protein

PFDN5 Protein, Human (His)

HY-P76542

5 μg;10 μg;50 μg;100 μg

75;125;355;600 USD

PFDN5 Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg

75;125;355;600 USD

PFDN5 protein selectively binds to cytosolic chaperonin (c-CPN), facilitating targeted protein transfer and promoting nascent polypeptide folding. Beyond its chaperone function, PFDN5 regulates MYC transcriptional activity by forming a heterohexamer. It interacts with MYC's N-terminal domain, showcasing a multifaceted role in cellular processes, bridging protein folding and transcriptional regulation. PFDN5 Protein, Human (His) is the recombinant human-derived PFDN5 protein, expressed by E. coli , with N-His labeled tag. The total length of PFDN5 Protein, Human (His) is 154 a.a., with molecular weight of ~20 kDa.

Human

PFDN5 protein demonstrates targeted binding to cytosolic chaperonin (c-CPN), facilitating the transfer of specific proteins to this chaperone. Additionally, PFDN5 binds to nascent polypeptide chains, actively supporting their proper folding within a cellular environment teeming with competing pathways for nonnative proteins. Beyond its chaperone function, PFDN5 plays a regulatory role by repressing the transcriptional activity of MYC. Structurally, PFDN5 forms a heterohexamer comprising two PFD-alpha type and four PFD-beta type subunits. Notably, it engages in specific interactions with the N-terminal domain of MYC, suggesting a multifaceted role for PFDN5 in cellular processes, encompassing both protein folding and transcriptional regulation.

Prefoldin subunit 5; Myc modulator 1; PFDN5; MM1; PFD5

Greater than 90% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris, 300 mM NaCl, 5% trehalose, 5% mannitol and 0.01% Tween80, pH 7.4.

Room temperature in continental US; may vary elsewhere.