protein

CCT2 Protein, Human (His-SUMO)

HY-P72120

5 μg;10 μg;50 μg

95;160;450 USD

CCT2 Protein, Human (His-SUMO)

proteins

E. coli

5 μg;10 μg;50 μg

95;160;450 USD

The CCT2 protein is an important component of the chaperone-containing T complex (TRiC), a molecular chaperone that assists in protein folding through ATP hydrolysis. CCT2 Protein, Human (His-SUMO) is the recombinant human-derived CCT2 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.

Human

CCT2 operates as an integral component of the chaperonin-containing T-complex (TRiC), a sophisticated molecular chaperone complex pivotal for protein folding through ATP hydrolysis. This versatile complex plays a crucial role in mediating the folding of various proteins, including WRAP53/TCAB1, thus influencing telomere maintenance. Furthermore, as part of the TRiC complex, CCT2 may contribute to the assembly of the BBSome, a complex essential for ciliogenesis that regulates the transport of vesicles to cilia. The TRiC complex's involvement in the folding of actin and tubulin underscores its multifaceted functions in cellular processes (Probable). Structurally, CCT2 is a key constituent of the TRiC complex, a heterooligomeric assembly characterized by two stacked rings, each measuring 12 to 16 nm in diameter. Beyond its structural role, CCT2 engages in interactions with various proteins, including PACRG, FLCN, and DLEC1, further highlighting its significance in diverse cellular processes.

99D8.1; CCT 2; CCT beta; CCT-beta; CCT2; CCTB; Chaperonin containing t complex polypeptide 1 beta subunit; Chaperonin containing TCP1 subunit 2 beta; ; 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

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm solution of 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.