Analytical Data
-
Gene name
VCL
- Application
-
Alternative Names
VCL；Vinculin
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P18206
-
Expression Region
2-235aa
-
AA Sequence
PVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVE
-
Molecular Weight
53.0kDa
-
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
Vibrio cholerae lectin (VCL) is a significant research subject due to its role in the pathogenicity of Vibrio cholerae, the bacterium responsible for cholera. VCL facilitates the adhesion of the bacterium to intestinal epithelial cells, which is a crucial step in the infection process. The study of VCL and its recombinant proteins has garnered attention not only for understanding the mechanisms of cholera pathogenesis but also for developing potential therapeutic interventions and vaccines. Utilizing recombinant DNA technology, researchers can produce VCL in a controlled manner, enabling detailed functional analyses and the exploration of its interactions with host cells. This approach allows for the investigation of VCL's structure-function relationships, providing insights into its binding affinities and the molecular underpinnings of its activity. Additionally, the recombinant VCL has potential applications in biomedicine, including as a diagnostic tool for cholera or as a platform for drug delivery systems. By elucidating the properties and behavior of VCL in vitro and in vivo, researchers aim to pave the way for new strategies in combating cholera and improving public health outcomes in regions disproportionately affected by this disease. Overall, the study of VCL recombinant proteins stands at the intersection of microbiology, immunology, and biotechnology, presenting opportunities to advance our understanding of cholera and enhance global health initiatives.
