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Recombinant Dog Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (ATP2A2), partial

Recombinant Dog Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (ATP2A2), partial

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

ATP2A2

Uniprot NO.

O46674

Species

Canis lupus familiaris (Dog) (Canis familiaris)

Source

Yeast

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation. Also modulates ER contacts with lipid droplets, mitochondria and endosomes.; Involved in the regulation of the contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca(2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca(2+) signaling cascades that promote osteoclast differentiation and activation.

Gene References into Functions

Fluorescence resonance energy transfer measurements in cells transiently transfected with fluorescently labeled SERCA2a revealed that SERCA readily forms homodimers; results suggest that SERCA forms constitutive homodimers in live cells and that dimer formation is not modulated by SERCA conformational poise, phospholamban binding, or phospholamban phosphorylation PMID:27653478
The present results provide insight into the structural dynamics of the Ca-ATPase. PMID:22808146
PLB decreases Ca(2+) binding to SERCA2a by stabilizing a unique E2.ATP state that is unable to bind thapsigargin or vanadate. PMID:20622261
Ca2+ binding to site I of the cardiac Ca2+ pump is sufficient to dissociate phospholamban PMID:19948724
Ser-38 phosphorylation of the Ca(2+)-ATPase is not a significant regulatory feature of cardiac Ca(2+) homeostasis PMID:14766745
phospholamban leucine 31 has roles in structural and functional interactions with SERCA2a PMID:15644311
Phenotypic consequences of depleted SERCA-gated stores for epidermal homeostasis explain how depleted SERCA2 calcium stores provoke focal lesions rather than generalized dermatoses, a reminiscent of the human genodermatosis Darier disease. PMID:16397524
The protein expression of SR Ca(2+) ATPase and SR Ca(2+)-release channel in RA was significantly reduced. PMID:17062976
analysis of reversal of phospholamban inhibition of the cardiac Ca2+-ATPase by protein kinase A and by anti-phospholamban monoclonal antibody 2D12 PMID:17548345