PACT (PKR activating protein) / PRKRA Antibody (Rabbit mAb) [E15C21]

Application: Reactivity: Human, Monkey

Usage Information

Dilution
WB1:1000 IP1:50

Application
WB, IP

Reactivity
Human, Monkey

Source
Rabbit 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 Observed MW
30 kDa N/A
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
PACT Antibody (Rabbit mAb) [E15C21] detects endogenous levels of total PACT protein.

Clone
E15C21

Synonym(s)
DYT16; HSD14; PACT; PKR-associated protein X; PRKRA; Protein kinase, interferon-inducible double-stranded RNA-dependent activator; RAX

Background
PACT belongs to the family of double-stranded RNA-binding proteins that regulate innate immune and stress-response signaling through direct protein-protein interactions rather than enzymatic activity of their own, and it carries tandem double-stranded RNA-binding motifs that mediate its engagement with multiple partner proteins. PACT functions as a direct cellular activator of protein kinase R, engaging PKR independently of viral double-stranded RNA and instead responding to cellular stress signals such as serum starvation and oxidative insult; this interaction triggers PKR autophosphorylation and subsequent phosphorylation of eIF2α, producing a transient attenuation of global protein synthesis as part of the integrated stress response, and sustained or dysregulated signaling through this axis can shift the pathway from a protective outcome toward apoptosis. Beyond PKR activation, PACT associates with the RNA interference machinery, forming a complex with Dicer and Argonaute2 that supports processing of small interfering RNA and influences the efficiency of microRNA accumulation, linking a single dsRNA-binding scaffold to both translational control and post-transcriptional gene silencing. PACT additionally binds directly to the C-terminal repression domain of RIG-I, a cytosolic viral RNA sensor, and this interaction stimulates the ATPase activity of RIG-I and potentiates RIG-I-driven type I interferon production independently of PKR or Dicer engagement, extending PACT's regulatory reach into antiviral innate immune signaling and positioning it as a convergence point across three distinct pathways. Physiological roles for PACT extend to development, since loss of the murine ortholog produces craniofacial and pituitary developmental defects alongside fertility impairment, indicating functions beyond acute stress signaling. Mutations in the gene encoding PACT are linked to dystonia, a movement disorder featuring involuntary muscle contractions, and disease-associated variants alter dsRNA-binding capacity and disrupt normal PKR regulation, producing dysregulated eIF2α signaling and a compromised stress response in affected cells.

Background

PACT belongs to the family of double-stranded RNA-binding proteins that regulate innate immune and stress-response signaling through direct protein-protein interactions rather than enzymatic activity of their own, and it carries tandem double-stranded RNA-binding motifs that mediate its engagement with multiple partner proteins. PACT functions as a direct cellular activator of protein kinase R, engaging PKR independently of viral double-stranded RNA and instead responding to cellular stress signals such as serum starvation and oxidative insult; this interaction triggers PKR autophosphorylation and subsequent phosphorylation of eIF2α, producing a transient attenuation of global protein synthesis as part of the integrated stress response, and sustained or dysregulated signaling through this axis can shift the pathway from a protective outcome toward apoptosis. Beyond PKR activation, PACT associates with the RNA interference machinery, forming a complex with Dicer and Argonaute2 that supports processing of small interfering RNA and influences the efficiency of microRNA accumulation, linking a single dsRNA-binding scaffold to both translational control and post-transcriptional gene silencing. PACT additionally binds directly to the C-terminal repression domain of RIG-I, a cytosolic viral RNA sensor, and this interaction stimulates the ATPase activity of RIG-I and potentiates RIG-I-driven type I interferon production independently of PKR or Dicer engagement, extending PACT's regulatory reach into antiviral innate immune signaling and positioning it as a convergence point across three distinct pathways. Physiological roles for PACT extend to development, since loss of the murine ortholog produces craniofacial and pituitary developmental defects alongside fertility impairment, indicating functions beyond acute stress signaling. Mutations in the gene encoding PACT are linked to dystonia, a movement disorder featuring involuntary muscle contractions, and disease-associated variants alter dsRNA-binding capacity and disrupt normal PKR regulation, producing dysregulated eIF2α signaling and a compromised stress response in affected cells.

References
https://pubmed.ncbi.nlm.nih.gov/25554729/ https://pubmed.ncbi.nlm.nih.gov/21501829/

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%