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Recombinant Human Ribonuclease K6 (RNASE6)

Amino acids 24-150 constitute the expression domain of recombinant Human RNASE6. The theoretical molecular weight of the RNASE6 protein is 19.7 kDa. The RNASE6 protein was expressed in e.coli. The RNASE6 coding gene included the N-terminal 10xHis tag and C-terminal Myc tag, which simplifies the detection and purification processes of the recombinant RNASE6 protein in following stages of expression and purification.Ribonuclease K6 (RNASE6), a member of the ribonuclease A superfamily, is a small secretory protein involved in the regulation of angiogenesis, and the formation of new blood vessels. RNASE6 has been identified as an angiogenin-binding protein, and it inhibits angiogenin-mediated endothelial cell proliferation and tube formation. This suggests a role in controlling the process of blood vessel growth. Additionally, RNASE6 exhibits ribonuclease activity, contributing to its regulatory functions. The precise mechanisms of RNASE6 in various physiological and pathological conditions, especially its involvement in angiogenesis-related processes, make it an intriguing molecule for further exploration in biomedical research.

ACP00992

Amino acids 24-150 constitute the expression domain of recombinant Human RNASE6. The theoretical molecular weight of the RNASE6 protein is 19.7 kDa. The RNASE6 protein was expressed in e.coli. The RNASE6 coding gene included the N-terminal 10xHis tag and C-terminal Myc tag, which simplifies the detection and purification processes of the recombinant RNASE6 protein in following stages of expression and purification.Ribonuclease K6 (RNASE6), a member of the ribonuclease A superfamily, is a small secretory protein involved in the regulation of angiogenesis, and the formation of new blood vessels. RNASE6 has been identified as an angiogenin-binding protein, and it inhibits angiogenin-mediated endothelial cell proliferation and tube formation. This suggests a role in controlling the process of blood vessel growth. Additionally, RNASE6 exhibits ribonuclease activity, contributing to its regulatory functions. The precise mechanisms of RNASE6 in various physiological and pathological conditions, especially its involvement in angiogenesis-related processes, make it an intriguing molecule for further exploration in biomedical research.

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Specifications


Cat.No ACP00992 Target NameRNASE6
FormLiquid or Lyophilized powderExpression SystemE.coli
Expression Range24-150aaMol Weight19.7 kDa
Protein LengthFull Length of Mature ProteinPurityGreater than 90% as determined by SDS-PAGE.
Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDQ93091
Background Information
  • Uniprot Id

    Q93091

  • Target Species

    Human

  • Target Name

    RNASE6

  • Target Full Name

    Ribonuclease K6

  • Target Function

    Ribonuclease which shows a preference for the pyrimidines uridine and cytosine. Has potent antibacterial activity against a range of Gram-positive and Gram-negative bacteria, including P.aeruginosa, A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus and E.coli. Causes loss of bacterial membrane integrity, and also promotes agglutination of Gram-negative bacteria. Probably contributes to urinary tract sterility. Bactericidal activity is independent of RNase activity.

  • Target Subcellular Location

    Secreted. Lysosome. Cytoplasmic granule.

  • Target Protein Families

    Pancreatic ribonuclease family

  • Target Tissue Specificity

    Highly expressed in spleen (at protein level). Has little or no expression in healthy kidneys (at protein level). Detected in interstitial leukocytes in infected kidneys (at protein level). Expressed in ureter where it localizes to urothelial and submucos

  • Target Research Area

    Epigenetics and Nuclear Signaling

  • Target Synonyms

    RNASE6; RNS6; Ribonuclease K6; RNase K6; EC 3.1.27.-

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