP1 recombinant protein: SDS-PAGE
• Antigen Species: Human
• Tag Information: His-tag
• Preparation and Storage: Can be stored at 4 degree C short term (1-2 weeks).; For long term storage, aliquot and store at -20 degree C or -70 degree C.; Avoid repeated freezing and thawing cycles.

SDS-Page

Related Product Information for TCP1 recombinant protein

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.

Product Categories/Family for TCP1 recombinant protein

Heat Shock Proteins

References

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

NCBI and Uniprot Product Information

• NCBI GI #: 57863257
• NCBI GeneID: 6950
• NCBI Accession #: NP_110379
• NCBI GenBank Nucleotide #: NM_030752.2
• UniProt Accession #: P17987; Q15556; Q5TCM3; E1P5B2
• Molecular Weight: 62.5 kDa (576aa) confirmed by MALDI-TOF
• NCBI Official Full Name: T-complex protein 1 subunit alpha isoform a
• NCBI Official Synonym Full Names: t-complex 1
• NCBI Official Symbol: TCP1
• NCBI Official Synonym Symbols: CCT1; CCTa; D6S230E; CCT-alpha; TCP-1-alpha
• NCBI Protein Information: T-complex protein 1 subunit alpha
• UniProt Protein Name: T-complex protein 1 subunit alpha
• Protein Family: T-complex protein
• UniProt Gene Name: TCP1
• UniProt Synonym Gene Names: CCT1; CCTA; TCP-1-alpha

NCBI Description

The protein encoded by this gene 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 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 folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene, encoding different isoforms, have been characterized. In addition, three pseudogenes that appear to be derived from this gene have been found. [provided by RefSeq, Jun 2010]

Uniprot Description

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin.