Analytical Data
-
Gene name
botD
- Application
-
Alternative Names
botD；KIAA1054；Synaptic vesicle glycoProtein 2C
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P19321
-
Expression Region
1-442aa
-
AA Sequence
MTWPVKDFNYSDPVNDNDILYLRIPQNKLITTPVKAFMITQNIWVIPERFSSDTNPSLSKPPRPTSKYQSYYDPSYLSTDEQKDTFLKGIIKLFKRINERDIGKKLINYLVVGSPFMGDSSTPEDTFDFTRHTTNIAVEKFENGSWKVTNIITPSVLIFGPLPNILDYTASLTLQGQQSNPSFEGFGTLSILKVAPEFLLTFSDVTSNQSSAVLGKSIFCMDPVIALMHELTHSLHQLYGINIPSDKRIRPQVSEGFFSQDGPNVQFEELYTFGGLDVEIIPQIERSQLREKALGHYKDIAKRLNNINKTIPSSWISNIDKYKKIFSEKYNFDKDNTGNFVVNIDKFNSLYSDLTNVMSEVVYSSQYNVKNRTHYFSRHYLPVFANILDDNIYTIRDGFNLTNKGFNIENSGQNIERNPALQKLSSESVVDLFTKVCLRLTK
-
Molecular Weight
52.5 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
BotD is a recombinant protein derived from the Botulinum toxin, specifically designed to study its physiological effects and therapeutic potential while minimizing the risks associated with its native form. The broader context of this research stems from the need to understand the mechanisms of neurotoxins, particularly their applications in medicine, such as in the treatment of various neurological disorders and cosmetic procedures. Botulinum toxin, known for causing botulism, is also recognized for its ability to induce muscle paralysis, making it a valuable tool in clinical settings. By utilizing recombinant DNA technology, researchers can produce BotD in a controlled manner, allowing for detailed investigation of its structure-function relationships and potential uses. This includes exploring its binding affinities, mechanisms of action, and possible therapeutic applications in conditions like dystonia, migraines, and spasticity. Furthermore, studying BotD contributes to the development of safer and more effective treatments, advancing our understanding of protein engineering and toxin biology. The compilation of knowledge surrounding BotD is essential for both scientific inquiry and therapeutic innovations in neurology, ultimately aiming to improve patient outcomes while ensuring safety.
