Recombinant Rat Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (Atp2a2), partial

Code CSB-YP002333RA
MSDS
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Source Yeast
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Code CSB-EP002333RA
MSDS
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Source E.coli
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Code CSB-EP002333RA-B
MSDS
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP002333RA
MSDS
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Source Baculovirus
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Code CSB-MP002333RA
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
Atp2a2Sarcoplasmic/endoplasmic reticulum calcium ATPase 2; SERCA2; SR Ca(2+)-ATPase 2; EC 7.2.2.10; Calcium pump 2; Calcium-transporting ATPase sarcoplasmic reticulum type; slow twitch skeletal muscle isoform; Endoplasmic reticulum class 1/2 Ca(2+) ATPase
Species
Rattus norvegicus (Rat)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
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.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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 Q&A
Q:

Please provide the information for CSB-EP002333RA. Please let me know did you make this product before? If so, which host? If not, what is the level of difficulty to make this protein? For example, do you feel confident it can be made or is it rather risky?

A:
Thanks for your inquiry.
Sorry, we haven't expressed these proteins before, however, we have successfully expressed the EP protein of Human species,
The similarity between the rat protein and human protein of the same region is 99%, so in theory we have a very high probability of successful expression, with no risk.
Below is the information for this protein of Human species:
Recombinant Human Sarcoplasmic/endoplasmic reticulum calcium ATPase 2(ATP2A2) ,partial
CSB-YP002333HU >> Yeast
CSB-EP002333HU >> E.coli
CSB-BP002333HU >> Baculovirus
CSB-MP002333HU >> Mammalian cell
Expression Region: 314-756aa; Partial, provide one of the complete Cytoplasmic domains
Tag information:EP: N-terminal 6xHis-tagged;YP, BP, MP: Tag type will be determined during the manufacturing process.
The expected tag for other expression systems: YP, BP, MP: N-terminal 6xHis-tagged
Sequence:

VITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDRVEGDTCSLNEFTITGSTYAPIGEVHKDDKPVNCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTSGVKQKIMSVIREWGSGSDTLRCLALATHDNPLRREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELNPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNM

Target Background

Function
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
  1. Low Serca2a expression is associated with ischemia-reperfusion- induced Injury and heart failure. PMID: 29141547
  2. ERSE present in the SERCA2 proximal promoter contains a CCAAT box that is involved in basal and ERS-mediated hSERCA2 transcriptional activation. PMID: 28884444
  3. We find that prolonged exposure of A7r5 cells to hyperglycemia (weeks) is associated with changes to Ca(2+) signaling, including most prominently an inhibition of the passive ER Ca(2+) leak and the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA). PMID: 28713824
  4. Whether the increased Ca(2+) transient and neurotransmission after SERCA2A overexpression contributes to enhanced sympathoexcitation in heart failure patients remains to be determined. PMID: 28223472
  5. This study demonstrated that Slowed relaxation of the diaphragm in septic rats was associated with reduced expression of SERCA2. PMID: 27104787
  6. findings show that SERCA's lipid annulus may influence its susceptibility to oxidative damage, which could have implications in muscular dystrophy and age-related muscle wasting PMID: 28137585
  7. 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. PMID: 27780728
  8. SERCA2b as a novel target for HIF-1 and may provide potential implications for HIF-1alpha-stabilizing strategy in activating endogenous neuroprotection PMID: 26969192
  9. potential mechanism in which iron exacerbates the diabetes-induced oxidative/nitrative modification of SERCA2a PMID: 27222135
  10. Our findings suggest that unlike the ventricle, SERCA2a is not a key regulator of cardiac alternans in the atrium. Importantly, SERCA2a overexpression in atrial myocytes can increase SCR, which may be arrhythmogenic PMID: 26352986
  11. This first-in-class small-molecule activator targeting SERCA2a SUMOylation may serve as a potential therapeutic strategy for treatment of heart failure PMID: 26068603
  12. SERCA2 overexpression protects against primary rat cardiomyocyte death due to chlorine. PMID: 25188881
  13. SERCA2b protein stability is decreased under inflammatory conditions through nitric oxide- and AMP-Activated Protein Kinase-dependent pathways PMID: 26086963
  14. Results showed that resistance training induces cardiac hypertrophy with improved contractile function of isolated cardiomyocytes probably, through increased expression of SERCA2a and decreased miRNA-214 expression. PMID: 25822872
  15. Collectively, our results suggest that DHA may promote skeletal muscle-based metabolism and thermogenesis through its influence on SERCA. PMID: 25772907
  16. TNF-alpha suppresses SERCA2a gene expression via the IKK/IkappaB/NF-kappaB pathway and binding of NF-kappaB to the SERCA2a gene promoter in inflammation related diastolic dysfunction. PMID: 25712896
  17. the findings suggest that one of the potential cardiovascular benefits of estrogen is upregulation of SERCA2b, via activation of the classic ERalpha and ERbeta pathway.[SERCA2b] PMID: 24684418
  18. Increased SERCA-2a protein expression may play a role in the preservation of right ventricular function post-myocardial infarction PMID: 25625241
  19. pathological changes of cardiomyocyte mechanics suggest the potential involvement of the beta-adrenergic system, which is possibly associated with changes in SERCA2a expression and disturbances in Ca(2+) intracellular kinetics PMID: 25095801
  20. Persistent overexpression of SERCA2a affects bladder functions under physiological conditions, but not in bladder outlet obstruction-induced sub-acute pathological conditions. PMID: 24037709
  21. SERCA2 activity is involved in the C-type natriuretic peptide-mediated functional responses in failing rat myocardium PMID: 23808942
  22. Suggest that elevated oxidative stress may induce oxidative modifications on SERCA2a leading to abnormal function of this protein in the metabolic syndrome heart. PMID: 23997093
  23. lipid-derived malondialdehyde and 4-hydroxynonenal adducts are not formed on SERCA2 in either control or diabetic rat hearts PMID: 23354458
  24. The amount of sarcoplasmic reticulum Ca2+-ATPase (SERCA) 2a and phospholamban (PLB) protein was decreased and that may play a role in the diastolic dysfunction in SHRSP fatty rats. PMID: 23458196
  25. Early type 2 diabetes is associated with an increase in the SERCA/PLB ratio and insulin directly stimulates SERCA expression and relaxation velocity. PMID: 22621761
  26. engagement of the CN/NFAT pathway by endogenous genes involved in hypertrophy produces downregulation of SERCA2 PMID: 21964539
  27. Compared with spinal isolation, spasticity promoted parvalbumin recovery (ninefold increase) and a SERCA2-to-SERCA1 transformation (84% increase in the ratio of SERCA1 to SERCA2) in tail muscle. PMID: 21930674
  28. NHE-1 participates in isoproterenol-induced downregulation of SERCA2a and development of cardiac remodeling in rat hearts. PMID: 21856903
  29. Trichloroethylene reduced Serca2a expression by altering the methylation status of its proximal promoter region in cardiac myocytes and embryonic heart. PMID: 21479763
  30. The myocardial dysfunction caused by obesity is related to L-type Ca2+ channel activity impairment without significant changes in SERCA2a expression and function as well as L-type Ca2thorn protein levels. PMID: 21302294
  31. Mitochondrial transcription factors TFAM and TFB2M regulate Serca2 gene transcription in cardiac myocytes. PMID: 21113058
  32. overexpression of SERCA2a prevented the down-regulation of SERCA protein in LVH hearts, TG-LVH hearts showed no increase in inotropic response when compared with WT-LVH hearts. PMID: 21278384
  33. In the female hypothyroid rat heart, expression of thyroid hormone-insensitive SERCA2a minigene compensates for loss of thyroid hormone-responsive native SERCA2a gene but only partially rescued heart function and sarcoplasmic reticulum Ca2+ uptake. PMID: 21217071
  34. These data identify carbonylation as a novel mechanism that contributes to SERCA2a activity loss and diastolic dysfunction during type 1 diabetes. PMID: 21300842
  35. Knockdown of Nox4 inhibits oxidation of SERCA, as well as neointima formation, after Zucker rat common carotid artery injury PMID: 20724704
  36. SERCA2a promoter plays a significant role in myocardial ischemia-preconditioning, with myocardial ischemia-preconditioning able to precondition the SERCA2a promoter against the deleterious effects of IRI-induced injury. PMID: 19714449
  37. Although Ang II had prominent effects on SERCA2 in ventricular myocytes, it did not alter SERCA2 gene expression and protein levels in atrial myocytes PMID: 19617272
  38. SERCA2a level was about 50% lower in the soleus of streptozocin-treated rats compared to that of the controls. PMID: 19738937
  39. Equivalent levels of SercaII inhibition by phospholamban (PLB) and activation by anti-PLB antibody are observed in sarcoplasmic reticulum (SR) from the heart as compared with Serca1 isoform from slow-twitch skeletal muscle SR. PMID: 12403631
  40. Mechanisms underlying increases in SR Ca2+-ATPase activity after exercise in rat skeletal muscle. No changes in relative isoform content of sarcoendoplasmic reticulum (SERCA)1 and SERCA2a. PMID: 12409282
  41. nerve impulses play a determinant role in the expression of the SERCA2 isoform. PMID: 12481932
  42. data do not support a role of SERCA2 in ameliorating anthracycline cardiotoxicity PMID: 12659846
  43. Regulation of SERCA2a expression is clearly distinct from that of the slow myosin in the regenerating soleus muscle and that SERCA2a expression is modulated by neuronal activity but is not entirely dependent on it. PMID: 12773312
  44. SERCA2a has a role in myocyte contraction and relaxation and Ca2+ channel kinetics PMID: 13129932
  45. Serca2 improves cardiac muscle contractility in vivo and in vitro. PMID: 14575311
  46. advanced glycation end products are formed on SERCA2a during experimental diabetes PMID: 14747299
  47. data suggested that thyroid stimulating hormone/cyclic AMP acts as an important regulator of both sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) 2b expression and activity in the thyroid system through protein kinase A PMID: 15191357
  48. SERCA2a gene expression decreased during the late phase of sepsis in the rat heart and that the decreased expression was regulated at the transcriptional level. PMID: 15201701
  49. More likely, a CaMKII-independent mechanism could be involved, whereby increasing stimulation frequency would disrupt the SERCA2a-PLN interaction, leading to an increase in SR Ca(2+) uptake and myocardial relaxation. PMID: 15528241
  50. Site-directed mutagenesis revealed that two Sp1 sites in the SERCA2 gene promoter region mediated the response to carvedilol under oxidative stress. PMID: 15670758

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Subcellular Location
Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein.
Protein Families
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily
Tissue Specificity
Isoform 2 is highly expressed in heart and slow twitch skeletal muscle. Isoform 1 is widely expressed.
Database Links
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