Anti-SERCA2 ATPase Rabbit Antibody [E19A2]

Catalog No.: F4007

    Application: Reactivity:

    Usage Information

    Dilution
    1:5000 - 1:10000
    1:50 - 1:100
    1:100 - 1:250
    1:100 - 1:1000
    Application
    WB, IHC, IF , FCM
    Reactivity
    Mouse, Rat, Human
    Source
    Rabbit
    Storage Buffer
    PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3
    Storage (from the date of receipt)
    -20°C (avoid freeze-thaw cycles), 2 years
    Predicted MW Observed MW
    115 kDa 115 kDa, 140 kDa
    *Why do the predicted and actual molecular weights differ?
    The following reasons may explain differences between the predicted and actual protein molecular weight.

    Datasheet & SDS

    Biological Description

    Specificity
    Anti-SERCA2 ATPase Rabbit Antibody [E19A2] detects endogenous levels of total SERCA2 ATPase protein.
    Clone
    E19A2
    Synonym(s)
    ATP2B, ATP2A2, Sarcoplasmic/endoplasmic reticulum calcium ATPase 2, SERCA2, SR Ca(2+)-ATPase 2, Calcium pump 2, Endoplasmic reticulum class 1/2 Ca(2+) ATPase
    Background
    SERCA2 (Sarco/Endoplasmic Reticulum Ca2+-ATPase 2) is a membrane-bound P-type ATPase predominantly expressed in cardiac and smooth muscle, where it plays a critical role in calcium homeostasis by actively pumping cytosolic Ca2+ into the sarco/endoplasmic reticulum (SR/ER), thus regulating muscle contraction and relaxation. SERCA2 contains ten transmembrane helices creating a channel for Ca2+ transport, along with three cytoplasmic domains (actuator, phosphorylation, and nucleotide-binding domains) responsible for ATP hydrolysis and conformational changes required for active transport. SERCA2 exists mainly as two isoforms, SERCA2a in cardiac muscle and SERCA2b in smooth muscle and non-muscle cells, with differences in their C-terminal sequences influencing their regulation and Ca2+ affinity. SERCA2's ATPase activity couples ATP hydrolysis to Ca2+ translocation, maintaining low cytosolic Ca2+ necessary for muscle relaxation. Its regulation is tightly controlled by accessory proteins such as phospholamban (PLB) and sarcolipin (SLN), which inhibit its Ca2+ affinity and ATPase activity; phosphorylation of PLB and SLN relieves this inhibition during muscle contraction. Post-translational modifications, luminal redox sensing via disulfide bonds, and isoform-specific intramolecular interactions further modulate SERCA2 activity. Dysregulation or decreased expression of SERCA2 is implicated in heart failure and other cardiac pathologies.
    References
    • https://pubmed.ncbi.nlm.nih.gov/35560336/
    • https://pubmed.ncbi.nlm.nih.gov/18006443/

    Tech Support

    Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

    Handling Instructions

    Tel: +1-832-582-8158 Ext:3
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