Analytical Data
-
Gene name
ARTN
- Application
-
Alternative Names
ARTN；EVN；Artemin
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q5T4W7
-
Expression Region
108-220aa
-
AA Sequence
AGGPGSRARAAGARGCRLRSQLVPVRALGLGHRSDELVRFRFCSGSCRRARSPHDLSLASLLGAGALRPPPGSRPVSQPCCRPTRYEAVSFMDVNSTWRTVDRLSATACGCLG
-
Molecular Weight
47.1 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
ARTN, or Artin M, is a recombinant protein derived from the seeds of the Artocarpus heterophyllus, commonly known as jackfruit. This protein has garnered significant attention in recent years due to its unique biological properties and potential therapeutic applications. Research on ARTN has primarily focused on its immunomodulatory effects, as it has been shown to influence the activity of various immune cells, including T cells and macrophages. These properties make ARTN a promising candidate for the development of novel treatments for autoimmune diseases, cancer immunotherapy, and infectious diseases. Furthermore, studies have indicated that ARTN could play a role in tissue regeneration and wound healing, highlighting its potential in regenerative medicine. Given the increasing prevalence of diseases that challenge current treatment strategies, the exploration of ARTN as a recombinant protein is crucial. It represents a significant advancement in our understanding of plant-derived proteins and their applicability in biotechnology and medicine. The ongoing research aims to elucidate the mechanisms of action of ARTN, optimize its production methods, and evaluate its efficacy and safety in clinical settings. Overall, ARTN's unique properties position it as a valuable subject for further investigation in the fields of immunology and therapeutics.
