Datasheet

Biological Description

Specificity	TRIM21 Rabbit mAb detects endogenous levels of total TRIM21 protein.
Background	TRIM21, also known as tripartite motif-containing protein 21 or Ro52, is a member of the TRIM (tripartite motif) family of proteins, characterized by a conserved domain architecture comprising a RING finger, one or two B-box domains, a coiled-coil region, and a C-terminal PRYSPRY (B30.2) domain. TRIM21 is a RING-type E3 ubiquitin ligase, involved in the ubiquitination pathway that governs protein degradation, signaling, and immune regulation. The RING domain coordinates zinc ions and mediates interaction with E2 ubiquitin-conjugating enzymes, catalyzing ubiquitin transfer. The B-box2 domain, which adopts a fold similar to the RING domain and also coordinates zinc, features an exposed surface patch likely involved in protein-protein interactions, including intramolecular regulation via binding to the RING domain. The PRYSPRY domain is critical for substrate recognition and immune functions, comprising two subdomains that form binding pockets for the CH2 and CH3 domains of the IgG Fc region. Key residues such as I253 in the PRYSPRY domain are essential for high-affinity Fc binding, enabling TRIM21 to function as a cytosolic antibody receptor. This allows TRIM21 to recognize antibody-coated pathogens within the cytosol, targeting them for ubiquitination and proteasomal degradation, effectively linking adaptive humoral immunity to intracellular innate defense mechanisms. TRIM21 also regulates inflammatory signaling by ubiquitinating transcription factors such as interferon regulatory factors (IRFs). Dysregulation of TRIM21 is implicated in autoimmune diseases like systemic lupus erythematosus and Sjögren’s syndrome.

Specificity

TRIM21 Rabbit mAb detects endogenous levels of total TRIM21 protein.

Background

TRIM21, also known as tripartite motif-containing protein 21 or Ro52, is a member of the TRIM (tripartite motif) family of proteins, characterized by a conserved domain architecture comprising a RING finger, one or two B-box domains, a coiled-coil region, and a C-terminal PRYSPRY (B30.2) domain. TRIM21 is a RING-type E3 ubiquitin ligase, involved in the ubiquitination pathway that governs protein degradation, signaling, and immune regulation. The RING domain coordinates zinc ions and mediates interaction with E2 ubiquitin-conjugating enzymes, catalyzing ubiquitin transfer. The B-box2 domain, which adopts a fold similar to the RING domain and also coordinates zinc, features an exposed surface patch likely involved in protein-protein interactions, including intramolecular regulation via binding to the RING domain. The PRYSPRY domain is critical for substrate recognition and immune functions, comprising two subdomains that form binding pockets for the CH2 and CH3 domains of the IgG Fc region. Key residues such as I253 in the PRYSPRY domain are essential for high-affinity Fc binding, enabling TRIM21 to function as a cytosolic antibody receptor. This allows TRIM21 to recognize antibody-coated pathogens within the cytosol, targeting them for ubiquitination and proteasomal degradation, effectively linking adaptive humoral immunity to intracellular innate defense mechanisms. TRIM21 also regulates inflammatory signaling by ubiquitinating transcription factors such as interferon regulatory factors (IRFs). Dysregulation of TRIM21 is implicated in autoimmune diseases like systemic lupus erythematosus and Sjögren’s syndrome.

Usage Information

Application

WB, IP, IHC

Dilution

WB	IP	IHC
1:1000	1:50	1:100 - 1:400

Reactivity

Human

Source

Rabbit

MW

50 kDa

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

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/17400754/
https://pubmed.ncbi.nlm.nih.gov/28753623/

TRIM21 Rabbit mAb

Biological Description

Usage Information

References

Application Data