protein

ATP2A2 Protein, Human (His)

HY-P72094

5 μg;10 μg;50 μg

52;90;250 USD

ATP2A2 Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg

52;90;250 USD

The ATP2A2 protein is a magnesium-dependent enzyme that hydrolyzes ATP and transfers calcium from the cytoplasm to the sarcoplasmic reticulum. It participates in autophagy during starvation and interacts with VMP1 to achieve ER isolating membrane contact. ATP2A2 Protein, Human (His) is the recombinant human-derived ATP2A2 protein, expressed by E. coli , with N-6*His labeled tag. The total length of ATP2A2 Protein, Human (His) is 443 a.a., with molecular weight of ~56 kDa.

Human

The ATP2A2 protein, a magnesium-dependent enzyme, catalyzes the hydrolysis of ATP, facilitating the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Beyond its role in calcium transport, ATP2A2 is implicated in autophagy response to starvation, where it interacts with VMP1 to control ER-isolation membrane contacts for autophagosome formation. Additionally, ATP2A2 modulates ER contacts with lipid droplets, mitochondria, and endosomes, showcasing its versatile involvement in cellular processes. In collaboration with FLVCR2, ATP2A2 mediates heme-stimulated switching from mitochondrial ATP synthesis to thermogenesis. It also serves as a crucial regulator of TNFSF11-mediated Ca(2+) signaling pathways, interacting with TMEM64 to activate CREB1 and induce mitochondrial ROS generation. This intricate network of interactions underscores ATP2A2's pivotal role in the regulation of cellular processes, ranging from calcium homeostasis to autophagy and osteoclast differentiation.

Atp2a2; ATP2B; ATPase Ca++ transporting cardiac muscle slow twitch 2; Calcium pump 2; ATPase 2

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

Lyophilized from a 0.2 μm sterile filtered PBS, 6% Trehalose, pH 7.4 or 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.