Analytical Data
-
Gene name
CU
- Application
-
Alternative Names
Dutch elm disease toxin
-
Species
Ophiostoma ulmi
-
Source
Yeast
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q06153
-
Expression Region
26-100aa
-
Molecular Weight
9.6 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
CU recombinant proteins have emerged as a significant area of research in the field of molecular biology and biotechnology. These proteins, which are synthesized through recombinant DNA technology, offer valuable insights into various biological processes and structural functions. The background of CU recombinant protein research is rooted in the need for high-quality, specific proteins for therapeutic and diagnostic applications. Historically, the production of proteins in native systems was challenging due to low yields, complex purification processes, and post-translational modifications. The advent of recombinant technology has allowed scientists to insert specific genes encoding proteins of interest into host cells, such as bacteria, yeast, or mammalian cells, facilitating large-scale production. Furthermore, CU recombinant proteins have been pivotal in the development of vaccines, antibody production, and enzyme engineering. Their use has expanded our understanding of protein folding, interactions, and functionality. With advancements in genetic engineering techniques, including CRISPR and synthetic biology, the versatility and application of CU recombinant proteins continue to grow, paving the way for innovative therapeutic solutions and contributing significantly to the fields of medicine, agriculture, and industrial biotechnology.
