Purity
Greater than 90% as determined by SDS-PAGE.
Alternative Names
def; fms; b3287; JW3248Peptide deformylase; PDF; EC 3.5.1.88; Polypeptide deformylase
Species
Escherichia coli (strain K12)
Expression Region
2-169aa
Target Protein Sequence
SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYAEEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEKSGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFELEADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEKLDRLKARA
Note: The complete sequence including tag
sequence, target protein sequence and linker sequence could be provided upon request.
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-SUMO-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that
we have in stock, however, if you have any special requirement for the format, please remark your
requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the
glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer,
6% Trehalose, pH 8.0.
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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw
cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature
and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized
form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description
The preparation of this recombinant E.coli def protein was to use gene recombination DNA technology to obtain a recombinant vector connected with a def fragment (2-169aa) that could be translated into the def protein and then transferred it into E.coli cells to express the recombinant def protein molecule. In order to get the target protein with high purity, N-terminal 6xHis-SUMO tag was used in the production. The purity is 90% determined by SDS-PAGE.
Peptide deformylase catalyzes the hydrolytic removal of the N-terminal formyl group from nascent proteins. This is an essential step in bacterial protein synthesis, making PDF an attractive target for antibacterial drug development. Peptide deformylase activity was first reported by Adams in 1968. However, further attempts to purify the enzyme from cell lysates failed because the activity was not stable. The enzyme was not characterized further until the early 1990s, when the deformylase gene, def, was cloned and peptide deformylase was subsequently overexpressed in Escherichia coli. Bacterial peptide deformylase belongs to a new class of metallohydrolases that utilize an Fe2+ ion as the catalytic metal ion. The ferrous ion in peptide deformylase is very unstable and can be quickly and irreversibly oxidized to the ferric ion, resulting in an inactive enzyme.