TRIP13 Protein, Human (His, Strep)

The TRIP13 protein plays a key role in meiosis, affecting chromosome reorganization and structural development. It is critical for the formation of crossing and noncrossing pathways, homologous synapses, and synaptonemal complexes. TRIP13 Protein, Human (His, Strep) is the recombinant human-derived TRIP13 protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of TRIP13 Protein, Human (His, Strep) is 432 a.a., .

TRIP13 Protein assumes a pivotal role in meiosis, contributing significantly to chromosome recombination and the development of chromosome structures. It is essential in the early stages of meiotic recombination, influencing both crossover and non-crossover pathways, and is critical for efficient homologous synapsis. Additionally, TRIP13 is required for the formation of higher-order chromosome structures and the development of the synaptonemal complex. In males, it is indispensable for the synapsis of sex chromosomes and the formation of sex bodies. TRIP13 plays a crucial role in promoting the early steps of the DNA double-strand breaks (DSBs) repair process by influencing the assembly of RAD51 complexes and facilitating the depletion of HORMAD1 and HORMAD2 from synapsed chromosomes. Beyond meiosis, TRIP13 is implicated in the activation of the mitotic spindle assembly checkpoint (SAC). It also exhibits specific interactions, including binding to the ligand binding domain of the thyroid receptor (TR) and interacting with HPV16 E1. Moreover, TRIP13 interacts with the proteasome subunit PSMA8, participating in meiosis progression during spermatogenesis.

Human

E. coli

N-Strep;N-6*His

Q15645 (M1-I432)

9319

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

<1 EU/μg, determined by LAL method.