TRIM37 Antibody (YA8939)
(Synonyms: KIAA0898, MUL, POB1, TRIM37, E3 ubiquitin-protein ligase TRIM37, Mulibrey nanism protein, RING-type E3 ubiquitin transferase TRIM37, Tripartite motif-containing protein 37)TRIM37 Antibody (YA8939) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to TRIM37.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, ICC/IF, IF-Tissue, IP, ELISA
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Reactivity :
human, mouse, rat
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Formulation:
Supplied in PBS(pH7.4) containing 0.1% gelatin and < 0.1% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
IF-Tissue
IF-Tissue: Immunofluorescence-Tissue
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IP
IP: Immunoprecipitation
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ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|---|---|---|---|
| Dilution Ratio | 1:100-1000 | 1:50-500 | 1:50-500 | 1-2μg per 100-500μg Total protein | 1:30-3000 |
Product Details
TRIM37 Antibody (YA8939) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to TRIM37.
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Host Mouse
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Species Reactivityhuman, mouse, rat
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Observed Molecular WeightObserved band size: 130/85 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: 108/89/104 kDa
OMIM: 605073
A synthesized peptide derived from human TRIM37.
Endogenous
Affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS(pH7.4) containing 0.1% gelatin and < 0.1% 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 2-8°C for 1 year, do not freeze.
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Shipping
Shipping with blue ice.
Background
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Function
TRIM37 is an E3 ubiquitin-protein ligase required to prevent centriole reduplication. Probably acts by ubiquitinating positive regulators of centriole reduplication. Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes. Also acts as a positive regulator of peroxisome import by mediating monoubiquitination of PEX5 at 'Lys-472': monoubiquitination promotes PEX5 stabilitation by preventing its polyubiquitination and degradation by the proteasome. Has anti-HIV activity[1][2][3][4][5].
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Subcellular Localization
Chromosome; Cytoplasm, perinuclear region; Peroxisome membrane
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Expression
Tissue_Specificity: Ubiquitous. Highly expressed in testis, while it is weakly expressed in other tissues.
Induction: Overexpressed in a number of breast cancer cell lines. -
Isoforms & Post-Translational Modification
TRIM37 has 3 isoforms, O94972-1: amino acid length is 964, molecular weight is 107906 Da (predicted); O94972-2: amino acid length is 803, molecular weight is 89186 Da (predicted); O94972-3: amino acid length is 930, molecular weight is 103941 Da (predicted).Auto-ubiquitinated
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Subunit
Associates with the PRC2/EED-EZH2 complex
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SwissProt ID
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Synonyms
KIAA0898, MUL, POB1, TRIM37, E3 ubiquitin-protein ligase TRIM37, Mulibrey nanism protein, RING-type E3 ubiquitin transferase TRIM37, Tripartite motif-containing protein 37
Documentation
References
[1]. Kallijärvi J, et al. TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase. Exp Cell Res. 2005 Aug 1;308(1):146-55. [Content Brief]
[2]. Balestra FR, et al. Discovering regulators of centriole biogenesis through siRNA-based functional genomics in human cells. Dev Cell. 2013 Jun 24;25(6):555-71. [Content Brief]
[3]. Bhatnagar S, et al. TRIM37 is a new histone H2A ubiquitin ligase and breast cancer oncoprotein. Nature. 2014 Dec 4;516(7529):116-20. [Content Brief]
[4]. Wang W, et al. TRIM37, a novel E3 ligase for PEX5-mediated peroxisomal matrix protein import. J Cell Biol. 2017 Sep 4;216(9):2843-2858. [Content Brief]
[5]. Tabah AA, et al. Anti-HIV-1 activity of Trim 37. J Gen Virol. 2014 Apr;95(Pt 4):960-967. [Content Brief]