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Human Recombinant RNase A (Prokaryotic) (from E. coli)
  MSPP-RPA297HU1
 :  
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Human Recombinant RNase A (Prokaryotic) (from E. coli)
  MSPP-RPA297HU1
 :  RPA297HU01
 :  
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  • Pack type:
    Vial
  • Conjugation:
    Unconjugated
  • Protein/Peptide Type:
    Recombinant
  • Source:
    E. coli
  • Species:
    Human
  • Size:
    50 µg
  • Tag sequence:
    MGHHHHHHSGSEF
  • Storage Conditions:
    –20 °C
  • Endotoxin Content:
    <1.0 EU per 1 μg (determined by the LAL method)
  • Gene ID:
    6035
  • Reconstitution Instructions:
    Reconstitute in 10 mM PBS (pH 7.4) to a concentration of 0.1 - 1.0 mg/ml. Do not vortex.
  • Endotoxin-free:
    N
  • Carrier-Free:
    Y
  • Protease-free:
    N
  • Animal-Free:
    Y
  • Protein Synonyms:
    Ribonuclease A
  • UniProtKB:
    P07998
  • Protein/Peptide Name:
    RNase A
  • Purity:
    90 - 100%
  • Molecular Weight:
    18 kDa
  • Sequence:
    Lys29~Thr156
  • Endotoxin Level:
    Low
  • Concentration:
    0.2 mg/ml
  • Formulation:
    Lyophilized from PBS, pH 7.4, containing 0.01% SKL, 5% Trehalose.
  • Nuclease-free:
    N
  • Shipping Temperature:
    4 °C
  • Tested Applications:
    Positive control, Immunogen, SDS-PAGE, Western blot.
  • Cat. No.:
    MSPP-RPA297HU1

 

 

This is a RNase A recombinant protein (prokaryotic), Human is sequencing from Lys29~Thr156 with 90 - 100% purity. Lyophilized from PBS, pH 7.4, containing 0.01% SKL, 5% Trehalose with 0.2 mg/ml.

  • High quality, purity, reproducibility and effectiveness
  • Offers customized buffers and tag options
  • 100% quality and service satisfaction guarantee

Ribonuclease A (RNase A) is an endonuclease that cleaves single-stranded RNA. Bovine pancreatic RNase A is one of the classic model systems of protein science.RNase A is a relatively small protein. It can be characterized as a two-layer α + β protein that is folded in half to resemble a taco, with a deep cleft for binding the RNA substrate. The first layer is composed of three alpha helices (residues 3-13, 24-34 and 50-60) from the N-terminal half of the protein. The second layer consist of three β-hairpins (residues 61-74, 79-104 and 105-124 from the C-terminal half) arranged in two β-sheets. The hairpins 61-74 and 105-124 form a four-stranded, antiparallel β-sheet that lies on helix 3 (residues 50-60). The longest β-hairpin 79-104 mates with a short β-strand (residues 42-45) to form a three-stranded, antiparallel β-sheet that lies on helix 2 .

 : ISO 9001 and ISO 13485 certified, three level QC system.
 : For research use only. Not for use in clinical diagnostic procedures. Please proper stored each component based on the instruction.