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Human Recombinant ERa (Prokaryotic) (from E. coli)
Human Recombinant ERa (Prokaryotic) (from E. coli)
  MSPP-RPB050HU1
 :  
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Human Recombinant ERa (Prokaryotic) (from E. coli)
  MSPP-RPB050HU1
 :  RPB050HU01
 :  

 

  • Pack type:
    Vial
  • Conjugation:
    Unconjugated
  • Protein Function:
    Cytokine
  • 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:
    2099
  • 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:
    Estrogen Receptor Alpha
  • UniProtKB:
    P03372
  • Protein/Peptide Name:
    ERa
  • Purity:
    90 - 100%
  • Molecular Weight:
    33 kDa
  • Sequence:
    Ser178~Met438
  • 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-RPB050HU1

 

 

This is a ERa recombinant protein (prokaryotic), Human is sequencing from Ser178~Met438 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

Estrogen receptor structure-function is a vast topic and the subject of very active current research. Nuclear receptors are a large family of structurally related ligand-inducible transcription factors, including steroid receptors (SRs), thyroid/retinoids receptors (TR, RARs and RXRs), vitamin D receptors (VDR), LXR, PPARs, estrogen receptors (ERα and ERβ), and orphan receptors for which no ligand has been yet identified. While having in common a modular structure, they are activated by distinct lipophilic small molecules such as glucocorticoids, progesterone, estrogens, retinoids, and fatty acid derivatives.All nuclear receptors have a hydrophobic pocket into which its specific ligand binds, with helix 12 (H12) being the key response element of NRs.

 : 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.