Analytical Data
-
Gene name
ALDOC
- Application
-
Alternative Names
ALDOC；ALDC；Fructose-bisphosphate aldolase C
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P09972
-
Expression Region
1-364aa
-
AA Sequence
MPHSYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVE NTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQD KGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRC VLKISERTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLK RCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYTPEEIA MATVTALRRTVPPAVPGVTFLSGGQSEEEASFNLNAINRCPLPRPWALTF SYGRALQASALNAWRGQRDNAGAATEEFIKRAEVNGLAAQGKYEGSGEDG GAAAQSLYIANHAY
-
Molecular Weight
39 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
Aldose reductase (ALR) is a key enzyme in the polyol pathway, responsible for the reduction of glucose to sorbitol via NADPH. Its overactivity has been implicated in various diabetic complications, such as retinopathy, neuropathy, and nephropathy, highlighting its potential as a therapeutic target. Research into ALR has led to the exploration of its structure and function, leading to the development of recombinant proteins for screening potential inhibitors. The use of recombinant ALR not only facilitates a better understanding of its catalytic mechanisms but also aids in the identification of drug candidates that can selectively inhibit its activity. Advances in protein engineering techniques, such as mutagenesis and molecular modeling, have further enhanced the efficacy and specificity of these inhibitors. The integration of high-throughput screening methods has accelerated the discovery process, allowing for the rapid evaluation of thousands of compounds against the recombinant ALR. Overall, studies on ALR recombinant proteins are crucial for unraveling the complexities of diabetic complications and paving the way for novel therapeutic strategies aimed at alleviating the burden of diabetes-related disorders.
