Recombinant Human Ring Finger Protein 11 (RNF11) Protein (His)

Beta LifeScience SKU/CAT #: BLC-10460P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Ring Finger Protein 11 (RNF11) Protein (His)

Beta LifeScience SKU/CAT #: BLC-10460P
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Product Overview

Description Recombinant Human Ring Finger Protein 11 (RNF11) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q9Y3C5
Target Symbol RNF11
Synonyms CGI 123; RING finger protein 11; RNF11; RNF11_HUMAN; Sid 1669; SID1669
Species Homo sapiens (Human)
Expression System Yeast
Tag N-6His
Target Protein Sequence GNCLKSPTSDDISLLHESQSDRASFGEGTEPDQEPPPPYQEQVPVPVYHPTPSQTRLATQLTEEEQIRIAQRIGLIQHLPKGVYDPGRDGSEKKIRECVICMMDFVYGDPIRFLPCMHIYHLDCIDDWLMRSFTCPSCMEPVDAALLSSYETN
Expression Range 2-154aa
Protein Length Full Length of Mature Protein
Mol. Weight 19.3kDa
Research Area Epigenetics And Nuclear Signaling
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 Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome.
Subcellular Location Early endosome. Recycling endosome. Cytoplasm. Nucleus.
Database References

HGNC: 10056

OMIM: 612598

KEGG: hsa:26994

STRING: 9606.ENSP00000242719

UniGene: PMID: 28292929

  • Up-regulation of COPII components requires the transcriptional regulator RNF11, which localizes to early endosomes and appears additionally in the cell nucleus upon continuous EGF stimulation. PMID: 27872256
  • RNF11 is at the center of a finally regulated system where it acts both as an adaptor and a modulator of itch-mediated control of ubiquitination events underlying membrane traffic. PMID: 25195858
  • Our data exemplifies the relevance of RNF11 and persistent NF-kappaB activation in Parkinson's disease PMID: 23669642
  • The negative influence that perturbation of RNF11 and SARA levels exerts on the lysosomal degradation of EGFRs could underscore the significance of overexpression of RNF11 in certain cancers. PMID: 23222715
  • RNF11 functions together with TAX1BP1 to restrict antiviral signaling and IFN-beta production. PMID: 23308279
  • RNF11 negatively regulates canonical NF-kappaB signaling in the nervous system. PMID: 22507528
  • Microglial RNF11 is a negative regulator of NF-kappaB signalling pathway and could be a strong potential target for modulating inflammatory responses in neurodegenerative diseases. PMID: 22975135
  • Data show that membrane anchoring through acylation is necessary for RNF11 to be post-translationally modified by the addition of several ubiquitin moieties. PMID: 20676133
  • overexpression of RNF11, through its interaction with Smurf2, can restore TGFbeta responsiveness in transfected tumor cells PMID: 14562029
  • characterization of ring finger protein 11 PMID: 16123141
  • RNF11 is a small RING E3 ligase that affects transforming growth factorbeta and EGF-R signaling and is overexpressed in invasive breast cancers PMID: 16925951
  • these findings identify RNF11 as a strong candidate gene at the PARK10 locus and highlight its potential significance in the development of the common form of Parkinson disease PMID: 17917589
  • Analysis reveals that the main determinants of selectivity between ubiquitin ligases RNF11 and E2 ubiquitin-conjugating enzymes resides on ring domains, rather than on the E2s. PMID: 18615712
  • RNF11, together with TAX1BP1 and Itch, is an essential component of an A20 ubiquitin-editing protein complex that ensures transient activation of inflammatory signalling pathways. PMID: 19131965
  • FAQs

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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.

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