Matrin 3 Antibody (Rabbit mAb) [D18G16]

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000 IHC1:2000 IF1:250 - 1:1500 FCM1:220

Application
WB, IHC, IF, FCM

Reactivity
Mouse, Rat, Human

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
95 kDa 125 kDa
^*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.

Positive Control	Human brain tissue; Human ovarian carcinoma tissue; Human colon tissue; Mouse brain tissue; Human lung carcinoma tissue; Human uterus tissue; Human breast carcinoma tissue; Rat brain tissue; Rat liver tissue; Mouse liver tissue; HAP1 cells; HEK-293 cells; HepG2 cells; K562 cells; HeLa cells; HEK293T cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Matrin 3 Antibody (Rabbit mAb) [D18G16] detects endogenous levels of total Matrin 3 protein.

Clone
D18G16

Synonym(s)
KIAA0723, MATR3, Matrin-3

Background
Matrin-3 is a highly conserved inner nuclear matrix protein built from two zinc finger domains and two RNA recognition motifs, and it interacts with RNA in a sequence-independent, RNA-dependent manner primarily through its second RNA recognition motif, RRM2, which mediates association with a defined set of RNA-processing partner proteins rather than functioning as an isolated RNA-binding module. Matrin-3 is phosphorylated by the DNA damage-responsive kinase ATM, directly linking this nuclear matrix protein to the cellular double-strand break response, and RNA immunoprecipitation sequencing of Matrin-3-bound transcripts identifies a defined set of small noncoding RNA species along with dozens of messenger RNA transcripts whose steady-state abundance depends on Matrin-3 presence, establishing a direct role for Matrin-3 in stabilizing specific mRNA species against degradation rather than in bulk transcript processing. Separately, Matrin-3 functions as a core structural component of a large ribonucleoprotein assembly termed the HDP-RNP complex, built around the long noncoding RNA NEAT1 and the protein HEXIM1, and this complex additionally incorporates DNA-PK catalytic subunit components, Ku70 and Ku80, together with the paraspeckle proteins SFPQ, NONO, PSPC1, RBM14, and Matrin-3 itself; HEXIM1 binding to NEAT1 is required for assembly of this entire complex. The HDP-RNP interacts directly with the cytosolic DNA sensor cGAS and its DNA-binding partner PQBP1, and introduction of foreign DNA remodels this cGAS-HDP-RNP interaction, triggering release of the paraspeckle protein components, recruitment of STING, and activation of both DNA-PK catalytic activity and IRF3, thereby coupling foreign DNA detection to type I interferon transcriptional output through the cGAS-STING-IRF3 axis. Because Matrin-3 sits within this multiprotein platform as one of several structurally interdependent components whose release is triggered by DNA sensing, its function in innate immune signaling depends on the intact assembly of the surrounding NEAT1-HEXIM1-paraspeckle scaffold rather than on Matrin-3 acting as an independent DNA sensor. Point mutations in MATR3 are established causes of amyotrophic lateral sclerosis and of a distal myopathy presenting with vocal cord and pharyngeal weakness, and because Matrin-3 operates simultaneously in mRNA stability control through its RRM2 domain and in DNA-sensing innate immune signaling through HDP-RNP complex assembly, it represents a defined molecular link between nuclear RNA metabolism and antiviral immune activation relevant to researchers studying both neuromuscular disease and cytosolic DNA-sensing pathways.

Background

Matrin-3 is a highly conserved inner nuclear matrix protein built from two zinc finger domains and two RNA recognition motifs, and it interacts with RNA in a sequence-independent, RNA-dependent manner primarily through its second RNA recognition motif, RRM2, which mediates association with a defined set of RNA-processing partner proteins rather than functioning as an isolated RNA-binding module. Matrin-3 is phosphorylated by the DNA damage-responsive kinase ATM, directly linking this nuclear matrix protein to the cellular double-strand break response, and RNA immunoprecipitation sequencing of Matrin-3-bound transcripts identifies a defined set of small noncoding RNA species along with dozens of messenger RNA transcripts whose steady-state abundance depends on Matrin-3 presence, establishing a direct role for Matrin-3 in stabilizing specific mRNA species against degradation rather than in bulk transcript processing. Separately, Matrin-3 functions as a core structural component of a large ribonucleoprotein assembly termed the HDP-RNP complex, built around the long noncoding RNA NEAT1 and the protein HEXIM1, and this complex additionally incorporates DNA-PK catalytic subunit components, Ku70 and Ku80, together with the paraspeckle proteins SFPQ, NONO, PSPC1, RBM14, and Matrin-3 itself; HEXIM1 binding to NEAT1 is required for assembly of this entire complex. The HDP-RNP interacts directly with the cytosolic DNA sensor cGAS and its DNA-binding partner PQBP1, and introduction of foreign DNA remodels this cGAS-HDP-RNP interaction, triggering release of the paraspeckle protein components, recruitment of STING, and activation of both DNA-PK catalytic activity and IRF3, thereby coupling foreign DNA detection to type I interferon transcriptional output through the cGAS-STING-IRF3 axis. Because Matrin-3 sits within this multiprotein platform as one of several structurally interdependent components whose release is triggered by DNA sensing, its function in innate immune signaling depends on the intact assembly of the surrounding NEAT1-HEXIM1-paraspeckle scaffold rather than on Matrin-3 acting as an independent DNA sensor. Point mutations in MATR3 are established causes of amyotrophic lateral sclerosis and of a distal myopathy presenting with vocal cord and pharyngeal weakness, and because Matrin-3 operates simultaneously in mRNA stability control through its RRM2 domain and in DNA-sensing innate immune signaling through HDP-RNP complex assembly, it represents a defined molecular link between nuclear RNA metabolism and antiviral immune activation relevant to researchers studying both neuromuscular disease and cytosolic DNA-sensing pathways.

References
https://pubmed.ncbi.nlm.nih.gov/21858232/ https://pubmed.ncbi.nlm.nih.gov/28712728/

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%