Recombinant Mouse E3 ubiquitin-protein ligase TRIM32 (Trim32)

Code CSB-YP807028MO
MSDS
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Source Yeast
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Code CSB-EP807028MO
MSDS
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Source E.coli
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Code CSB-EP807028MO-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-BP807028MO
MSDS
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Source Baculovirus
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Code CSB-MP807028MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
Trim32; E3 ubiquitin-protein ligase TRIM32; EC 2.3.2.27; RING-type E3 ubiquitin transferase TRIM32; Tripartite motif-containing protein 32
Species
Mus musculus (Mouse)
Expression Region
1-655
Target Protein Sequence
MAAAAAASHL NLDALREVLE CPICMESFTE EQLRPKLLHC GHTICRQCLE KLLASSINGV RCPFCSKITR ITSLTQLTDN LTVLKIIDTA GLSEAVGLLM CRGCGRRLPR QFCRSCGVVL CEPCREADHQ PPGHCTLPVK EAAEERRRDF GEKLTRLREL TGELQRRKAA LEGVSRDLQA RYKAVLQEYG HEERRIQEEL ARSRKFFTGS LAEVEKSNSQ VVEEQSYLLN IAEVQAVSRC DYFLAKIKQA DVALLEETAD EEEPELTASL PRELTLQDVE LLKVGHVGPL QIGQAVKKPR TVNMEDSWAG EEGAASSASA SVTFREMDMS PEEVAPSPRA SPAKQRSSEA ASGIQQCLFL KKMGAKGSTP GMFNLPVSLY VTSQSEVLVA DRGNYRIQVF NRKGFLKEIR RSPSGIDSFV LSFLGADLPN LTPLSVAMNC HGLIGVTDSY DNSLKVYTMD GHCVACHRSQ LSKPWGITAL PSGQFVVTDV EGGKLWCFTV DRGAGVVKYS CLCSAVRPKF VTCDAEGTVY FTQGLGLNVE NRQNEHHLEG GFSIGSVGPD GQLGRQISHF FSENEDFRCI AGMCVDARGD LIVADSSRKE ILHFPKGGGY SVLIREGLTC PVGIALTPKG QLLVLDCWDH CVKIYSYHLR RYSTP
Protein Length
full length 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.

Customer Reviews and Q&A

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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-alphaAlso 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.
Gene References into Functions
  1. suppression of Trim32 promotes the recovery of neurological function after traumatic brain injury. PMID: 28933219
  2. the presented data link the Parkinson's disease-associated gene alpha-synuclein to the neuronal cell fate determinant TRIM32. PMID: 27339877
  3. TRIM32 is a novel essential positive factor modulating axonal regeneration and the recovery of motor function following SCI, possibly through suppressing proliferation of glial cells. PMID: 28514764
  4. 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
  5. TRIM32 protein expression is defective in atopic dermatitis lesional skin. PMID: 27720760
  6. that TRIM32 plays a protective role in aortic banding-induced pathological cardiac remodelling by blocking Akt-dependent signalling PMID: 26884348
  7. In summary, the data presented here reveal that TRIM32 directly regulates at least two of the four Yamanaka Factors (cMyc and Oct4), to modulate cell fate transitions. PMID: 26307407
  8. 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
  9. NDRG2 accumulated in skeletal muscle and myoblasts in the absence of TRIM32. NDRG2 overexpression in myoblasts led to reduced cell proliferation and delayed cell cycle withdrawal during differentiation. PMID: 25701873
  10. TRIM32 overexpression promotes cell oncogenic transformation and tumorigenesis in mice in a largely p53-dependent manner. PMID: 25146927
  11. Data show that RNA helicase DDX6 colocalizes with ubiquitin-protein ligase TRIM32 in neural stem cells and neurons and that it increases the activity of microRNA Let-7a. PMID: 25722370
  12. TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress. PMID: 24839933
  13. The results highlight the function of the cell fate-determinant TRIM32 for a balanced activity of the adult neurogenesis process. PMID: 24357807
  14. Trim32 reduces PI3K-Akt-FoxO signaling in normal and atrophying muscle by promoting plakoglobin-PI3K dissociation. PMID: 24567360
  15. TRIM32 physically interacts with TAp73 and promotes its ubiquitination and degradation while TAp73 regulates TRIM32 gene expression. PMID: 23828567
  16. 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
  17. During fasting, desmin phosphorylation increases and enhances Trim32-mediated degradation of the desmin cytoskeleton, which appears to facilitate the breakdown of Z-bands and thin filaments. PMID: 22908310
  18. Loss of TRIM32 function induces a LGMD2H-like phenotype and strongly affects muscle regeneration in vivo. PMID: 22299041
  19. Study provides evidence that the neuronal fate determinant TRIM32 binds to the protein kinase C zeta. Through this interaction, TRIM32 is retained in the cytoplasm. PMID: 21732497
  20. one potential mechanism of LGMD2H might be destabilization of mutated TRIM32 protein leading to a null phenotype. PMID: 21775502
  21. by controlling Piasy stability, Trim32 regulates UVB-induced keratinocyte apoptosis through induction of NFkappaB PMID: 16816390
  22. TRIM32 is a novel oncogene that promotes tumor growth, metastasis, and resistance to anticancer drugs via degradation of Abl-interactor 2 PMID: 18632609
  23. Muscular dystrophy due to TRIM32 mutations involves both neurogenic and myogenic characteristics. PMID: 19155210
  24. TRIM32 overexpression induces neuronal differentiation while inhibition of TRIM32 causes both daughter cells to retain progenitor cell fate; also it binds Argonaute-1 and thereby increases the activity of specific microRNAs. PMID: 19269368

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Subcellular Location
Cytoplasm.
Protein Families
TRIM/RBCC family
Tissue Specificity
Ubiquitous. High expression in brain.
Database Links
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7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
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