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

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.

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.

Human

E. coli Cell-free

N-6*His;N-SUMO

Q96BI3 (M1-D247)

51107

MGAAVFFGCTFVAFGPAFALFLITVAGDPLRVIILVAGAFFWLVSLLLASVVWFILVHVTDRSDARLQYGLLIFGAAVSVLLQEVFRFAYYKLLKKADEGLASLSEDGRSPISIRQMAYVSGLSFGIISGVFSVINILADALGPGVVGIHGDSPYYFLTSAFLTAAIILLHTFWGVVFFDACERRRYWALGLVVGSHLLTSGLTFLNPWYEASLLPIYAVTVSMGLWAFITAGGSLRSIQRSLLCKD

Observed band size: Monomer: 40 kDa Dimer: 90 kDa It is speculated that the protein forms a dimeric structure.

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

Lyophilized powder.

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.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add 5-50% of glycerol (final concentration). Our default final concentration of glycerol is 50%. Customers could use it as reference.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.