Recombinant Rat Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (Atp2a1), partial

Code CSB-YP717551RA
MSDS
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Source Yeast
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Code CSB-EP717551RA
MSDS
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Source E.coli
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Code CSB-EP717551RA-B
MSDS
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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-BP717551RA
MSDS
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Source Baculovirus
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Code CSB-MP717551RA
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Atp2a1
Uniprot No.
Alternative Names
Atp2a1; Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; SERCA1; SR Ca(2+)-ATPase 1; EC 7.2.2.10; Calcium pump 1; Calcium-transporting ATPase sarcoplasmic reticulum type; fast 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, pH 8.0
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.

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Target Background

Function
Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction.
Gene References into Functions
  1. In acute stages of sepsis, the improvement of SERCA function could reduce the disequilibrium of calcium homeostasis to improve the critical illness myopathy and respiratory failure. PMID: 28765908
  2. This study demonstrated that Slowed relaxation of the diaphragm in septic rats was associated with reduced expression of SERCA1. PMID: 27104787
  3. SERCA has a role in sarcoplasmic reticulum calcium content and calcium wave propagation in rat ventricular myocytes PMID: 27242324
  4. these results suggest that sAnk1 interacts with SERCA1 through its TM and cytoplasmic domains to regulate SERCA1 activity and modulate sequestration of Ca(2+) in the sarcoplasmic reticulum lumen. PMID: 26405035
  5. Thus the human SERCA1b has a different expression pattern from that of rodents and it is associated with DM2. PMID: 25487304
  6. changes between enzyme activity and fluorescence isothiocyanate binding suggest that, at least during recovery after exercise, changes in SERCA activity may not correlate with structural alterations to the adenine nucleotide binding site within the enzyme PMID: 19302261
  7. SERCA1 levels were not different on immunoblots of the soleus of streptozocin-treated and control rats. PMID: 19738937
  8. Inactivation of sarcoplasmic reticulum Ca(2+)-atpase in low-frequency stimulated rat muscle. PMID: 12222829
  9. Equivalent levels of SERCA1 inhibition by phospholamban (PLB) and activation by anti-PLB antibody are observed in sarcoplasmic reticulum (SR) from the heart as compared with SercaII isoform from slow-twitch skeletal muscle SR. PMID: 12403631
  10. High-intensity, exhaustive exercise causes oxidation of sarcoplasmic reticulum Ca(2+)-ATPase(SERCA). Oxidation of amino acids other than cysteine in SERCA may be responsible, at least in part, for exercise-induced inactivation. PMID: 12684795
  11. A serca1 was identified in rat brown adipose tissue that differs in kinetic properties from skeletal muscle SERCA1, and may represent a source of heat production contributing to the thermogenic function of brown adipose tissue. PMID: 12912988
  12. upregulation of Ca(2+)transporting-ATPase(Serca1) activity may be an adaptive mechanism and/or a contributory process in the pathology of alcohol-induced muscle disease PMID: 14506614
  13. These data confirm that burn trauma alters calcium transporter expression, likely contributing to cardiomyocyte calcium loading and cardiac contractile dysfunction. PMID: 15180978
  14. HSP70 can bind to SERCA1a and, depending on the severity of heat stress, protect SERCA1a function by stabilizing the nucleotide binding domain PMID: 15371420
  15. Adenoviral Serca1 overexpression triggers an apoptotic response in cultured neonatal but not in adult cardiomyocytes. PMID: 15663193
  16. Impaired SERCA activity (with normal protein content) contributes to cardiomyocyte dysfunction in insulin resistant animals, whereas NCX function and expression are normal PMID: 15878173
  17. An age-dependent loss of cysteine residues (approx. 2.8 mol of cysteine/mol of SERCA1), which may be partially responsible for the age-dependent decrease in the specific Ca2+-ATPase activity, is reported. PMID: 16307534
  18. Muscle glycogen does not influence exercise tolerance and work productivity in working muscles by modulating the structure of protein involved in Ca(2+) sequestering. PMID: 16369770
  19. Our studies point to an important regulation of SERCA1b expression at the protein level and hints to a role in the growth of the developing muscle. PMID: 17010426
  20. Serca specific antibodies demonstrated a rapid up-regulation of the fast fiber type- specific isoform (Serca1). PMID: 17482761
  21. Hearts of SERCA1a(+/+) transgenic mice were markedly protected against I/R injury, suggesting that expression of SERCA 1a isoform reduces postischemic Ca(2+) overload and thus provides potent myocardial protection. PMID: 17630344
  22. Serca1 was not altered in diaphragm of buthionine sulfoximine treated rats. PMID: 17717121
  23. These results suggest that impairment of the SERCA function may be an early event in excitotoxicity. PMID: 18307036
  24. There was no expression of pancreatic SERCA1 mRNA in the control group or the acute pancreatitis group. PMID: 18416460
  25. Concluded that increased SERCA activity in adjuvant arthritis was due to increased levels of SERCA protein and structural changes to the protein, probably induced by direct and specific oxidation involving reactive nitrogen species. PMID: 19591012

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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
Skeletal muscle, fast twitch muscle (type II) fibers.
Database Links

KEGG: rno:116601

UniGene: Rn.217139

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