ARP3/ACTR3 Protein, Human (sf9, His-GST)

ARP3/ACTR3 Proteinas, an ATPase preferentially stimulated by single-stranded DNA, crucially participates in homologous recombination repair (HRR). Independent of its ATPase function, it exhibits DNA-binding activity. SWSAP1 forms a functional complex with ZSWIM7, contributing to HRR and mutual protein stabilization. It also interacts with key players in HRR, including RAD51, RAD51B, RAD51C, RAD51D, and XRCC3, emphasizing its role in facilitating DNA repair through homologous recombination mechanisms. ARP3/ACTR3 Protein, Human (sf9, His-GST) is the recombinant human-derived ARP3/ACTR3 protein, expressed by Sf9 insect cells, with N-His, N-GST labeled tag. The total length of ARP3/ACTR3 Protein, Human (sf9, His-GST) is 417 a.a., with molecular weight of ~75.1 KDa.

SWSAP1 is an ATPase preferentially stimulated by single-stranded DNA, playing a crucial role in homologous recombination repair (HRR). This protein exhibits DNA-binding activity independent of its ATPase function. It forms a functional complex with ZSWIM7, contributing to homologous recombination repair and mutual stabilization of the proteins. SWSAP1 also interacts with key players in the homologous recombination repair process, including RAD51, RAD51B, RAD51C, RAD51D, and XRCC3. These interactions highlight the involvement of SWSAP1 in facilitating the repair of DNA through homologous recombination mechanisms.

Human

Sf9 insect cells

N-His;N-GST

P61158 (A2-S418)

10096  [NCBI]

Approximately 75.1 kDa.

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

Solution.

Supplied as a 0.2 μm filtered solution of 20 mM Tris, 500 mM NaCl, pH 7.4, 10% Glycerol, 3 mM DTT. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

<1 EU/μg, determined by LAL method.

N/A.

Stored at -80°C for 1 year. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.