Analytical Data
-
Gene name
SALa
- Application
-
Alternative Names
SALa；Ectoine dioxygenase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P21749
-
Expression Region
17-139aa
-
AA Sequence
QNGF GQGGYGGQGG FGGFGGLGGQ AGFGGQIGFN GQGGVGGQVG IGQGGVHPGQ GGFAGQGSPN QYQPGYGNPV GSGHFHGGNP VESGHFHGNP HEYPEHHGEH HREHHEHHGH HEHHGHHRH
-
Molecular Weight
14.1 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
SALa protein, derived from the Salvia genus of plants, has garnered significant attention in recent years due to its potential therapeutic applications. Research focusing on SALa protein is primarily driven by its unique biochemical properties, including its ability to modulate various biological pathways. Previous studies have highlighted SALa's role in enhancing antioxidant activity, which is critical for combating oxidative stress associated with numerous diseases, such as cancer and neurodegenerative disorders. Additionally, SALa protein exhibits antimicrobial properties, making it a candidate for developing new antibiotics amid rising resistance to conventional drugs. Understanding the structure-function relationship of SALa through recombinant protein technology allows researchers to elucidate its mechanisms of action, optimize its efficacy, and explore its use in biomedical applications. The ongoing research aims to harness SALa's diverse functionalities, paving the way for innovative therapeutic strategies that could significantly impact human health. Through interdisciplinary collaborations combining molecular biology, pharmacology, and biotechnology, the full potential of SALa protein can be unlocked, fostering the development of novel treatments that address pressing health challenges.
