Analytical Data
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Gene name
pdh
- Application
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Alternative Names
pdh;PHD finger Protein 23
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08559
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Expression Region
31-390aa
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AA Sequence
ANDATFEIKK CDLHRLEEGP PVTTVLTRED GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA HGFTFTRGLS VREILAELTG RKGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST DYYKRGDFIP GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP LEELGYHIYS SDPPFEVRGA NQWIKFKSVS
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Molecular Weight
43.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Phosphoenolpyruvate-dependent phosphotransferase system (PTS) plays a crucial role in bacterial carbohydrate transport and metabolism, with phosphoenolpyruvate (PEP) acting as the primary energy source for this process. Among the various proteins involved in this system, the phosphotransferase protein, known as Pdh (phosphoenolpyruvate-dependent dihydroxyacetone kinase), has garnered significant attention in biochemical research. Pdh is essential for the efficient conversion of PEP into various metabolic intermediates, thereby influencing cellular energy levels and substrate utilization. The study of Pdh and its recombinant forms has implications for understanding bacterial growth patterns, metabolism regulation, and enzyme kinetics. Furthermore, recombinant Pdh can be harnessed for biotechnological applications, including the development of biosensors and metabolic engineering strategies aimed at optimizing biofuel production and enhancing industrial fermentation processes. Investigating the structural and functional characteristics of recombinant Pdh proteins can provide insights into their catalytic mechanisms and regulatory roles, which may lead to novel therapeutic approaches against bacterial infections and the enhancement of beneficial microbial strains in agricultural and environmental contexts. Overall, research on recombinant Pdh proteins continues to expand our understanding of bacterial metabolism and presents new avenues for innovation in biotechnology.










