Analytical Data
-
Gene name
1.0
- Application
-
Alternative Names
DKK1；Dickkopf-related Protein 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O94907
-
Expression Region
32-266aa
-
AA Sequence
TLNSVLNSNAIKNLPPPLGGAAGHPGSAVSAAPGILYPGGNKYQTIDNYQ PYPCAEDEECGTDEYCASPTRGGDAGVQICLACRKRRKRCMRHAMCCPGN YCKNGICVSSDQNHFRGEIEETITESFGNDHSTLDGYSRRTTLSSKMYHT KGQEGSVCLRSSDCASGLCCARHFWSKICKPVLKEGQVCTKHRRKGSHGL EIFQRCYCGEGLSCRIQKDHHQASNSSRLHTCQRH
-
Molecular Weight
26 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
Recombinant proteins have become a cornerstone of modern biochemistry and biotechnology, driven by advances in genetic engineering and molecular biology. Their development allows for the production of proteins that are identical to those found in nature, or even novel proteins with specific desired functions. The ability to express proteins in various host organisms, such as bacteria, yeast, or mammalian cells, has opened new avenues for research and therapeutic applications. This innovation is particularly significant in the fields of medicine and industry; for instance, recombinant proteins are pivotal in the production of insulin, growth hormones, monoclonal antibodies, and vaccines. Moreover, they serve as vital tools in basic research, enabling scientists to study protein function, cellular processes, and disease mechanisms. As the demand for therapeutic proteins continues to rise, ongoing research focuses on enhancing expression systems, optimizing production yields, and ensuring the correct folding and post-translational modifications of proteins. Challenges such as aggregation, solubility, and scalability of production are actively being addressed, paving the way for more efficient and cost-effective biopharmaceutical manufacturing. Overall, the study of recombinant proteins not only contributes to scientific understanding but also holds the potential to revolutionize healthcare and industrial processes by providing targeted solutions to existing challenges.
