Analytical Data
-
Gene name
VF
- Application
-
Alternative Names
VF；C7orf9；RFRP；Pro-FMRFamide-related neuropeptide VF
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9HCQ7
-
Expression Region
56-92aa
-
AA Sequence
SLNFE ELKDWGPKNV IKMSTPAVNK MPHSFANLPL RF
-
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
VF recombinant proteins have gained significant attention in the fields of biotechnology and medicine due to their diverse applications and therapeutic potential. VF proteins are originally derived from various organisms, including bacteria, fungi, and plants, and are engineered to enhance their functional properties for specific purposes. The production of recombinant VF proteins enables researchers to study protein interactions, mechanisms of action, and disease pathways in a controlled environment. Moreover, these proteins are crucial in developing vaccines, diagnostic tools, and enzyme-based therapies. As advancements in genetic engineering, such as CRISPR and synthetic biology, continue to evolve, the ability to optimize VF proteins for improved efficacy and safety becomes increasingly feasible. The rising prevalence of infectious diseases, cancers, and metabolic disorders has further driven research toward the utilization of VF proteins for innovative treatment strategies. Current studies focus on the production efficiency, purification methods, structural characterization, and functional analysis of VF recombinant proteins, leading to promising developments in drug design and personalized medicine. These groundbreaking discoveries hold great potential for revolutionizing therapeutic approaches and addressing global health challenges.
