Recombinant Human E3 Ubiquitin-Protein Ligase Trim11 (TRIM11) Protein (His-SUMO)

Name: Recombinant Human E3 Ubiquitin-Protein Ligase Trim11 (TRIM11) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09879P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human E3 Ubiquitin-Protein Ligase Trim11 (TRIM11) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q96F44
Target Symbol	TRIM11
Synonyms	BIA 1; BIA1; E3 ubiquitin protein ligase TRIM11; E3 ubiquitin-protein ligase TRIM11; Protein BIA1; RING finger protein 92; RING type E3 ubiquitin transferase TRIM11; RNF 92; RNF92; TRI11_HUMAN; Trim 11; TRIM11; Tripartite motif containing 11; tripartite motif protein 11; Tripartite motif-containing protein 11
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MELRTVCRVPGLVETLRRFRGDVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGSGDTLAPQ
Expression Range	267-468aa
Protein Length	Partial
Mol. Weight	38.5kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	TRIM/RBCC family
Database References	HGNC: 16281 OMIM: 607868 KEGG: hsa:81559 STRING: 9606.ENSP00000284551 UniGene: PMID: 29581427 Data show that miR-24-3p downregulation contributes to tripartite motif-containing protein 11 (TRIM11) upregulation in cancer (CC). PMID: 27888625 TRIM11 promotes the development and progression of HCC through regulating p53 and its downstream signals. PMID: 29190611 data showed that tripartite motif-containing protein 11(TRIM11) expression was significantly elevated in hepatocellular carcinoma(HCC) tissues and overexpression of TRIM11 is closely associated with HCC progression and poor survival PMID: 28065743 Results show that TRIM11 was highly expressed in lung cancer tissues and cell lines and suggest that it acts as an oncogene in lung cancer through promoting cell growth, migration and invasion. PMID: 27329103 TRIM11 suppresses AIM2 inflammasome by degrading AIM2 via p62-dependent selective autophagy. PMID: 27498865 TRIM11 to be overexpressed in HCC tissues and cell lines. Downregulation of TRIM11 inhibited HCC cell proliferation and invasion in vitro and in vivo as well as suppressed the epithelial-mesenchymal transition (EMT) process. PMID: 28244856 study identified TRIM11 as a new HIV-1 capsid binding protein; data also reveal that TRIM11 restricts HIV-1 reverse transcription by accelerating viral uncoating, and microtubule dynamics is implicated in TRIM11-imposed block to early events of HIV-1 replication PMID: 27737691 TRIM11 is a host cellular factor that interferes with the early steps of HIV-1 replication and provides a connection between viral protein and host antiviral factors. PMID: 25105968 TRIM11 is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. PMID: 23178488 TRIM11 negatively regulates IFN-beta production and antiviral activity by targeting TBK1. PMID: 23675467 Study shows that the E3 ubiquitin ligase TRIM11 plays a critical role in the clearance of mutant PHOX2B, which causes congenital central hypoventilation syndrome, through the proteasome. PMID: 22307522 PAX6 interacts with HOMER3, DNCL1, and TRIM11. Three C-terminal PAX6 mutations, previously identified in patients with eye malformations, all reduced or abolished the interactions. PMID: 16098226 These results suggest that TRIM11, with the ubiquitin-proteasome pathway, regulates ARC105 function in TGFbeta signaling. PMID: 16904669 Downregulation of TRIM11 and TRIM15 enhanced virus release suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. PMID: 18248090 This study suggests a potential role for Trim11 in the specification of NA phenotype by interaction with Phox2b. PMID: 18275850

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.