Analytical Data
-
Gene name
ndkC-1
- Application
-
Alternative Names
NDK;NDP kinase
-
Species
Dictyostelium discoideum
-
Source
E. coli
-
Tag
N- His-V5
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P22887
-
Expression Region
1-155aa
-
Molecular Weight
24.2 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 NDKC-1 protein, a member of the nucleoside diphosphate kinase (NDK) family, plays a critical role in cellular processes, particularly in the regulation of nucleoside triphosphate (NTP) levels and the maintenance of cellular energy homeostasis. Research into NDKC-1 has gained traction due to its involvement in various biological mechanisms, including signal transduction and DNA/RNA synthesis, highlighting its potential implications in cancer biology and other diseases where cellular energy metabolism is disrupted. Studies suggest that NDKC-1 may act as a molecular switch, influencing cellular responses to stress and promoting cell survival under unfavorable conditions. Moreover, the re-combinational aspect of NDKC-1 offers insights into its structural and functional dynamics, providing opportunities to explore its enzymatic capabilities and interactions with other cellular molecules. Understanding the properties of NDKC-1 through recombinant protein research could pave the way for novel therapeutic strategies aimed at targeting metabolic pathways in diseases characterized by aberrant NDK functions. This investigation not only addresses the fundamental biochemical functions of NDKC-1 but also its broader implications in health and disease, making it a promising candidate for further exploration in the fields of biochemistry and molecular biology.
