Mouse Polyclonal TRIM13 antibody. N-terminal. Suitable for WB and reacts with Recombinant fragment - Human, Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human E3 ubiquitin-protein ligase TRIM13 aa 1-100.
IgG
Mouse
Constituents: 50% Glycerol (glycerin, glycerine)
Liquid
Polyclonal
WB | |
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Human | Tested |
Mouse | Predicted |
Rat | Predicted |
Cow | Predicted |
Recombinant fragment - Human | Tested |
Species | Dilution info | Notes |
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Species Recombinant fragment - Human | Dilution info 1/500 - 1/1000 | Notes - |
Species Human | Dilution info 1/500 - 1/1000 | Notes - |
Species | Dilution info | Notes |
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Species Mouse, Rat, Cow | Dilution info - | Notes - |
Select an associated product type
Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor (PubMed:22178386). Also plays a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation (PubMed:28087809). Participates as well in T-cell receptor-mediated NF-kappa-B activation (PubMed:25088585). In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B (PubMed:25152375).
LEU5, RFP2, RNF77, TRIM13, LEU5, RFP2, RNF77, E3 ubiquitin-protein ligase TRIM13, B-cell chronic lymphocytic leukemia tumor suppressor Leu5, Leukemia-associated protein 5, Putative tumor suppressor RFP2, RING finger protein 77, RING-type E3 ubiquitin transferase TRIM13, Ret finger protein 2, Tripartite motif-containing protein 13
Mouse Polyclonal TRIM13 antibody. N-terminal. Suitable for WB and reacts with Recombinant fragment - Human, Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human E3 ubiquitin-protein ligase TRIM13 aa 1-100.
IgG
Mouse
Constituents: 50% Glycerol (glycerin, glycerine)
Liquid
Polyclonal
Whole antiserum
Blue Ice
1-2 weeks
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
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This supplementary information is collated from multiple sources and compiled automatically.
TRIM13 also known as RFP2 is a protein encoded by the TRIM13 gene with an approximate mass of 42 kDa. Mechanically TRIM13 functions as an E3 ubiquitin ligase mediating ubiquitination and proteasomal degradation. It belongs to the tripartite motif family characterized by a RING zinc finger one or more B-box domains and a coiled-coil region. The protein is expressed in various tissues including the heart liver and pancreas suggesting a wide range of functional roles.
This protein is important for maintaining cellular homeostasis by regulating protein turnover and quality control. TRIM13 is involved in the endoplasmic reticulum-associated degradation (ERAD) pathway where it facilitates the removal of misfolded proteins. Additionally it interacts with other molecules to form complexes that modulate autophagy a process vital for cellular cleaning and response to stress.
Ubiquitination processes and quality control systems incorporate TRIM13 into the intricacies of the ERAD and autophagy pathways. It coordinates with proteins like p62 and Beclin1 which are important for autophagy regulation. In the ERAD pathway TRIM13 functions alongside components such as Derlin-1 helping to identify and direct aberrant proteins toward degradation. These interactions balance protein synthesis and degradation essential for cellular stress responses and survival.
TRIM13's roles tie to neurodegenerative diseases and cancer. Mutations or dysregulation of TRIM13 lead to an accumulation of misfolded proteins contributing to the progression of amyotrophic lateral sclerosis (ALS). In cancer altered TRIM13 expression can disrupt normal degradation processes affecting tumor growth and metastasis. TRIM13 interacts with CHOP a protein involved in pro-apoptotic signaling which links it to cellular stress responses that are pivotal in disease states.
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All lanes: Western blot - Anti-TRIM13 antibody - N-terminal (ab194477) at 1/500 dilution
All lanes: HeLa cell lysate at 50 µg
Developed using the ECL technique.
Predicted band size: 47 kDa
Predicted MWt of immunogen: 37.11 KDa.
All lanes: Western blot - Anti-TRIM13 antibody - N-terminal (ab194477) at 1/1000 dilution
All lanes: recombinant immunogen at 0.2 µg
Developed using the ECL technique.
Predicted band size: 47 kDa
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