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  4. Recombinant Bovine Ribonuclease pancreatic (RNASE1)

Recombinant Bovine Ribonuclease pancreatic (RNASE1)

  • 中文名称：
    牛RNASE1重组蛋白
  • 货号：
    CSB-YP019789BO
  • 规格：
  • 来源：
    Yeast
  • 其他：
  • 中文名称：
    牛RNASE1重组蛋白
  • 货号：
    CSB-EP019789BO
  • 规格：
  • 来源：
    E.coli
  • 其他：
  • 中文名称：
    牛RNASE1重组蛋白
  • 货号：
    CSB-EP019789BO-B
  • 规格：
  • 来源：
    E.coli
  • 共轭：
    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.

  • 其他：
  • 中文名称：
    牛RNASE1重组蛋白
  • 货号：
    CSB-BP019789BO
  • 规格：
  • 来源：
    Baculovirus
  • 其他：
  • 中文名称：
    牛RNASE1重组蛋白
  • 货号：
    CSB-MP019789BO
  • 规格：
  • 来源：
    Mammalian cell
  • 其他：

产品详情

  • 纯度：
    >85% (SDS-PAGE)
  • 基因名：
    RNASE1
  • Uniprot No.：
  • 别名：
    RNASE1; RNS1; Ribonuclease pancreatic; EC 4.6.1.18; RNase 1; RNase A
  • 种属：
    Bos taurus (Bovine)
  • 蛋白长度：
    Full Length of Mature Protein
  • 表达区域：
    27-150
  • 氨基酸序列
    KETA AAKFERQHMD SSTSAASSSN YCNQMMKSRN LTKDRCKPVN TFVHESLADV QAVCSQKNVA CKNGQTNCYQ SYSTMSITDC RETGSSKYPN CAYKTTQANK HIIVACEGNP YVPVHFDASV
  • 蛋白标签：
    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.
  • 产品提供形式：
    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.
  • 复溶：
    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.
  • 储存条件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期：
    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.
  • 货期：
    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.
  • 注意事项：
    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.

产品评价

靶点详情

  • 功能：
    Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.
  • 基因功能参考文献：
    1. Thermal unfolding of ribonuclease A (RNase) was analyzed in various osmolyte solutions of glycine, proline, sarcosine, N,N-dimethylglycine, betaine, myo-inositol, taurine, and trimethylamine-N-oxide (TMAO). PMID: 24292629
    2. investigation of structure/stability of native pancreatic RNase A compared to specific analogs: Results suggest that a reverse turn (Asn113-Pro114) exhibits great control over unfolding, conformational stability, and enzymatic activity of RNase A. PMID: 23238807
    3. The initials steps of the molecular mechanism of Urea-RNase A interaction passes through the establishment of a three center four electron adduct. PMID: 23381689
    4. Inactivation and reactivation of ribonuclease A studied by computer simulation. PMID: 22868279
    5. Overexpression of bovine RNase in Toll-like receptor (TLR)7 transgenic mice results in reduction in splenomegaly, reduced numbers of activated B and T cells, fewer immune deposits in the kidney, reduced liver inflammation, and increased survival. PMID: 23382559
    6. Data show that Asp83 replaced by Glu in ribonuclease A resulted in a comparable stabilization. PMID: 22594773
    7. Effect of D-amino acids on the functional activity and conformational stability of ribonuclease-A PMID: 22905393
    8. The study suggests that domain swapping occurs via a local high-energy fluctuation at the C-terminus. PMID: 21805524
    9. Folding, quality control, and secretion of pancreatic ribonuclease in live cells. PMID: 21156800
    10. Hydrogen/deuterium (H/D) exchange of the RNase A C-dimer reveal that the H-bonds formed between the swapped C-terminal beta-strand and the other subunit are strong. Their rupture may be crucial for C-dimer dissociation. PMID: 21094126
    11. These results provide support for a more general role for proline 114 isomerization as a conformational gatekeeper in domain swapping and oligomerization. PMID: 20471398
    12. RNase A is chiefly unfolded in 40% acetic acid; it partially retains the native helices, whereas the beta-sheet is fully denatured and all X-Pro peptide bonds are predominantly in the trans conformation. PMID: 20085318
    13. Data suggest that, in addition to Pro19 and Leu28, the presence of a glycine at the N-terminal end of the hinge peptide is also important to push the swapped form of RNase A dimer into the compact quaternary organization observed for NCD-BS. PMID: 19280639
    14. Studies propose a structural model for the major and the minor hydrophobic nuclei of RNase A. PMID: 19373927
    15. The ribbon of hydrogen bonds and the pseudomolecule in the three-dimensional structure of pancreatic ribonuclease A and seminal ribonuclease PMID: 12389214
    16. Under folding conditions, reduced RNASE1 shows no sign of secondary structure, yet the C-terminal domain of the molecule has a compact structure with native-like features which can undergo unfolding/refolding transitions. PMID: 12450386
    17. bovine ribonuclease A has two three-dimensional domain-swapped tetramers PMID: 15218036
    18. analysis of unfolding of ribonuclease A embedded in spherical polyelectrolyte brushes PMID: 15633159
    19. native state of RNase A, Tyr 92 lies atop its (40-95) disulfide bond, effectively shielding this bond from the reducing agent, thereby promoting protein oxidative regeneration PMID: 15686534
    20. A direct correlation between the number of cis-prolyl bonds in a native protein and the complexity with which it folds is shown in the folding of three structurally homologous proteins of the ribonuclease family, namely RNase A, onconase and angiogenin. PMID: 16949585
    21. the hydrophilic or hydrophobic character of the Ribonuclease A N-terminus or C-terminus can be an important variable governing the oligomerization of RNase A and possibly other proteins through the 3D domain-swapping mechanism. PMID: 16953565
    22. placental ribonuclease inhibitor (hRI) containing six Trp residues located at positions 19, 261, 263, 318, 375, and 438 and its complex with RNase A have been studied using steady-state and time-resolved fluorescence and low-temperature phosphorescence PMID: 17048964
    23. The quadruple mutant K7H/R10H/H12K/H119Q shows a clear increase of the exonucleolytic activity; in this case the original native active site has been suppressed, and, as consequence, its activity can only be associated to the new active site. PMID: 17192592
    24. The ribonuclease A structures of the two dimers and one trimer have been solved. PMID: 17763469
    25. Computer simulations show that subtle, functionally important changes in protein conformation can occur below the melting temperature of RNaseA. PMID: 18161991
    26. Data point out the importance of the native structure of RNase A in preventing an uncontrolled aggregation and precipitation in a reducing and highly crowded environment like that existing in a living cell. PMID: 18261475
    27. Data show that experimental small-angle x-ray scattering profiles of ribonuclease A closely matched those predicted by the computational model assuming relatively small solvation energies. PMID: 18329044
    28. Results describe the mechanism of millisecond motions in the RNase A catalytic cycle. PMID: 19588901

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  • 亚细胞定位：
    Secreted.
  • 蛋白家族：
    Pancreatic ribonuclease family
  • 组织特异性：
    Pancreas.
  • 数据库链接：

    KEGG: bta:282340

    STRING: 9913.ENSBTAP00000011586

    UniGene: Bt.4630