protein

APH1A Protein, Human (Cell-Free, His, SUMO)

HY-P702211

20 μg;50 μg

520;980 USD

APH1A Protein, Human (Cell-Free, His, SUMO)

proteins

E. coli Cell-free

20 μg;50 μg

520;980 USD

The APH1A protein is a noncatalytic subunit of the γ-secretase complex and is essential for the assembly of this endoprotease. The γ-secretase complex, including presenilin homodimer, nicastrin, APH1A, and PSENEN/PEN2, catalyzes the cleavage of intramembrane proteins such as Notch and APP. APH1A Protein, Human (Cell-Free, His, SUMO) is the recombinant human-derived APH1A protein, expressed by E. coli Cell-free , with N-6*His, N-SUMO labeled tag. The total length of APH1A Protein, Human (Cell-Free, His, SUMO) is 247 a.a., with molecular weight of 42.9 kDa.

Human

APH1A protein serves as a non-catalytic subunit within the gamma-secretase complex, an endoprotease assembly crucial for catalyzing the intramembrane cleavage of integral membrane proteins, including Notch receptors and APP (amyloid-beta precursor protein). Its involvement in gamma-secretase assembly is essential, contributing to the normal formation of this complex. The gamma-secretase complex, comprising a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B), and PSENEN/PEN2, plays a pivotal role in various cellular processes, such as Notch and Wnt signaling cascades, as well as the regulation of downstream events by processing key regulatory proteins. Additionally, it is implicated in modulating cytosolic CTNNB1 levels, highlighting its significance in diverse cellular pathways.

Gamma-secretase subunit APH-1A; Aph-1alpha; Presenilin-stabilization factor

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

Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 0.15 M NaCl, 0.05% FOS12, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.