Alternative Name(s):

CDA2; YLR308W; L2142.1Chitin deacetylase 2; EC 3.5.1.41

Species: (Organism)

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Gene Names:

CDA2

Tag info:

N-terminal 6xHis-tagged

Target Protein AA Sequence:

EANREDLKQIDFQFPVLERAATKTPFPDWLSAFTGLKEWPGLDPPYIPLDFIDFSQIPDYKEYDQNHCDSVPRDSCSFDCHHCTEHDDVYTCSKLSQTFDDGPSASTTKLLDRLKHNSTFFNLGVNIVQHPDIYQRMQKEGHLIGSHTWSHVYLPNVSNEKIIAQIEWSIWAMNATGNHTPKWFRPPYGGIDNRVRAITRQFGLQAVLWDHDTFDWSLLLNDSVITEQEILQNVINWNKSGTGLILEHDSTEKTVDLAIKINKLIGDDQSTVSHCVGGIDYIKEFLS

Expression Region:

26-312aa

Subcellular Location:

Tissue Specificity:

Protein Length:

Full Length of Mature Protein

Pathway:

Mol. Weight:

34.9 kDa

Purity:

Greater than 90% 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:

Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin.

Involvement in disease:

Relevance:

Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin.

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:

Polysaccharide deacetylase family

Reference:

The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.Nature 387:87-90(1997)