Recombinant Human E3 ubiquitin-protein ligase TRIM32 (TRIM32)

Code CSB-YP614389HU
MSDS
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Source Yeast
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Code CSB-EP614389HU
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Source E.coli
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Code CSB-EP614389HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP614389HU
MSDS
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Source Baculovirus
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Code CSB-MP614389HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
72 kda Tat interacting Protein; 72 kDa Tat-interacting protein; BBS11 ; E3 ubiquitin-protein ligase TRIM32; HT2A; LGMD2H ; Limb girdle muscular dystrophy 2H (autosomal recessive); Limb girdle muscular dystrophy 2H; Muscular dystrophy Hutterite type; TAT interactive protein 72KD; TATIP ; TRI32_HUMAN; Trim32; Tripartite Motif Containing Protein 32; Tripartite motif-containing protein 32; Zinc finger protein HT2A
Species
Homo sapiens (Human)
Expression Region
2-653
Target Protein Sequence
AAAAASHLN LDALREVLEC PICMESFTEE QLRPKLLHCG HTICRQCLEK LLASSINGVR CPFCSKITRI TSLTQLTDNL TVLKIIDTAG LSEAVGLLMC RSCGRRLPRQ FCRSCGLVLC EPCREADHQP PGHCTLPVKE AAEERRRDFG EKLTRLRELM GELQRRKAAL EGVSKDLQAR YKAVLQEYGH EERRVQDELA RSRKFFTGSL AEVEKSNSQV VEEQSYLLNI AEVQAVSRCD YFLAKIKQAD VALLEETADE EEPELTASLP RELTLQDVEL LKVGHVGPLQ IGQAVKKPRT VNVEDSWAME ATASAASTSV TFREMDMSPE EVVASPRASP AKQRGPEAAS NIQQCLFLKK MGAKGSTPGM FNLPVSLYVT SQGEVLVADR GNYRIQVFTR KGFLKEIRRS PSGIDSFVLS FLGADLPNLT PLSVAMNCQG LIGVTDSYDN SLKVYTLDGH CVACHRSQLS KPWGITALPS GQFVVTDVEG GKLWCFTVDR GSGVVKYSCL CSAVRPKFVT CDAEGTVYFT QGLGLNLENR QNEHHLEGGF SIGSVGPDGQ LGRQISHFFS ENEDFRCIAG MCVDARGDLI VADSSRKEIL HFPKGGGYSV LIREGLTCPV GIALTPKGQL LVLDCWDHCI KIYSYHLRRY STP
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Has an E3 ubiquitin ligase activity. 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.; (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.
Gene References into Functions
  1. TRIM32 as a crucial positive regulator of Herpes Simplex Virus type 1 (HSV-1) induced IFN-beta production in corneal epithelial cells, and it played a predominant role in clearing HSV-1 from the cornea. PMID: 28954259
  2. HSP70-TRIM32 complex is biochemically distinct from the previously characterized 14-3-3-TRIM32 phospho-complex. PMID: 28052117
  3. Data suggest that, in cardiomyocytes, TRIM32 attenuates activation of SRF signaling and hypertrophy due to dysbindin; TRIM24 promotes these effects. TRIM32 promotes dysbindin degradation; TRIM24 protects dysbindin from degradation. (TRIM = tripartite motif-containing protein; SRF = serum response factor) PMID: 28465353
  4. Duchenne muscular dystrophy muscles showed a selective up-regulation of the ubiquitin ligase tripartite motif-containing protein 32 (TRIM32). The induction of TRIM32 was due to a transcriptional effect and it correlated with disease severity. PMID: 27295345
  5. we provide a detailed characterization of the TRIM ligases TRIM25 and TRIM32 and show how their oligomeric state is linked to catalytic activity PMID: 27154206
  6. that TRIM32 plays a protective role in aortic banding-induced pathological cardiac remodelling by blocking Akt-dependent signalling PMID: 26884348
  7. these findings suggest that TRIM32 might play important roles in the hepatocarcinogenesis. PMID: 27573002
  8. results show a novel molecular cascade involving miR-155 and TRIM32 leading to HIV-1 Tat-induced attenuated proliferation of neural precursor cells; study also uncovered an unidentified role for miR-155 in modulating human neural stem cell proliferation, helping in better understanding of neural precursor cells and diseased brain PMID: 26586575
  9. Results suggest that Salmonella effector SseK3 binding to host tripartite motif-containing 32 protein (TRIM32) in the inhibition of nuclear factor kappa B (NF-kappaB) activation: [SseK3] PMID: 26394407
  10. TRIM32 represents a model of intrinsic immunity, in which a host protein directly senses and counters viral infection in a species specific fashion by directly limiting viral replication PMID: 26057645
  11. Data indicate that variants in tripartite motif-containing 32 protein (TRIM32) in two patients presenting nonspecific limb-girdle muscular dystrophy type 2H (LGMD2H) were identified by using high-throughput variants screening techniques. PMID: 25351777
  12. TRIM32, an E3 ubiquitin ligase, promotes HIV reactivation from latency by directly modifying IkappaBalpha PMID: 25873391
  13. Identification of TRIM32 as a novel p53 target and as a novel negative regulator for p53. PMID: 25146927
  14. Trim32 is a positive regulator of ACD that acts against MYCN and should be considered as a tumor-suppressor candidate PMID: 25100564
  15. Deletions near the 3' terminus of ASTN2, a subset of these deletions also includes TRIM32, are significantly enriched in neurodevelopmental disorder subjects. PMID: 24381304
  16. BBS11 promotes accumulation of NPHP7, changing the properties of NPHP7. TRIM32 Modulates the Transcriptional Activities of Glis2 PMID: 24500717
  17. a novel connection between ubiquitylation and phosphorylation pathways, which could modulate a variety of cell events by stimulating the formation of the 14-3-3-TRIM32 signaling complex. PMID: 23444366
  18. TRIM32 assembles polyubiquitin chains as a Ubc5-linked thioester intermediate. PMID: 23408431
  19. TRIM32 protein modulates type I interferon induction and cellular antiviral response by targeting MITA/STING protein for K63-linked ubiquitination PMID: 22745133
  20. These findings suggest that TRIM32 functions as one of the coactivators for RARalpha-mediated transcription in acute promyelogenous leukemia cells. PMID: 22182411
  21. promotes neural differentiation through retinoic acid receptor-mediated transcription PMID: 21984809
  22. Malin is related to TRIM32 at both the phylogenetic and functional level. PMID: 21798009
  23. TRIM32 sensitizes TNFalpha-induced apoptosis by antagonizing XIAP PMID: 21628460
  24. It is likely that C-terminal mutations in TRIM32 affect the ability of muscle proteins to be degraded by the ubiquitin-proteasome pathway.[review] PMID: 21496629
  25. As CCL20 is activated by Th17 cytokines, the upregulation of CCL20 production by Trim32 provides a positive feedback loop of CCL20 and Th17 activation in the self-perpetuating cycle of psoriasis PMID: 20054338
  26. limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene PMID: 11822024
  27. TRIM32 mutation found in the sarcotubular myopathy patients is identical to the causative mutation for LGMD2H (D487N) PMID: 15786463
  28. Mutation analysis of TRIM32 shows it is a Bardet-Biedl syndrome gene. PMID: 16606853
  29. by controlling Piasy stability, Trim32 regulates UVB-induced keratinocyte apoptosis through induction of NFkappaB PMID: 16816390
  30. The mutations here reported may cause muscular dystrophy by affecting the interaction properties of TRIM32. PMID: 17994549
  31. Together with two recently reported mutations, this novel mutation confirms that integrity of the C-terminal domain of TRIM32 is necessary for muscle maintenance. PMID: 19303295
  32. TRIM32 is a widely expressed ubiquitin ligase and binds and ubiquitinates dysbindin. PMID: 19349376
  33. Intragenic deletion of TRIM32 in compound heterozygotes with sarcotubular myopathy/LGMD2H PMID: 19492423
  34. The interplay between Trim32 and Pias3 is positively regulated by nitric oxide. PMID: 17987106

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Involvement in disease
Limb-girdle muscular dystrophy 2H (LGMD2H); Bardet-Biedl syndrome 11 (BBS11)
Subcellular Location
Cytoplasm.
Protein Families
TRIM/RBCC family
Tissue Specificity
Spleen, thymus, prostate, testis, ovary, intestine, colon and skeletal muscle.
Database Links

HGNC: 16380

OMIM: 254110

KEGG: hsa:22954

STRING: 9606.ENSP00000363095

UniGene: Hs.591910

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