Analytical Data
-
Gene name
CLVS2
- Application
-
Alternative Names
Retinaldehyde-binding protein 1-like 2
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q5SYC1
-
Expression Region
1-327aa
-
Molecular Weight
54 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
The CLVS2 protein, or Cathepsin L-like protein 2, has garnered attention in recent years due to its potential roles in various physiological and pathological processes. CLVS2 is believed to be involved in cellular signaling pathways and may have implications in developmental biology and disease mechanisms, particularly in relation to immunity and inflammation. Research indicates that CLVS2 may play a critical role in the regulation of cellular processes such as apoptosis, autophagy, and cytokine secretion. Abnormal expression or activity of CLVS2 has been associated with several diseases, including cancer and autoimmune disorders, prompting investigations into its functional properties and signaling mechanisms. The recombinant expression and characterization of CLVS2 allow researchers to better understand its structure-function relationships and develop targeted therapeutic strategies. By creating recombinant forms of the CLVS2 protein, scientists can study its interactions with other biomolecules, assess its enzymatic activities, and explore its potential as a biomarker or a therapeutic target. Consequently, studies on CLVS2 are not only important for elucidating its basic biological functions but also for uncovering its roles in disease and potential applications in medicine.
