Analytical Data
-
Gene name
Secretogranin-2
- Application
-
Alternative Names
SN; SgII; CHGC; Chromogranin C; Secretoneurin
-
Species
Mouse
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q03517
-
Expression Region
Gln342~Leu609
-
Molecular Weight
39kDa
-
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
Secretogranin-2 (SgII), a member of the secretogranin family, is a protein predominantly expressed in neuroendocrine tissues. It plays a significant role in the packaging and secretion of neuropeptides and hormones, influencing various physiological processes, including neurodevelopment, hormone regulation, and neurotransmission. Studies have indicated that SgII may be involved in the pathophysiology of several conditions, such as neurodegenerative diseases and certain cancers, making it a potential biomarker for early diagnosis and therapeutic targets. The recombinant production of SgII has garnered attention, as it allows for the exploration of its functional properties in controlled experimental settings. By expressing and purifying this protein, researchers can investigate its structural characteristics, interactome, and biological activities, providing deeper insights into its role in health and disease. Furthermore, recombinant SgII can serve as a valuable tool for the development of diagnostic assays and therapeutic interventions. Understanding the molecular mechanisms governed by SgII may ultimately contribute to advancing treatment strategies for neuroendocrine disorders and enhancing the comprehension of neuropeptide functions within various biological contexts. Hence, the study of SgII through recombinant protein research is vital for unveiling its biological significance and potential clinical implications.
