ATP2A1 Protein, Human (Cell-Free, His)

ATP2A1 is critical for striated muscle function, acting as the primary Ca(2+) ATPase to efficiently reuptake cytosolic Ca(2+) into the sarcoplasmic reticulum. Through ATP hydrolysis, ATP2A1 transfers calcium from the cytoplasm to the sarcoplasmic reticulum lumen, which is critical for precise control of calcium levels, regulation of isolation, and control of muscle excitation and contraction dynamics. ATP2A1 Protein, Human (Cell-Free, His) is the recombinant human-derived ATP2A1 protein, expressed by E. coli Cell-free, with N-10*His labeled tag.

ATP2A1, a pivotal player in striated muscle function, serves as the primary Ca(2+) ATPase responsible for the efficient reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Operating through the hydrolysis of ATP, ATP2A1 facilitates the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen, a process crucial for the regulation of calcium sequestration and the intricate dynamics of muscular excitation and contraction. This intricate molecular mechanism highlights the indispensable role of ATP2A1 in orchestrating the precise control of calcium levels within muscle cells, ultimately contributing to the overall performance and functionality of striated muscles.

Human

E. coli Cell-free

N-10*His

O14983 (E10-E450)

784

Partial

EECLAYFGVSETTGLTPDQVKRNLEKYGLNELPAEEGKTLWELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILIANAIVGVWQERNAENAIEALKEYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILAIKSTTLRVDQSILTGESVSVIKHTEPVPDPRAVNQDKKNMLFSGTNIAAGKALGIVATTGVGTEIGKIRDQMAATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWFRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCKMFIIDKVDGDICLLNEFSITGSTYAPEGEVLKNDKPVRPGQYDGLVELATICALCNDSSLDFNEAKGVYEKVGEATETALTTLVE

Approximately 50 kDa,based on SDS-PAGE under reducing conditions.

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

<1 EU/μg, determined by LAL method.