Rabbit anti-Human, Mouse TRIM13 Polyclonal Antibody | anti-TRIM13 antibody

TRIM13 Antibody

Cat. Num. AAA9629778

• Gene Names: TRIM13; CAR; LEU5; RFP2; DLEU5; RNF77
• Reactivity: Human, Mouse
• Applications: ELISA
• Purity: The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin (Thermo Fisher Scientific).
• Synonyms: TRIM13; Polyclonal Antibody; TRIM13 Antibody; B cell chronic lymphocytic leukemia tumor suppressor Leu5; B-cell chronic lymphocytic leukemia tumor suppressor Leu5; CAR; DLEU5; E3 ubiquitin-protein ligase TRIM13; HGNC:9976; LEU5; Leukemia associated protein 5; Leukemia-associated protein 5; Putative tumor suppressor RFP2; Ret finger protein 2; RFP2; RING finger protein 77; RNF77; TRI13_HUMAN; Trim13; Tripartite motif protein 13; Tripartite motif-containing protein 13; anti-TRIM13 antibody

• Host: Rabbit
• Reactivity: Human, Mouse
• Clonality: Polyclonal
• Isotype: Rabbit IgG
• Specificity: TRIM13 Antibody detects endogenous levels of TRIM13.
• Purity/Purification: The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin (Thermo Fisher Scientific).
• Form/Format: Liquid. Rabbit IgG in phosphate buffered saline, pH7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
• Concentration: 1mg/ml (varies by lot)

• Applicable Applications for anti-TRIM13 antibody: ELISA (EIA)(peptide)
• Application Notes: ELISA(peptide): 1:20000-1:40000
• Immunogen: A synthesized peptide derived from human TRIM13.
• Conjugation: Unconjugated
• Similarity: The coiled-coil domain is required for the induction of autophagy during endoplasmic reticulum (ER) stress. The RING-type zinc finger is required for auto-polyubiquitination. The C-terminal domain transmembrane domain is indispensable for the localization to the ER. Belongs to the TRIM/RBCC family.
• Post Translational Modifications: Auto-ubiquitinated; requires the RING-type zinc finger. Auto-polyubiquitination leads to proteasomal degradation.
• Subunit Structure: Interacts (via C-terminal domain) with VCP. Interacts with AKT1; the interaction ubiquitinates AKT1 and leads to its proteasomal degradation. Interacts with MDM2; the interaction ubiquitinates AKT1 and leads to its proteasomal degradation. Interacts with p62/SQSTM1. Interacts with TRAF6. Interacts with IKBKG/NEMO.
• Function: 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. Plays also 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. Participates as well in T-cell receptor-mediated NF-kappa-B activation. In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B.
• Note: Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum.
• Preparation and Storage: Store at -20 degree C. Stable for 12 months from date of receipt.

Product Categories/Family for anti-TRIM13 antibody

Endoplasmic reticulum membrane; Single-pass membrane protein; Primary

NCBI and Uniprot Product Information

• NCBI GI #: 71153168
• NCBI GeneID: 10206
• UniProt Accession #: O60858; Q5UBW0; Q5W0U8; Q5W0U9; Q9BQ47; Q9C021; B2RB49
• Molecular Weight: 407
• NCBI Official Full Name: E3 ubiquitin-protein ligase TRIM13
• NCBI Official Synonym Full Names: tripartite motif containing 13
• NCBI Official Symbol: TRIM13
• NCBI Official Synonym Symbols: CAR; LEU5; RFP2; DLEU5; RNF77
• NCBI Protein Information: E3 ubiquitin-protein ligase TRIM13; ret finger protein 2; RING finger protein 77; CLL-associated RING finger; tripartite motif protein 13; leukemia-associated protein 5; putative tumor suppressor RFP2; tripartite motif-containing 13; tripartite motif-cont
• UniProt Protein Name: E3 ubiquitin-protein ligase TRIM13
• Protein Family: Tripartite motif containing
• UniProt Gene Name: TRIM13
• UniProt Synonym Gene Names: LEU5; RFP2; RNF77
• UniProt Entry Name: TRI13_HUMAN

NCBI Description

This gene encodes a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This gene is located on chromosome 13 within the minimal deletion region for B-cell chronic lymphocytic leukemia. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

TRIM13: E3 ubiquitin 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. Belongs to the TRIM/RBCC family. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Ligase; Membrane protein, integral; EC 6.3.2.-; Ubiquitin ligase; Ubiquitin conjugating system; Tumor suppressor

Chromosomal Location of Human Ortholog: 13q14

Cellular Component: endoplasmic reticulum membrane; cytoplasm; integral to membrane

Molecular Function: protein binding; signal transducer activity; zinc ion binding; ubiquitin-protein ligase activity; ligase activity

Biological Process: proteasomal ubiquitin-dependent protein catabolic process; negative regulation of viral transcription; ER-associated protein catabolic process; anatomical structure morphogenesis; protein autoubiquitination; positive regulation of I-kappaB kinase/NF-kappaB cascade; response to gamma radiation; innate immune response; signal transduction; positive regulation of macroautophagy; activation of NF-kappaB transcription factor