APH1A 蛋白, 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 蛋白作为 γ-分泌酶复合物中的非催化亚基，γ-分泌酶复合物是一种内切蛋白酶组装体，对于催化整合膜蛋白（包括 Notch 受体和 APP（淀粉样蛋白-β 前体蛋白））的膜内裂解至关重要。它参与γ-分泌酶组装至关重要，有助于该复合物的正常形成。γ-分泌酶复合物包含早老素同型二聚体（PSEN1 或 PSEN2）、尼卡斯特林 (NCSTN)、APH1（APH1A 或 APH1B）和 PSENEN/PEN2，在各种细胞过程中发挥着关键作用，例如 Notch 和 Wnt 信号级联，以及通过处理关键调节蛋白来调节下游事件。此外，它还参与调节胞质 CTNNB1 水平，突出了其在多种细胞途径中的重要性。

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.

无菌粉末.

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.