Recombinant Staphylococcus haemolyticus Dihydropteroate synthase(folP) CSB-EP682423SLF
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Dihydropteroate pyrophosphorylase
Species: (Organism)
Staphylococcus haemolyticus
Gene Names:
folP
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
MTKTKIIGILNVTPDSFSDGGKYNSVDKAIARAKEMIDEGVDIIDVGGVSTRPGHTEVSLEEEMERVVPVVEQLVKLDVQISVDTYRSEVAEACLKLGATMINDQWAGLYDPKIFDVVSDYNAEIVLMHNGDGQREQPVVEEMLLSLLTQANKAEMAGIEKGNIWLDPGIGFAKSRSEEKEVMARLDELVATEYPVLLATSRKRFIKEMIGKETTPAERDEATAATTVYGIMKGIQAVRVHNVDLNVKLAQSIDFLKENEHERHHLS
Expression Region:
1-267aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length
Pathway:
Mol. Weight:
33.6 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:
Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
Involvement in disease:
Relevance:
Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
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:
DHPS family
Reference:
"Functional cloning of the dihydropteroate synthase gene of Staphylococcus haemolyticus." Kellam P., Dallas W.S., Ballantine S.P., Delves C.J. FEMS Microbiol. Lett. 134:165-169(1995)
