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AB269065

Recombinant Human TRIM32 protein (Tagged)

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Recombinant Human TRIM32 protein (Tagged) is a Human Full Length protein, in the 2 to 653 aa range, expressed in Baculovirus infected Sf9 cells, with >75%, suitable for SDS-PAGE.

View Alternative Names

HT2A, TRIM32, 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

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SDS-PAGE - Recombinant Human TRIM32 protein (Tagged) (AB269065)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human TRIM32 protein (Tagged) (AB269065)

SDS-PAGE analysis of ab269065.

Key facts

Purity

>75% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

GST tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q13049

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.79% Tris HCl, 0.31% Glutathione, 0.29% Sodium chloride, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"AAAAASHLNLDALREVLECPICMESFTEEQLRPKLLHCGHTICRQCLEKLLASSINGVRCPFCSKITRITSLTQLTDNLTVLKIIDTAGLSEAVGLLMCRSCGRRLPRQFCRSCGLVLCEPCREADHQPPGHCTLPVKEAAEERRRDFGEKLTRLRELMGELQRRKAALEGVSKDLQARYKAVLQEYGHEERRVQDELARSRKFFTGSLAEVEKSNSQVVEEQSYLLNIAEVQAVSRCDYFLAKIKQADVALLEETADEEEPELTASLPRELTLQDVELLKVGHVGPLQIGQAVKKPRTVNVEDSWAMEATASAASTSVTFREMDMSPEEVVASPRASPAKQRGPEAASNIQQCLFLKKMGAKGSTPGMFNLPVSLYVTSQGEVLVADRGNYRIQVFTRKGFLKEIRRSPSGIDSFVLSFLGADLPNLTPLSVAMNCQGLIGVTDSYDNSLKVYTLDGHCVACHRSQLSKPWGITALPSGQFVVTDVEGGKLWCFTVDRGSGVVKYSCLCSAVRPKFVTCDAEGTVYFTQGLGLNLENRQNEHHLEGGFSIGSVGPDGQLGRQISHFFSENEDFRCIAGMCVDARGDLIVADSSRKEILHFPKGGGYSVLIREGLTCPVGIALTPKGQLLVLDCWDHCIKIYSYHLRRYSTP","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":653,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"Baculovirus infected Sf9 cells","accessionNumber":"Q13049","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

TRIM32 also known as Tripartite Motif Containing 32 is a protein that functions as an E3 ubiquitin ligase. It plays a role in attaching ubiquitin molecules to proteins tagging them for degradation by the proteasome. TRIM32 consists of a RING domain a B-box and a coiled-coil region which are characteristic of the TRIM family. The molecular mass of TRIM32 is approximately 71 kDa. It is expressed in various tissues with notable expression in skeletal muscle and the heart implying an important role in muscle physiology.
Biological function summary

TRIM32 participates in regulating muscle cell differentiation and proliferation. It interacts with several proteins including dysbindin and myospryn suggesting its involvement in a multi-protein complex. TRIM32 has a regulatory role in muscle maintenance where it influences the stability and function of muscle proteins. Moreover it is also involved in neurogenesis affecting neuronal differentiation and survival emphasizing its role beyond muscle tissues.

Pathways

TRIM32 plays a significant role in the PI3K/Akt signaling pathway and the TGF-beta signaling pathway. In the PI3K/Akt pathway TRIM32 modulates cell growth and survival interacting with proteins such as Akt and mTOR. In the context of TGF-beta signaling TRIM32 can influence cellular processes like proliferation and differentiation possibly by interacting with SMAD proteins. These interactions indicate its importance in cellular growth and differentiation pathways.

TRIM32 is linked with limb-girdle muscular dystrophy type 2H and certain forms of sarcopenia. Mutations in TRIM32 cause dysfunction in muscle protein turnover leading to muscle deterioration and weakness. In limb-girdle muscular dystrophy TRIM32 mutations disrupt its interaction with dysbindin impairing muscle structure. Furthermore TRIM32 might be involved in neurodegenerative diseases with connections to proteins like alpha-synuclein hinting at a potential role in Parkinson's disease.
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Specifications

Form

Liquid

Additional notes

Affinity purified.

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General info

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 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 (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). Under metabolic stress and phosphorylation by CHK2, mediates 'Lys-63'-linked ubiquitination of ATG7 at 'Lys-45' to initiate autophagy (PubMed : 37943659).. (Microbial infection) May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo (PubMed : 7778269). Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo (PubMed : 7778269).

Sequence similarities

Belongs to the TRIM/RBCC family.

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.

Subcellular localisation

Mitochondrion

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Product protocols

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Target data

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 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 (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). Under metabolic stress and phosphorylation by CHK2, mediates 'Lys-63'-linked ubiquitination of ATG7 at 'Lys-45' to initiate autophagy (PubMed : 37943659).. (Microbial infection) May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo (PubMed : 7778269). Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo (PubMed : 7778269).
See full target information TRIM32
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