Analytical Data
-
Gene name
gmhA
- Application
-
Alternative Names
gmhA；lpcA；tfrA；yafI；Phosphoheptose isomerase
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P63224
-
Expression Region
1-192aa
-
AA Sequence
MYQDLIRNELNEAAETLANFLKDDANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAISDVSHISCVGNDFGFNDIFSRYVEAVGREGDVLLGISTSGNSANVIKAIAAAREKGMKVITLTGKDGGKMAGTADIEIRVPHFGYADRIQEIHIKVIHILIQLIEKEMVK
-
Molecular Weight
36.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
The study of the gmhA recombinant protein has gained significant attention due to its crucial role in bacterial polysaccharide biosynthesis, particularly in the formation of lipopolysaccharides (LPS) and capsular polysaccharides. GmhA is an enzyme that catalyzes the conversion of GDP-mannose to GDP-4-keto-6-deoxy-D-mannose, a key precursor in the biosynthetic pathway involving the modification of d-mannose, which is essential for the structural integrity and virulence of various pathogenic bacteria. Understanding the function and mechanism of gmhA can provide insights into bacterial pathogenesis and aid in the development of novel antimicrobial agents. Given the rise of antibiotic-resistant strains, targeting polysaccharide biosynthesis represents a promising strategy for novel drug design. Additionally, the recombinant production of gmhA in heterologous systems allows researchers to investigate its enzymatic properties, substrate specificity, and potential as a target for inhibiting bacterial growth. By elucidating the biochemical pathways involving gmhA and its associated proteins, researchers aim to uncover new avenues for intervention in bacterial infections, making this enzyme a focal point in the fields of microbiology, biochemistry, and pharmaceutical research. Through a combination of structural biology, enzymology, and genetic studies, the ongoing research into gmhA not only enhances our understanding of bacterial physiology but also opens up possibilities for the development of innovative therapeutic approaches to combat infectious diseases.
