Recombinant Bovine Catalase(CAT) ,partial

Code CSB-YP004563BO
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Source Yeast
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Code CSB-EP004563BO
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Source E.coli
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Code CSB-EP004563BO-B
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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-BP004563BO
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Source Baculovirus
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Code CSB-MP004563BO
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names CAT
Uniprot No. P00432
Alternative Names CATCatalase; EC
Species Bos taurus (Bovine)
Protein Length Partial
Tag Info The following tags are available.
N-terminal His-tagged
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
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.
and FAQs
Protein FAQs
Storage Condition Store at -20°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

(From Uniprot)
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells.
Gene References into Functions
  1. Enzyme activity assay and molecular docking revealed that the activity of CAT was slightly inhibited in the presence of Sudan dyes. In comparison, the binding of Sudan II with CAT was slightly stronger than Sudan IV. Also, Sudan II and Sudan IV showed a different impact on the microenvironment of aromatic amino acid residues. PMID: 28613393
  2. the decrease in accessible surface area and increase in pKa of important lysine residues were considered as predominant factors in decreased glycation of bovine liver catalase by curcumin. PMID: 28668706
  3. ITC confirms the stability of bovine liver catalase (BLC)upon gemini combination. Docking provides support to fluorescence results by presenting the localization site of m-E2-m surfactants near to aromatic residues (mainly Tyr, Trp and Phe) PMID: 27060016
  4. Data show that liver catalase is able to tolerate very high levels of the modifying alpha-oxoaldehyde methylglyoxal so that its essential enzymatic function is not impaired. PMID: 26715035
  5. The structure of bovine liver catalase determined from a single crystal at 3.2 A resolution by MicroED, is reported. PMID: 25303172
  6. These maps demonstrate that it is indeed possible to build atomic models from such crystals and even to determine the charged states of amino acid residues in the Ca(2+)-binding sites of Ca(2+)-ATPase and that of the iron atom in the heme in catalase. PMID: 25730881
  7. Data indicate compatible osmolytes, proline, xylitol, and valine destabilize the denatured form of the catalase enzyme and, therefore, increase its disaggregation and thermal stability. PMID: 23249140
  8. Flavonoid inhibition of catalase activity is, at least partially, due to the formation of hydrogen bonds between catalase and the flavonoid. PMID: 23567286
  9. Comparison of deoxyferrous and oxyferrous complexes of cAOS and MAP with bovine liver catalase elucidates unresolved mechanistic questions in the catalytic cycles of these enzymes PMID: 22104301
  10. Catalase is not influenced by the solvent during the catalytic reaction, which represents a lower energy barrier to be crossed in the overall energetics of the reaction, a fact that contributes to the high turnover rate of catalase. PMID: 21529340
  11. At room temperature (25.0 degrees C) and higher, the addition of high concentrations of polymer is found to significantly enhance the affinity of SOD for catalase. PMID: 20682270
  12. Immunohistochemistry in rectus abdominis muscle from foetuses at 180 and 260 days post-conception PMID: 12441094
  13. study of bovine liver catalase and [14C]NADPH and [14C]NADH revealed that unbound NADPH or NADH are substrates for an internal reductase and transhydrogenase reaction respectively PMID: 15456401
  14. Overexpression of catalase prevents the stimulation of reactive oxygen species and angiotensinogen mRNA in tubules owing to elevated glucose or angiotensin II in transgenic diabetic mice. PMID: 17342175
  15. CAT transgenic mice became obese and hyperglycemic but had normal blood pressure and attenuated albuminuria compared with diabetic mice. PMID: 17977949
  16. The structure of the active site of liver catalase B chain (PDB 4BLC) in the radical state (tyrosyl radical) was studied using EPR. PMID: 19639135
  17. Data show that acriflavine induced in vitro a profound change in the structure of catalase so that the enzyme could no longer function. PMID: 19723068

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Subcellular Location Peroxisome
Protein Families Catalase family
Database Links

KEGG: bta:531682

STRING: 9913.ENSBTAP00000027941

UniGene: Bt.48925

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  Email: [email protected]
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