PLCβ1 Antibody [N12B19] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:100- 1:1000 IHC1:50-1:500 IF1:50-1:500

Application
WB, IP, IHC, IF, ELISA

Reactivity
Mouse, Rat, Human

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
150 kDa

Positive Control	Human brain; Mouse brain; Human cerebral cortex tissue
Negative Control

Datasheet & SDS

Biological Description

Specificity
PLCβ1 Antibody [N12B19] detects endogenous levels of total PLCβ1 protein.

Clone
N12B19

Synonym(s)
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1; PLC-154; Phosphoinositide phospholipase C-beta-1; Phospholipase C-I (PLC-I); Phospholipase C-beta-1 (PLC-beta-1); PLCB1; KIAA0581

Background
PLC beta 1, or phospholipase C beta 1, is a key effector enzyme of the PLC-beta subfamily that acts downstream of G protein-coupled receptors to hydrolyze membrane phosphatidylinositol-4,5-bisphosphate into the second messengers inositol 1,4,5-trisphosphate, which triggers calcium release, and diacylglycerol, which activates protein kinase C, primarily in response to stimulation by G alpha q/11 and G beta gamma subunits. PLC beta 1 contains an N-terminal pleckstrin homology domain for binding phosphatidylinositol-4,5-bisphosphate and G beta gamma, four EF-hand motifs for calcium coordination, a catalytic TIM-barrel formed by X and Y domains housing the active site, a C2 domain for calcium and phospholipid docking, and an approximately four-hundred-residue C-terminal extension. This C-terminal segment is divided into a proximal C-terminal domain for G alpha q helical domain binding, a flexible linker, and a distal C-terminal domain with a coiled-coil structure important for membrane tubulation and caveolae association. Splice variants PLC beta 1a and PLC beta 1b differ in their C-termini, with the former containing a PDZ motif and the latter a proline-rich region. The core function of PLC beta 1 involves G alpha q bound to GTP interacting with the proximal C-terminal domain to relieve autoinhibition and enable phosphatidylinositol-4,5-bisphosphate hydrolysis at the XY interface, catalyzed by a histidine and glutamate dyad. This activity is further amplified by G beta gamma at the pleckstrin homology domain and membrane recruitment via the C2, EF, and C-terminal regions. Basal activity is low, and isoforms differ in their sensitivity to Gq proteins. PLC beta 1 is involved in regulating calcium oscillations, myogenesis through beta-catenin, c-Jun, and cyclin D3, osteogenesis and hematopoiesis, neuronal signaling, and the nuclear G1 to S phase transition, with PLC beta 1a and PLC beta 1b showing distinct roles; PLC beta 1b also scaffolds with Homer and Shank proteins at the sarcolemma. Dysregulation of PLC beta 1 is linked to diseases such as schizophrenia, bipolar disorder, and cancer through aberrant calcium and PKC signaling, and its distal C-terminal domain acts as a sensor of membrane curvature to modulate activity.

Background

PLC beta 1, or phospholipase C beta 1, is a key effector enzyme of the PLC-beta subfamily that acts downstream of G protein-coupled receptors to hydrolyze membrane phosphatidylinositol-4,5-bisphosphate into the second messengers inositol 1,4,5-trisphosphate, which triggers calcium release, and diacylglycerol, which activates protein kinase C, primarily in response to stimulation by G alpha q/11 and G beta gamma subunits. PLC beta 1 contains an N-terminal pleckstrin homology domain for binding phosphatidylinositol-4,5-bisphosphate and G beta gamma, four EF-hand motifs for calcium coordination, a catalytic TIM-barrel formed by X and Y domains housing the active site, a C2 domain for calcium and phospholipid docking, and an approximately four-hundred-residue C-terminal extension. This C-terminal segment is divided into a proximal C-terminal domain for G alpha q helical domain binding, a flexible linker, and a distal C-terminal domain with a coiled-coil structure important for membrane tubulation and caveolae association. Splice variants PLC beta 1a and PLC beta 1b differ in their C-termini, with the former containing a PDZ motif and the latter a proline-rich region. The core function of PLC beta 1 involves G alpha q bound to GTP interacting with the proximal C-terminal domain to relieve autoinhibition and enable phosphatidylinositol-4,5-bisphosphate hydrolysis at the XY interface, catalyzed by a histidine and glutamate dyad. This activity is further amplified by G beta gamma at the pleckstrin homology domain and membrane recruitment via the C2, EF, and C-terminal regions. Basal activity is low, and isoforms differ in their sensitivity to Gq proteins. PLC beta 1 is involved in regulating calcium oscillations, myogenesis through beta-catenin, c-Jun, and cyclin D3, osteogenesis and hematopoiesis, neuronal signaling, and the nuclear G1 to S phase transition, with PLC beta 1a and PLC beta 1b showing distinct roles; PLC beta 1b also scaffolds with Homer and Shank proteins at the sarcolemma. Dysregulation of PLC beta 1 is linked to diseases such as schizophrenia, bipolar disorder, and cancer through aberrant calcium and PKC signaling, and its distal C-terminal domain acts as a sensor of membrane curvature to modulate activity.

References
https://pubmed.ncbi.nlm.nih.gov/23880553/ https://pubmed.ncbi.nlm.nih.gov/33422547/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%