Analytical Data
-
Gene name
PLCg2
- Application
-
Alternative Names
PLC-IV; Phosphoinositide phospholipase C-gamma-2; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P16885
-
Expression Region
Leu930~Thr1152
-
Molecular Weight
29kDa
-
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
PLCg2, or phospholipase C gamma 2, is a key enzyme that plays a crucial role in various cellular signaling pathways, particularly in immune responses and hematopoiesis. Its importance is underscored by its involvement in the activation of B and T lymphocytes, where it facilitates the generation of inositol trisphosphate and diacylglycerol, second messengers that trigger calcium release and activate protein kinase C pathways. Dysregulation of PLCg2 has been linked to various immunological disorders and cancers, making it a significant target for therapeutic intervention. Studies investigating PLCg2 have focused on its structure, function, and regulatory mechanisms, revealing insights into its catalytic activity and interactions with other signaling molecules. Recombining PLCg2 into specific proteins aids in understanding its enzymatic functions and the implications of its activity in health and disease. Research continues to explore the potential of targeting PLCg2 in drug development to modulate immune responses and address conditions associated with its dysregulation, thus highlighting the ongoing relevance of PLCg2 in biomedical research.











