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anti-Human ATP2A2 Antibodies:
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Human Polyclonal ATP2A2 Primary Antibody for ChIP, IP - ABIN151703
Emter, McCune, Sparagna, Radin, Moore: Low-intensity exercise training delays onset of decompensated heart failure in spontaneously hypertensive heart failure rats. in American journal of physiology. Heart and circulatory physiology 2005
Show all 12 Pubmed References
Amphibian Monoclonal ATP2A2 Primary Antibody for FACS, ICC - ABIN152736
Asahi, Kurzydlowski, Tada, MacLennan: Sarcolipin inhibits polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2+-ATPases (SERCAs). in The Journal of biological chemistry 2002
Show all 11 Pubmed References
Amphibian Monoclonal ATP2A2 Primary Antibody for BP, ELISA - ABIN152688
Sharp, McPherson, Dawson, Aoki, Campbell, Snyder: Differential immunohistochemical localization of inositol 1,4,5-trisphosphate- and ryanodine-sensitive Ca2+ release channels in rat brain. in The Journal of neuroscience : the official journal of the Society for Neuroscience 1993
Show all 16 Pubmed References
Human Polyclonal ATP2A2 Primary Antibody for IHC (p), WB - ABIN3044280
Guo, Zeng, Zhang, Zhang, Li, Wu, Guan, Liu, Zhang, Li, Wan: Extracellular matrix of mechanically stretched cardiac fibroblasts improves viability and metabolic activity of ventricular cells. in International journal of medical sciences 2013
Atp2a2/serca2 is found in a larger subset of cells, but is not ubiquitous as reported in adults.
the genomic organization and the equine ATP2A2 coding sequence and an association analysis for chronic pastern dermatitis using a sample of South German draft horses
alpha-synuclein aggregates bind SERCA and stimulate its activity. Reducing SERCA activity is neuroprotective.
Mutation in SERCA2b gene is associated with Darier disease.
SGK3 a kinase transcriptionally regulated by estrogen receptor alpha (ERalpha) in breast cancer, sustains ERalpha signaling and drives the acquired aromatase inhibitors resistance by protecting against endoplasmic reticulum (EnR) stress-induced ERalpha downregulation and cell death through preserving SERCA2b function.
Darier disease (DD) is a rare autosomal dominant skin disorder due to mutations in the ATP2A2 gene.
SERCA2a gene transfer significantly improves left ventricle function and dimensions in doxorubicin-induced cardiomyopathy, suggesting LV-SERCA2a gene transfer an attractive treatment modality for doxorubicin-induced heart failure.
Studies indicate that Darier disease (DD) is caused by mutations in the ATP2A2 gene, whereas the ATP2C1 gene is associated with Hailey-Hailey disease (HHD).
Taken together, these results suggest that SERCA2 contributes to the migration of CCL21-activated Dendritic Cells as an important feature of the adaptive immune response and provide novel insights regarding the role of SERCA2 in Dendritic Cells functions.
Novel mutations in Darier disease and association to self-reported disease severity
VMP1 modulates SERCA2 activity to control endoplasmic reticulum contacts for autophagosome formation.
The left atrium / right atrium expression ratio was significantly increased in Atrial fibrillation for SERCA2 - gene related to calcium uptake and release, and located on the sarcoplasmic reticulum membrane.
Loss of SERCA2 impairs ER-to-Golgi transport of nascent DC.
We propose that the increased SERCA1a expression indicates the existence and location of compensating mechanisms in ischemic muscle.
Results show that ATP2A2 is variably expressed in astrocytoma tissues and its expression correlates with tumor grade. Its overexpression suppresses growth of astrocytoma cells.
study identifies a novel splice acceptor site mutation in the ATP2A2 gene, in a family showing Darier disease
Data suggest that mutations of the sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (ATP2A2) gene may lead to the occurrence of Darier disease (DD) in both familial and sporadic cases with DD.
Phospholamban and sarcolipin are membrane proteins that differentially regulate SERCA function. (Review)
CAPN3 deficiency leads to degradation of SERCA proteins and Ca2+ dysregulation in the skeletal muscle.
High SERCA2 expression is associated with colorectal cancer.
Quantification of SERCA2 mRNA or protein expression levels revealed no differences in airway smooth muscle cells obtained from subjects with asthma compared to non-asthmatic controls.
Data suggest that the beneficial effects of SERCA2a gene transfer may involve the attenuation of ER stress-associated myocardial apoptosis.
Oxidative/nitrosative stress associated with lung resection influences SERCA2a activity independent of any influence on protein expression or phospholamban phosphorylation.
overexpression of SERCA2a by in vivo rAAV1-mediated intracoronary gene transfer preserved systolic function, potentially prevented diastolic dysfunction, and improved ventricular remodeling.
pulmonary artery banding decreased the expression of (Serca) 2a while expression of Na(+)/Ca(2+) exchanger-1 was significantly upregulated in the right but not in the left atria of rabbit hearts; pressure is the major trigger.
Crystal structure of Ca2+-ATPase from skeletal muscle sarcoplasmic reticulum is determined, which shows that a two-step rotation of the cytoplasmic A-domain opens and closes the luminal gate through the movements of the M1-M4 transmembrane helices.
Data show that rabbit cold tolerance is probably related to increased muscle oxidative metabolism and heat production by SERCA1 and that these changes are not completely dependent on normal thyroid function.
These results indicate a mechanism relating SERCA1 vicinal-cysteines oxidation to muscle fatigue.
These data demonstrate that the activity of RyR2, but not SERCA2a, is a major determinant of Ca2+ alternans in intact working mouse hearts.
Here the show that DWORF has a higher apparent binding affinity for SERCA than PLN and that DWORF overexpression mitigates the contractile dysfunction associated with PLN overexpression, substantiating its role as a potent activator of SERCA.
Etoposide-induced protein 2.4 functions as a regulator of the calcium ATPase and protects pancreatic beta-cell survival
Pin1 serves as a modulator of SERCA2a and Na(2+)/Ca(2+) exchanger 1 Ca(2+) handling proteins, with loss of function resulting in impaired cardiomyocyte relaxation.
Pep2.5 prevented the down-regulation of SERCA2 expression in a) murine heart samples obtained from mice with sepsis and b) in cardiomyocytes exposed to serum from septic shock patients. Thus, we speculate that Pep2.5 may be able to prevent down-regulation of cardiac SERCA2 expression in patients with sepsis.
The findings support a salutary role of TLR9 in some subsets of HF conditions and underline the importance for future studies on the mechanisms of TLR9 in diastolic HF.
Our results indicate that changes in cell shape changed nuclear morphology and then the gene expression of IP3R1 and SERCA2, which produced different intracellular calcium transient patterns.
Nevertheless, the functional role of protein serotonylation in controlling SAN automaticity is largely unexplored. In this study, we screened the cardiomyocytes proteins and found that sarco(endo)plasmic reticulum Ca ATPase type 2a (SERCA2a) can be serotonylated. Simulation studies using mathematical SAN cell model showed that variation of Ca(2+) affinity of SERCA2a pump cause either tachycardia or bradycardia.
Muscle RANK deletion had no significant effects on the sham or denervated slow-twitch soleus muscles. These data identify a novel role for RANK as a key regulator of Ca(2+)storage and SERCA activity, ultimately affecting denervated skeletal muscle function.
Generated were mice harboring N-ethyl-N-nitrosourea (ENU)-induced allelic mutations in Serca2: three missense mutations and one nonsense mutation. Mice harboring these Serca2 mutations developed tumors that were categorized as either early onset squamous cell tumors (SCT), with development similar to null-type knockout mice [2,4] (aggressive form; M682, M814), or late onset tumors (mild form; M1049, M1162).
Identify Atrap as a novel regulatory protein of the cardiac Ca(2+)-ATPase SERCA2a. Suggest that Atrap enhances the activity of SERCA2a and, consequently, facilitates ventricular relaxation.
Sustained activation of Toll-like receptor 9 causes cardiac and systemic inflammation, and deterioration of SERCA2a depletion-mediated diastolic heart failure.
The LRP1/Pyk2 axis represses SERCA2 mRNA expression via HIF-1a.
This first-in-class small-molecule activator targeting SERCA2a SUMOylation may serve as a potential therapeutic strategy for treatment of heart failure
privileged signal communication between the beta1-adrenergic receptor and SERCA2a impaired in cardiac hypertrophy
These data reveal myofibrillar Ca(2+)-sensitivity to be an important determinant of the cardiac effects of SERCA2 haploinsufficiency and raise the possibility that Darier disease patients are more susceptible to heart failure under certain conditions.
SEPN1 enhances SERCA2 activity by reducing luminal cysteines that are hyperoxidized by ERO1-generated peroxides.
SERCA 2 and ERO1 mediate endothelial cell and macrophage angiogenic response to ischemia/hypoxia.
SERCA2a gene transfer in the failing heart not only improves contractile function but also directly restores electric stability through amelioration of key arrhythmogenic substrate.
This gene encodes one of the SERCA Ca(2+)-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of muscle cells. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol into the sarcoplasmic reticulum lumen, and is involved in regulation of the contraction/relaxation cycle. Mutations in this gene cause Darier-White disease, also known as keratosis follicularis, an autosomal dominant skin disorder characterized by loss of adhesion between epidermal cells and abnormal keratinization. Alternative splicing results in multiple transcript variants encoding different isoforms.
Calcium ATPase at 60A
, ATPase, Ca++ transporting, cardiac muscle, slow twitch 2
, sarcoplasmic/endoplasmic reticulum calcium ATPase 2
, sarcoplasmic/endoplasmic reticulum calcium ATPase 2-like
, ATPase, Ca++ dependent, slow-twitch, cardiac muscle-2
, SR Ca(2+)-ATPase 2
, calcium pump 2
, calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
, cardiac Ca2+ ATPase
, endoplasmic reticulum class 1/2 Ca(2+) ATPase
, calcium ATPase
, sarcoplasmic reticulum Ca2+-transport ATPase isoform
, Ca(2+)-transport ATPase class 3
, sarcoplasmic/endoplasmic-reticulum Ca(2+) pump gene 2
, ATPase, Ca++ transporting, slow twitch 2
, sarco(endo)plasmic reticulum Ca(2+)-dependent ATPase 2
, sarco/endoplasmic reticulum Ca2+-ATPase 2
, sarcoplasmic reticulum slow-twitch Ca2 ATPase