Analytical Data
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Gene name
PKIg
- Application
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Alternative Names
PKIg；cAMP-dependent Protein kinase inhibitor gamma
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O70139
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Expression Region
1-76aa
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AA Sequence
MMEVESSYSD FISCDRTGRR NAVPDIQGDS EAVSVRKLAG DMGELALEGA EGQAEGSTPD KEASSQPESS DANTSS
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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 study of PKIg (Protein Kinase G, type I gamma) recombinant proteins has gained significant attention due to its pivotal role in various physiological and pathological processes. PKIg is a serine/threonine kinase that is activated by cyclic GMP, playing a crucial role in the signaling pathways that regulate smooth muscle relaxation, platelet aggregation, and neuronal signaling. Understanding the function and regulation of PKIg is vital for elucidating its contributions to cardiovascular health, neurobiology, and cancer biology. The production of recombinant PKIg proteins allows for detailed biochemical and structural studies, facilitating the investigation of its enzymatic activity, substrate specificity, and interaction with other cellular proteins. Moreover, insights gained from recombinant PKIg studies are essential for exploring its potential as a therapeutic target in diseases associated with aberrant signaling pathways, such as hypertension and heart failure. The ability to manipulate and study PKIg in vitro also paves the way for the development of novel pharmacological agents that can selectively modulate its activity, potentially leading to innovative treatments. Thus, the research on PKIg recombinant proteins is not only foundational for understanding basic biological mechanisms but also holds promise for translating these findings into clinical applications.
