Profilin-2 Protein, Human

Profilin-2 protein is a key player in protein folding. It specifically binds to cytosolic chaperone protein (c-CPN) and promotes the transfer of target proteins. It also interacts with nascent polypeptide chains, helping unnatural proteins fold correctly in various competing pathways. Profilin-2 Protein, Human is the recombinant human-derived Profilin-2 protein, expressed by E. coli , with tag free. The total length of Profilin-2 Protein, Human is 140 a.a., with molecular weight of ~14.0 kDa.

PFDN2, a key player in protein folding, exhibits a specific binding affinity for cytosolic chaperonin (c-CPN), facilitating the transfer of target proteins to this complex. Additionally, PFDN2 interacts with nascent polypeptide chains, promoting their proper folding in an environment where various competing pathways for nonnative proteins exist. The heterohexameric structure of PFDN2 comprises two PFD-alpha type and four PFD-beta type subunits. Moreover, PFDN2 is an integral component of the PAQosome complex, collaborating with other members such as RUVBL1, RUVBL2, RPAP3, PIH1D1, PFDN6, PDRG1, UXT, URI1, ASDURF, POLR2E, and DNAAF10/WDR92 in the biogenesis of diverse protein complexes. Notably, the interaction between PFDN2 and URI1 is phosphorylation-dependent and exhibits a growth-dependent pattern, highlighting the intricate regulatory mechanisms involved in cellular processes.

Human

E. coli

Tag Free

P35080 (M1-F140)

5217  [NCBI]

MAGWQSYVDNLMCDGCCQEAAIVGYCDAKYVWAATAGGVFQSITPIEIDMIVGKDREGFFTNGLTLGAKKCSVIRDSLYVDGDCTMDIRTKSQGGEPTYNVAVGRAGRVLVFVMGKEGVHGGGLNKKAYSMAKYLRDSGF

Approximately 14.0 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.