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  4. Recombinant Bovine Seminal ribonuclease (SRN)

Recombinant Bovine Seminal ribonuclease (SRN)

  • 中文名稱：
    牛SRN重組蛋白
  • 貨號：
    CSB-YP360569BO
  • 說明書：
  • 規格：
  • 來源：
    Yeast
  • 其他：
  • 中文名稱：
    牛SRN重組蛋白
  • 貨號：
    CSB-EP360569BO
  • 說明書：
  • 規格：
  • 來源：
    E.coli
  • 其他：
  • 中文名稱：
    牛SRN重組蛋白
  • 貨號：
    CSB-EP360569BO-B
  • 說明書：
  • 規格：
  • 來源：
    E.coli
  • 共軛：
    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：
  • 中文名稱：
    牛SRN重組蛋白
  • 貨號：
    CSB-BP360569BO
  • 說明書：
  • 規格：
  • 來源：
    Baculovirus
  • 其他：
  • 中文名稱：
    牛SRN重組蛋白
  • 貨號：
    CSB-MP360569BO
  • 說明書：
  • 規格：
  • 來源：
    Mammalian cell
  • 其他：

產品詳情

  • 純度：
    >85% (SDS-PAGE)
  • 基因名：
    SRN
  • Uniprot No.：
  • 別名：
    SRN; Seminal ribonuclease; S-RNase; Seminal RNase; EC 4.6.1.18; Ribonuclease BS-1
  • 種屬：
    Bos taurus (Bovine)
  • 蛋白長度：
    Full Length of Mature Protein
  • 表達區域：
    27-150
  • 氨基酸序列
    KESA AAKFERQHMD SGNSPSSSSN YCNLMMCCRK MTQGKCKPVN TFVHESLADV KAVCSQKKVT CKNGQTNCYQ SKSTMRITDC RETGSSKYPN CAYKTTQVEK HIIVACGGKP SVPVHFDASV
  • 蛋白標簽：
    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.
  • 產品提供形式：
    Lyophilized powder Warning: in_array() expects parameter 2 to be array, null given in /www/web/cusabio_cn/public_html/caches/caches_template/default/content/show_product_protein.php on line 662
    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.
  • 復溶：
    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.
  • 儲存條件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保質期：
    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.
  • 貨期：
    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.
  • 注意事項：
    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.

產品評價

靶點詳情

  • 功能：
    This enzyme hydrolyzes both single- and double-stranded RNA.
  • 基因功能參考文獻：
    1. In the regions involved in 3D swapping, the study observed an accumulation of weaknesses in the monomer, which disappear in the dimer and especially in the swapped dimer. PMID: 26573727
    2. Data suggest that dimerization of seminal ribonuclease (SRN) facilitates three-dimensional domain swapping; both swapped and un-swapped dimers of SRN exhibit increased flexibility as compared to monomeric subunit SRN. PMID: 24616921
    3. A report of the first clear experimental evidence on the formation of a C-terminal swapped dimer of the monomeric BS-RNase derivatives. PMID: 24140346
    4. Data indicate that BS-RNase oligomers are more enzymatically active than the native dimer. PMID: 23071641
    5. The domain swapping in BS-RNase must be influenced by the distinct features of the dimers, suggesting a prominent role for the interchain disulfide bridges. PMID: 22253705
    6. the replacement of of Arg80 by Ser significantly decreases the cytotoxic activity of BS-RNase and the stability of the NCD form with respect to the parent protein, but does not affect the ribonucleolytic activity or the dissociation mechanism PMID: 21122069
    7. 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
    8. Data show that all the proteins have a very poor cytotoxic activity, independently on the swapping propensity, that can even reach the same value of native BS-RNase. PMID: 19263489
    9. The structural data enable existing kinetic data on the binding of these compounds to a variety of ribonucleases to be rationalized. PMID: 19191310
    10. Studies show the two isoforms of dimeric RNase, with interchange of the N-terminal helical segments, and without interchange. PMID: 19156888
    11. engineering of refolding pathway and quaternary structure PMID: 12377788
    12. Data report on monomeric derivatives of bovine seminal ribonuclease (BS-RNase) that, although strongly inhibited by the cytosolic RNase inhibitor, are cytotoxic towards malignant cells. PMID: 12709057
    13. Crystal structure of the free and liganded monomeric derivatives of seminal ribonuclease. PMID: 12833549
    14. crystal structure, at 2.2 A resolution, of the unswapped form of bovine seminal ribonuclease explains the dependence of the enzyme cooperative effects on its swapping state PMID: 14596923
    15. structural determinants that control the exchange of N-terminal arms in BS-RNase may not be located within the hinge peptide, and point to a crucial role of the interface residues PMID: 14622261
    16. analysis of structure and stability of the non-covalent swapped dimer of seminal ribonuclease PMID: 15192098
    17. Results describe the assembly of the non-covalent dimer of bovine seminal ribonuclease (BS-RNase), the species produced by selective reduction of the interchain disulfides and considered responsible for the special biological functions of BS-RNase. PMID: 15647261
    18. Bovine seminal-RNase monomers described herein are more toxic to human tumor cells than is any known variant or homologue of RNase A, exceeding the wild-type dimer by up to 30-fold. PMID: 16313179
    19. Subtle changes in structure conformation of both bovine seminal ribonucleases (BS-RNase) and oligomeric RNase A are shown to result in a modification of the affinity of these proteins toward the immobilized transition-metal chelate, IDA-Cu(II). PMID: 16933205
    20. The role of intermolecular hydrogen-bonding, protein/water interaction, and protein/water networks in stabilising the seminal ribonuclease dimer have been investigated. PMID: 17191881
    21. Overall, these data suggest that the presence of Arg80 triggers the swapping of N-terminal ends and plays a relevant role in the stability of the swapped form of bovine seminal RNase. PMID: 17269658
    22. analysis of how the unfolding process is slowed by single N-glycosylation of ribonuclease A PMID: 17937402

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  • 亞細胞定位：
    Secreted.
  • 蛋白家族：
    Pancreatic ribonuclease family
  • 組織特異性：
    Seminal plasma. Can reach 3% of the protein content of this fluid.
  • 數據庫鏈接：


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