Anti-SERCA1 ATPase antibody [EPR7322]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

SERCA1 ATPase also known as sarco/endoplasmic reticulum Ca2+ ATPase 1 is an important enzyme responsible for the active transport of Ca2+ ions from the cytosol into the sarcoplasmic reticulum which is important for muscle relaxation. This protein has a molecular weight of about 110 kDa. SERCA1 ATPase predominantly expresses in fast-twitch skeletal muscle allowing these muscles to relax rapidly after contraction. The enzyme utilizes ATP to pump calcium ions which highlights its role as an ATPase protein and its functionality in maintaining calcium homeostasis.

Biological function summary

SERCA1 ATPase ensures proper calcium regulation and muscle function by facilitating the reuptake of Ca2+ ions into the sarcoplasmic reticulum following muscle contraction. It does not operate as part of a complex but plays a significant role in calcium ion translocation thereby regulating muscle contraction-relaxation cycles. This ATPase protein is directly involved in muscle physiology and its efficient function is critical for fast muscle fibers.

Pathways

SERCA1 ATPase is a significant component of the calcium signaling and muscle contraction pathways. In the context of muscle contraction the release and reuptake of Ca2+ ions regulated by SERCA1 ATPase are central events. The protein works closely with the ryanodine receptor (RyR) and calsequestrin which also participate in the modulation of intracellular calcium levels. Their interactions ensure precise coordination during muscle contraction and relaxation processes.

Associated diseases and disorders

Mutations or dysregulation of SERCA1 ATPase can lead to conditions such as Brody disease and certain forms of myopathy. Brody disease is characterized by impaired muscle relaxation which directly relates to the malfunctioning of this Ca2+ ATPase. Additionally the disrupted function of SERCA1 ATPase may also involve interactions with other proteins like the ryanodine receptor which can exacerbate muscle-related symptoms and contribute to the pathophysiology of these disorders.