Recombinant Aspergillus clavatus Ribonuclease clavin(cla) CSB-EP316109AVC
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
/
Species: (Organism)
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Gene Names:
cla
Tag info:
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Target Protein AA Sequence:
AATWTCMNEQKNPKTNKYENKRLLYNQNNAESNAHHAPLSDGKTGSSYPHWFTNGYDGDGKILKGRTPIKWGNSDCDRPPKHSKNGDGKNDHYLLEFPTFPDGHQYNFDSKKPKEDPGPARVIYTYPNKVFCGIVAHTRENQGDLKLCSH
Expression Region:
28-177aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length of Mature Protein
Pathway:
Mol. Weight:
24.5 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:
Transcription
Function:
Involvement in disease:
Relevance:
Clavin has the same substrate specificity as alpha-sarcin. It is specific for purines in both single- and double-stranded RNA. Its toxic action on eukaryotic cells is the result of cleavage of a single phosphodiester bond in the 60S subunit of ribosomes.
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:
Reference:
"Clavin, a type-1 ribosome-inactivating protein from Aspergillus clavatus IFO 8605. cDNA isolation, heterologous expression, biochemical and biological characterization of the recombinant protein." Parente D., Raucci G., Celano B., Pacilli A., Zanoni L., Canevari S., Adobati E., Colnaghi M.I., Dosio F., Arpicco S., Cattel L., Mele A., de Santis R. Eur. J. Biochem. 239:272-280(1996)
