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Recombinant Human T-complex protein 1 subunit beta (CCT2)

Amino acids 2-535 form the expressed segment for recombinant Human CCT2. The expected molecular weight for the CCT2 protein is calculated to be 73.4 kDa. The CCT2 protein was expressed in e.coli. The N-terminal 6xHis-SUMO tag was fused into the coding gene segment of CCT2, making it easier to detect and purify the CCT2 recombinant protein in the later stages of expression and purification.T-complex protein 1 subunit beta (CCT2) is a crucial molecular chaperone in cells, primarily involved in the process of protein folding. Research on CCT2 plays a vital role in our understanding of protein folding and maintaining structural integrity within cells. In cancer research, the expression of CCT2 is associated with various types of tumors, particularly playing a significant role in the proliferation and invasion of tumor cells. Scientists aim to uncover the molecular mechanisms of CCT2 in cancer development, hoping to provide new targets for cancer treatment. Additionally, CCT2 is linked to research on neurological disorders. Its function in neurons may be related to the occurrence of neurodegenerative diseases. Scientists are working to gain a deeper understanding of the role of CCT2 in the nervous system, aiming to provide new clues for the treatment of related diseases.

ACP02437

Amino acids 2-535 form the expressed segment for recombinant Human CCT2. The expected molecular weight for the CCT2 protein is calculated to be 73.4 kDa. The CCT2 protein was expressed in e.coli. The N-terminal 6xHis-SUMO tag was fused into the coding gene segment of CCT2, making it easier to detect and purify the CCT2 recombinant protein in the later stages of expression and purification.T-complex protein 1 subunit beta (CCT2) is a crucial molecular chaperone in cells, primarily involved in the process of protein folding. Research on CCT2 plays a vital role in our understanding of protein folding and maintaining structural integrity within cells. In cancer research, the expression of CCT2 is associated with various types of tumors, particularly playing a significant role in the proliferation and invasion of tumor cells. Scientists aim to uncover the molecular mechanisms of CCT2 in cancer development, hoping to provide new targets for cancer treatment. Additionally, CCT2 is linked to research on neurological disorders. Its function in neurons may be related to the occurrence of neurodegenerative diseases. Scientists are working to gain a deeper understanding of the role of CCT2 in the nervous system, aiming to provide new clues for the treatment of related diseases.

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Specifications


Cat.No ACP02437 Target NameCCT2
FormLiquid or Lyophilized powderExpression SystemE.coli
Expression Range2-535aaMol Weight70.3 kDa
Protein LengthFull Length of Mature ProteinPurityGreater than 90% as determined by SDS-PAGE.
Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDP78371
Background Information
  • Uniprot Id

    P78371

  • Target Species

    Human

  • Target Name

    CCT2

  • Target Full Name

    T-complex protein 1 subunit beta

  • Target Function

    Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.

  • Target Subcellular Location

    Cytoplasm.

  • Target Protein Families

    TCP-1 chaperonin family

  • Target Research Area

    Signal Transduction

  • Target Synonyms

    99D8.1; CCT 2; CCT beta; CCT-beta; CCT2; CCTB; Chaperonin containing t complex polypeptide 1 beta subunit; Chaperonin containing t complex polypeptide 1 subunit 2; Chaperonin containing TCP1 subunit 2; Chaperonin containing TCP1 subunit 2 (beta); CTP:phosphocholine cytidylyltransferase 2; Epididymis secretory sperm binding protein Li 100n; HEL S 100n; MGC142074; MGC142076; MGC94480; PRO1633; T complex protein 1 beta subunit; T complex protein 1 subunit beta; T-complex protein 1 subunit beta; TCP 1 beta; TCP-1-beta; TCPB_HUMAN

  • Target Background

    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. Two transcript variants encoding different isoforms have been found for this gene.

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