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TRIM32 Antibody (N-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q13049 |
|---|---|
| Clone Names | 100408318 |
| Gene ID | 22954 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase TRIM32, 632-, 72 kDa Tat-interacting protein, Tripartite motif-containing protein 32, Zinc finger protein HT2A, TRIM32, HT2A |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP13287a was selected from the N-term region of TRIM32. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | TRIM32 |
|---|---|
| Synonyms | HT2A |
| Function | E3 ubiquitin ligase that plays a role in various biological processes including neural stem cell differentiation, innate immunity, inflammatory resonse and autophagy (PubMed:19349376, PubMed:31123703). Plays a role in virus-triggered induction of IFN-beta and TNF-alpha by mediating the ubiquitination of STING1. Mechanistically, targets STING1 for 'Lys-63'-linked ubiquitination which promotes the interaction of STING1 with TBK1 (PubMed:22745133). Regulates bacterial clearance and promotes autophagy in Mycobacterium tuberculosis-infected macrophages (PubMed:37543647). Negatively regulates TLR3/4-mediated innate immune and inflammatory response by triggering the autophagic degradation of TICAM1 in an E3 activity-independent manner (PubMed:28898289). Plays an essential role in oxidative stress induced cell death by inducing loss of transmembrane potential and enhancing mitochondrial reactive oxygen species (ROS) production during oxidative stress conditions (PubMed:32918979). Ubiquitinates XIAP and targets it for proteasomal degradation (PubMed:21628460). Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation (PubMed:19349376). May ubiquitinate BBS2 (PubMed:22500027). Ubiquitinates PIAS4/PIASY and promotes its degradation in keratinocytes treated with UVB and TNF-alpha (By similarity). Also acts as a regulator of autophagy by mediating formation of unanchored 'Lys-63'-linked polyubiquitin chains that activate ULK1: interaction with AMBRA1 is required for ULK1 activation (PubMed:31123703). Positively regulates dendritic branching by promoting ubiquitination and subsequent degradation of the epigenetic factor CDYL (PubMed:34888944). |
| Cellular Location | Cytoplasm. Mitochondrion. Endoplasmic reticulum. Note=Localized in cytoplasmic bodies, often located around the nucleus |
| Tissue Location | Spleen, thymus, prostate, testis, ovary, intestine, colon and skeletal muscle. |
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Provided below are standard protocols that you may find useful for product applications.
Background
The protein encoded by this gene is a member of thetripartite motif (TRIM) family. The TRIM motif includes threezinc-binding domains, a RING, a B-box type 1 and a B-box type 2,and a coiled-coil region. The protein localizes to cytoplasmicbodies. The protein has also been localized to the nucleus, whereit interacts with the activation domain of the HIV-1 Tat protein.The Tat protein activates transcription of HIV-1 genes. [providedby RefSeq].
References
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Liu, Y., et al. J. Invest. Dermatol. 130(5):1384-1390(2010)Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)Markson, G., et al. Genome Res. 19(10):1905-1911(2009)van Wijk, S.J., et al. Mol. Syst. Biol. 5, 295 (2009) :
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