Recombinant Mouse Tripartite motif-containing protein 72 (Trim72), Mus musculus (Mouse), E.coli, N-terminal 10xHis-tagged and C-terminal Myc-tagged, 57.8 kDa, purity >90% as determined by SDS-PAGE.

Recombinant Mouse Tripartite motif-containing protein 72 (Trim72)

Recombinant Mouse Tripartite motif-containing protein 72 (Trim72) — Muscle-specific E3 ubiquitin-protein ligase that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Purity >90%.

SKU: BCRECP-004622 Category:
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Product Specifications

Product SkuBCRECP-004622
Product DescriptionRecombinant Mouse Tripartite motif-containing protein 72 (Trim72) Protein is expressed from nan with N-terminal 10xHis-tagged and C-terminal Myc-tagged. It contains 1-477aa. [Accession | Q1XH17].
Uniprot No.Q1XH17
Gene NamesTrim72
PurityGreater than 90% as determined by SDS-PAGE.
Expression SystemE.coli
Expression Region1-477aa
SpeciesMus musculus (Mouse)
Tag InfoN-terminal 10xHis-tagged and C-terminal Myc-tagged
Molecular weight57.8 kDa
ActivityPlease contact us to obtain bioactivity data.
BufferIf the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Research AreasCell Biology

Function

Muscle-specific E3 ubiquitin-protein ligase that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Its ubiquitination activity is mediated by E2 ubiquitin-conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site.

Biological Context

Subcellular Location: Cell membrane, sarcolemma; Cytoplasmic vesicle membrane
Tissue Specificity: Muscle-specific. Exclusively expressed in cardiac and skeletal muscle
Pathway: Protein modification; protein ubiquitination

Product Specifications

Recombinant Mouse Tripartite motif-containing protein 72 (Trim72) is a recombinant protein from Mus musculus (Mouse), expressed in E.coli, covering amino acids 1-477aa, with N-terminal 10xHis-tagged and C-terminal Myc-tagged tag, molecular weight 57.8 kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

SDS-PAGE: Single band at expected molecular weight confirming purity.

ELISA: Suitable as coating antigen or detection standard.

Western Blot: Compatible with standard Western Blot protocols.

Protein Interaction: Validated for SPR (Surface Plasmon Resonance) and BLI (Bio-Layer Interferometry) studies.

Shipping: Shipped at ambient temperature. Lyophilized protein is stable during transit.

Storage: Store lyophilized protein at -20°C to -80°C. Reconstituted protein should be aliquoted and stored at -80°C. Avoid repeated freeze-thaw cycles.

Shelf Life: 12 months from date of receipt when stored as recommended.

Shipping Time: Orders placed before 2 PM EST ship same day. International orders typically deliver within 5-10 business days.

Related products

Protein Biology

Function

Muscle-specific E3 ubiquitin-protein ligase that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites (PubMed:19043407, PubMed:37770719). Its ubiquitination activity is mediated by E2 ubiquitin-conjugating enzymes UBE2D1, UBE2D2 and UBE2D3 (PubMed:37770719). Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site (PubMed:19043407, PubMed:19202355). This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation (PubMed:19043407). Probably acts upstream of the Ca(2+)-dependent membrane resealing process (PubMed:19043407). Required for transport of DYSF to sites of cell injury during repair patch formation (PubMed:19043407). Regulates membrane budding and exocytosis (PubMed:19029292). May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (PubMed:19202355)

Subcellular Location

Cell membrane, sarcolemma; Cytoplasmic vesicle membrane

Tissue Specificity

Muscle-specific. Exclusively expressed in cardiac and skeletal muscle

Subunit

Homodimer (PubMed:37770719). Homooligomer; disulfide-linked (PubMed:19043407, PubMed:37770719). Oligomerizes on the phospholipid membrane (PubMed:37770719). Interacts with DYSF and CAV3 (PubMed:19380584)

Pathway

Protein modification; protein ubiquitination

Gene: Trim72  |  Organism: Mus musculus  |  Synonyms: Mitsugumin-53
Key Publications

Frequently Asked Questions

How do I order or inquire about this product?

Fill out the Online Inquiry form with your required quantity and specifications. You can also email sales@biocrestsci.com. Our team typically responds within 4 business hours with a quote and availability confirmation.

What is the shipping and delivery time?

Orders placed before 2 PM EST ship the same day. Domestic (US) delivery typically takes 2-3 business days. International orders deliver within 5-10 business days. All products are shipped at ambient temperature with appropriate packaging to ensure stability.

How should I store this recombinant protein?

Lyophilized proteins should be stored at -20°C to -80°C upon receipt. After reconstitution, aliquot and store at -80°C. Avoid repeated freeze-thaw cycles. Shelf life is 12 months from date of receipt when stored as recommended.

What quality controls are performed on your products?

Each product undergoes SDS-PAGE purity analysis (typically >85-95%), endotoxin testing, and bioactivity validation. Products are validated for ELISA, Western Blot, and SPR/BLI applications as specified on this product page. A Certificate of Analysis (CoA) is available upon request.

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