Analytical Data
-
Gene name
NEU3
- Application
-
Alternative Names
NEU3；NEURL3；E3 ubiquitin-Protein ligase NEURL1B
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9UQ49
-
Expression Region
2-428aa
-
AA Sequence
EEVTTCSFNSPLFRQEDDRGITYRIPALLYIPPTHTFLAFAEKRSTRRDEDALHLVLRRGLRIGQLVQWGPLKPLMEATLPGHRTMNPCPVWEQKSGCVFLFFICVRGHVTERQQIVSGRNAARLCFIYSQDAGCSWSEVRDLTEEVIGSELKHWATFAVGPGHGIQLQSGRLVIPAYTYYIPSWFFCFQLPCKTRPHSLMIYSDDLGVTWHHGRLIRPMVTVECEVAEVTGRAGHPVLYCSARTPNRCRAEALSTDHGEGFQRLALSRQLCEPPHGCQGSVVSFRPLEIPHRCQDSSSKDAPTIQQSSPGSSLRLEEEAGTPSESWLLYSHPTSRKQRVDLGIYLNQTPLEAACWSRPWILHCGPCGYSDLAALEEEGLFGCLFECGTKQECEQIAFRLFTHREILSHLQGDCTSPGRNPSQFKSN
-
Molecular Weight
52.1 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
NEU3, a sialidase enzyme, plays a crucial role in the metabolism of sialic acids, which are important components of glycoproteins and glycolipids on cell surfaces. Research has shown that NEU3 is involved in various physiological processes, including cell adhesion, immune response, and signaling pathways. Its dysregulation has been linked to several pathological conditions, such as cancer, where altered sialic acid expression can influence tumor progression and metastasis. The study of NEU3 recombinant protein has gained significant attention in recent years due to its potential therapeutic implications. By producing NEU3 in a recombinant form, researchers can investigate its enzymatic activity, substrate specificity, and interactions with other cellular components in detail. This understanding could pave the way for novel cancer treatments or interventions in diseases associated with sialic acid metabolism. Furthermore, NEU3's role in modulating cell signaling makes it a valuable target for drug development, as restoring its normal function may help counteract some of the damaging effects seen in disease states. Thus, the exploration of NEU3 recombinant protein not only enhances our basic understanding of sialidase functions but also opens avenues for innovative therapeutic strategies in oncology and other fields aligned with aberrant sialic acid biology.
