Human TRIM32 protein (Recombinant) (N-His-SUMO & C-Strep) (STJP010926)

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STJP010926
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Host: E. coli
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description : Recombinant-Human TRIM32-N-His-SUMO & C-Strep protein was developed from e. coli and has a target region of N-His-SUMO & C-Strep. For use in research applications.
Formulation: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Storage Instruction: Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt.
Gene Symbol: TRIM32
Gene ID: 22954
Uniprot ID: TRI32_HUMAN
Immunogen Region: Ser7-Arg101
Immunogen: Homo sapiens (Human)
Post Translational Modifications Ubiquitinated. Phosphorylation at Ser-55 by CHEK2 under oxidative stress, activates the E3 ligase activity and promotes ATG7 ubiquitination leading to positive regulation of the autophagosme assembly.
Function E3 ubiquitin ligase that plays a role in various biological processes including neural stem cell differentiation, innate immunity, inflammatory resonse and autophagy. 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. Regulates bacterial clearance and promotes autophagy in Mycobacterium tuberculosis-infected macrophages. Negatively regulates TLR3/4-mediated innate immune and inflammatory response by triggering the autophagic degradation of TICAM1 in an E3 activity-independent manner. 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. Ubiquitinates XIAP and targets it for proteasomal degradation. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May ubiquitinate BBS2. Ubiquitinates PIAS4/PIASY and promotes its degradation in keratinocytes treated with UVB and TNF-alpha. 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. Positively regulates dendritic branching by promoting ubiquitination and subsequent degradation of the epigenetic factor CDYL. Under metabolic stress and phosphorylation by CHK2, mediates 'Lys-63'-linked ubiquitination of ATG7 at 'Lys-45' to initiate autophagy. (Microbial infection) May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo.
Protein Name E3 Ubiquitin-Protein Ligase Trim32
72 Kda Tat-Interacting Protein
Ring-Type E3 Ubiquitin Transferase Trim32
Tripartite Motif-Containing Protein 32
Zinc Finger Protein Ht2a
Database Links Reactome: R-HSA-3134975
Reactome: R-HSA-983168
Cellular Localisation Cytoplasm
Mitochondrion
Endoplasmic Reticulum
Localized In Cytoplasmic Bodies
Often Located Around The Nucleus
Alternative Protein Names E3 Ubiquitin-Protein Ligase Trim32 protein
72 Kda Tat-Interacting Protein protein
Ring-Type E3 Ubiquitin Transferase Trim32 protein
Tripartite Motif-Containing Protein 32 protein
Zinc Finger Protein Ht2a protein
TRIM32 protein
HT2A protein

Information sourced from Uniprot.org