TRIM21 Antibody (YA658)
(Synonyms: SSA; RO52; SSA1; RNF81; Ro/SSA)Based on 1 Customer Validation
TRIM21 Antibody (YA658) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to TRIM21.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB
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Reactivity :
Human
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Formulation:
Supplied in 1*PBS (pH 7.3), 50% glycerol and 0.5% BSA. Preservative: 0.02% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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|---|---|
| Dilution Ratio | 1:500-1:1000 |
Product Details
TRIM21 Antibody (YA658) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to TRIM21.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 50 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 54 kDa
Synthetic peptide corresponding to Human TRIM21.The exact sequence is proprietary to MCE.
Endogenous
affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in 1*PBS (pH 7.3), 50% glycerol and 0.5% BSA. Preservative: 0.02% sodium azide.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Verification Images
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Western blot analysis of extracts from HEK293T (lane2(20μg), MOLT-4 (lane3(20μg), HeLa (lane4(20μg) and A549 (lane5(20μg) using TRIM21 Antibody (HY-P80921). Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80993, 1/10,000) was used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse IgG-HRP Secondary Antibody (HY-P8004 ,1/10,000) was used for 1 hour at room temperature.
Background
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Function
Tripartite motif-containing 21 (TRIM21) is a cytosolic E3 ubiquitin ligase that functions in intracellular immunity and protein homeostasis[1][2]. Mechanistically, TRIM21 mediates K48- and K11-linked ubiquitination of target proteins, including viral antigens and transcription factors, modulating their stability, signaling, and degradation[3][4][5]. TRIM21 regulates protein translation by interacting with PKR and promoting K6-linked ubiquitination of PP1α, thereby controlling eIF2α dephosphorylation and protein synthesis under stress conditions[6]. In cancer models, TRIM21 suppresses tumorigenesis by promoting cuproptosis in esophageal squamous cell carcinoma through ID1 ubiquitination and inhibits ovarian cancer cell proliferation and migration via cell cycle regulation[3][7]. TRIM21 also contributes to hepatocarcinogenesis by negatively regulating the p62-Keap1-Nrf2 antioxidant pathway, enhancing oxidative stress and tumor progression[8]. Compared with related TRIM isoforms, TRIM21 specifically targets interferon regulatory factors, such as IRF3 and IRF5, with differential isoform-specific degradation, thereby modulating innate immunity and autoimmune responses[9][10]. Experimental applications exploit TRIM21’s antibody-binding Fc domain to degrade specific intracellular proteins, enabling precise protein depletion in cell and zebrafish models[1][11]. Small molecules or inhibitors targeting upstream regulators, like Sorafenib, can enhance TRIM21-mediated ubiquitination, highlighting its potential in therapeutic intervention and functional studies[3][5]. Collectively, TRIM21 integrates immune defense, protein quality control, and disease modulation, making it a versatile tool for mechanistic and translational research.
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Subcellular Localization
Cytoplasm; Cytoplasmic vesicle, autophagosome; Nucleus; Cytoplasm, P-body; Cytoplasm, Stress granule
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Expression
Tissue_specificity:Isoform 1 and isoform 2 are expressed in human heart and fetal lung
Induction:Up-regulated by isoform 2 of XBP1. Up-regulated by IFNG/interferon-gamma, with a peak after 2-4 hours of treatment in monocytes/macrophages -
Isoforms & Post-Translational Modification
P19474 has 2 isomers: P19474-1: 54170 Da (predicted); P19474-2: 45057 Da (predicted).
Autoubiquitinated; does not lead to its proteasomal degradation. Deubiquitinated by USP4; leading to its stabilization -
Subunit
Homotrimer (PubMed:17156811, PubMed:26347139). Interacts (via C-terminus) with IRF8 (via C-terminus) (By similarity). Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Interacts with CALR, CUL1, FBXW11, HSPA5, IKBKB, IRF3, SKP1 and VCP. Interacts with SKP2; the interaction with SKP2 does not depend on an intact F-box domain. Interacts (via N-terminus and C-terminus) with DCP2 (via N-terminus and C-terminus). Interacts with ULK1, BECN1 and with ATG8 family members, including GABARAP, GABARAPL1, GABARAPL2 and MAP1LC3C/LC3C. Interacts with TRIM21 and SQSTM1/sequestosome 1. Interacts with IRF3 (By similarity) (PubMed:12699405, PubMed:16880511, PubMed:17156811, PubMed:18022694, PubMed:18361920, PubMed:18641315, PubMed:19675099, PubMed:26347139, PubMed:8666824). Interacts (via the SPRY domain) with NMI (via coiled-coil domain); the interaction promotes 'Lys-63'-linked ubiquitination of NMI (PubMed:26342464). Interacts with IFI35 and NMI; the interaction facilitates NMI-IFI35 complex formation (PubMed:26342464)
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SwissProt ID
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Synonyms
SSA; RO52; SSA1; RNF81; Ro/SSA
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Research Field
Epigenetics and Nuclear Signaling
Documentation
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Data Sheet (263 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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User Guide for Antibodies (1077 KB)
[1]. Foss S, et al. TRIM21-From Intracellular Immunity to Therapy. Front Immunol. 2019 Aug 28;10:2049. [Content Brief]
[2]. Jones EL, et al. TRIM21/Ro52 - Roles in Innate Immunity and Autoimmune Disease. Front Immunol. 2021 Sep 6;12:738473. [Content Brief]
[3]. Li L, et al. TRIM21-Mediated K11-Linked Ubiquitination of ID1 Suppresses Tumorigenesis and Promotes Cuproptosis in Esophageal Squamous Cell Carcinoma. Adv Sci (Weinh). 2025 Sep;12(35):e02501. [Content Brief]
[4]. Wu S, et al. Ubiquitin-dependent proteasomal degradation of small hepatitis B virus surface antigen mediated by TRIM21 and antagonized by OTUD4. J Virol. 2025 May 20;99(5):e0230924. [Content Brief]
[5]. Li Y, et al. CNOT7 facilitates radiation resistance in colorectal cancer through TRIM21/XRCC6-mediated non-homologous end joining repair. Cell Death Dis. 2025 Nov 17;16(1):833. [Content Brief]
[6]. Hermans A, et al. A 3D-Printed and Freely Available Device to Measure the Zebrafish Optokinetic Response Before and After Injury. Zebrafish. 2024 Apr;21(2):144-148. [Content Brief]
[7]. Sun J, et al. TRIM21 deficiency promotes cell proliferation and tumorigenesis via regulating p21 expression in ovarian cancer. Bioengineered. 2022 Mar;13(3):6024-6035. [Content Brief]
[8]. Wang F, et al. The Ubiquitin E3 Ligase TRIM21 Promotes Hepatocarcinogenesis by Suppressing the p62-Keap1-Nrf2 Antioxidant Pathway. Cell Mol Gastroenterol Hepatol. 2021;11(5):1369-1385. [Content Brief]
[9]. Stacey KB, et al. Tyrosine phosphorylation of the E3 ubiquitin ligase TRIM21 positively regulates interaction with IRF3 and hence TRIM21 activity. PLoS One. 2012;7(3):e34041. [Content Brief]
[10]. Lazzari E, et al. TRIpartite motif 21 (TRIM21) differentially regulates the stability of interferon regulatory factor 5 (IRF5) isoforms. PLoS One. 2014 Aug 1;9(8):e103609. [Content Brief]
[11]. Chin W J. Functional and mechanistic studies on engineered antibodies that engage TRIM21[J]. 2020.