Recombinant Amylomyces rouxii Chitin deacetylase CSB-EP344641AJI
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Chitin deacetylase; EC 3.5.1.41
Species: (Organism)
Amylomyces rouxii(Filamentous fungus)(Mucor rouxii)
Gene Names:
N/A
Tag info:
N-terminal 10xHis-tagged
Target Protein AA Sequence:
DTSANYWQSFTSQINPKNISIPSIEQTSSIDPTQECAYYTPDASLFTFNASEWPSIWEVATTNGMNESAEFLSVYNSIDWTKAPNISVRTLDANGNLDTTGYNTATDPDCWWTATTCTSPKISDINDDISKCPEPETWGLTYDDGPNCSHNAFYDYLQEQKLKASMFYIGSNVVDWPYGAMRGVVDGHHIASHTWSHPQMTTKTNQEVLAEFYYTQKAIKLATGLTPRYWRPPYGDIDDRVRWIASQLGLTAVIWNLDTDDWSAGVTTTVEAVEQSYSDYIAMGTNGTFANSGNIVLTHEINTTMSLAVENLPKIISAYKQVIDVATCYNISHPYFEDYEWTNVLNGTKSSATASGSATSASASGGATTAAAHIQASTSGAMSVLPNLALISAFIATLLF
Expression Region:
22-421aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length of Mature Protein
Pathway:
Mol. Weight:
49.9 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:
Others
Function:
Involvement in disease:
Relevance:
Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin. This enzyme specifically acts on beta-1-4-linked N-acetylglucosamine homopolymers and requires at least 4 residues for catalysis.
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:
"The primary structure of a fungal chitin deacetylase reveals the function for two bacterial gene products." Kafetzopoulos D., Thireos G., Vournakis J.N., Bouriotis V. Proc. Natl. Acad. Sci. U.S.A. 90:8005-8008(1993)
