Analytical Data
-
Gene name
PPP1R1C
- Application
-
Alternative Names
PPP1R1C；Protein phosphatase 1 regulatory subunit 1C
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8WVI7
-
Expression Region
1-109aa
-
AA Sequence
MEPNSPKKIQ FAVPVFQSQI APEAAEQIRK RRPTPASLVI LNEHNPPEID DKRGPNTQGE LQNASPKQRK QSVYTPPTIK GVKHLKGQNE SAFPEEEEGT NEREEQRDH
-
Molecular Weight
12.3 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
PPP1R1C, also known as Protein Phosphatase 1 Regulatory Inhibitor Subunit 1C, is a critical regulatory component in the protein phosphatase 1 (PP1) complex, playing a significant role in various cellular processes, including cell division, muscle contraction, and neuron signaling. The regulation of protein phosphorylation through PP1 is essential for maintaining cellular homeostasis and responding to external stimuli. Aberrant regulation of this pathway has been linked to numerous diseases, including cancer, neurodegenerative disorders, and cardiovascular conditions. Recent studies have highlighted the importance of PPP1R1C in modulating PP1 activity and its implications in pathological states. Researchers aim to understand the structure-function relationship of the PPP1R1C protein, develop recombinant forms for functional assays, and explore potential therapeutic interventions targeting this pathway. By employing techniques such as protein purification and crystallization, scientists can elucidate the molecular mechanisms underlying PPP1R1C's regulatory functions, paving the way for the development of targeted therapies that could mitigate the effects of diseases associated with dysregulated protein phosphorylation.
