Recombinant Neosartorya fumigata Ribonuclease mitogillin(mitF) CSB-EP304681NGSa3
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Allergen Asp f I Allergen I/a IgE-binding ribotoxin Major allergen Asp f 1 Allergen: Asp f 1 aspF1
Species: (Organism)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Gene Names:
mitF
Tag info:
N-terminal 6xHis-SUMO-tagged and C-terminal Myc-tagged
Target Protein AA Sequence:
ATWTCINQQLNPKTNKWEDKRLLYSQAKAESNSHHAPLSDGKTGSSYPHWFTNGYDGNGKLIKGRTPIKFGKADCDRPPKHSQNGMGKDDHYLLEFPTFPDGHDYKFDSKKPKEDPGPARVIYTYPNKVFCGIVAHQRGNQGDLRLCSH
Expression Region:
28-176aa
Subcellular Location:
Secreted
Tissue Specificity:
Protein Length:
Full Length of Mature Protein
Pathway:
Mol. Weight:
31.2 kDa
Purity:
Greater than 85% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Signal Transduction
Function:
This purine-specific ribonuclease cleaves 28S RNA in eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor activity.
Involvement in disease:
Relevance:
This purine-specific ribonuclease cleaves 28S RNA in eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor activity.
Reconstitution:
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.
Protein Families:
Ribonuclease U2 family
Reference:
"Secretion of a potential virulence factor, a fungal ribonucleotoxin, during human aspergillosis infections." Lamy B., Moutaouakil M., Latge J.P., Davies J. Mol. Microbiol. 5:1811-1815(1991)
