Analytical Data
-
Gene name
CALB1
- Application
-
Alternative Names
(Calbindin D28)(D-28K)(Vitamin D-dependent calcium-binding protein, avian-type)
-
Species
Human
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P05937
-
Expression Region
2-261aa
-
Molecular Weight
37.3 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
S100G is a member of the S100 protein family, characterized by its EF-hand calcium-binding motif, which is crucial in various cellular processes such as cell growth, differentiation, and regulation of cytoskeletal dynamics. Research on S100G has gained significance due to its involvement in numerous physiological and pathological conditions, including cancer. Its expression is often dysregulated in tumor tissues, making it a potential biomarker for cancer diagnostics and a target for therapeutic interventions. Recent studies have focused on the structural and functional aspects of S100G, exploring its interactions with other proteins and its role in signaling pathways. This research aims to elucidate the molecular mechanisms underlying S100G's effects on tumor progression and to assess its potential as a therapeutic target. Additionally, recombinant S100G protein has been produced to facilitate these studies, enabling detailed investigations into its biochemical properties and functional roles in cellular contexts. Understanding the role of S100G in cancer and other diseases could pave the way for novel treatment strategies and improve diagnostic accuracy, highlighting the importance of ongoing research in this area.
