Recombinant Human E3 Ubiquitin-Protein Ligase Nrdp1 (RNF41) Protein (GST)

Name: Recombinant Human E3 Ubiquitin-Protein Ligase Nrdp1 (RNF41) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08682P
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 Nrdp1 (RNF41) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9H4P4
Target Symbol	RNF41
Synonyms	4930511A05Rik; 4933415P08Rik; E3 ubiquitin protein ligase NRDP1; E3 ubiquitin-protein ligase NRDP1; Fetal Liver RING finger protein; FLRF; MGC45228; Neuregulin receptor degradation protein 1; NRDP1; RING finger protein 41; rnf41; RNF41_HUMAN; SBBI03
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MGYDVTRFQGDVDEDLICPICSGVLEEPVQAPHCEHAFCNACITQWFSQQQTCPVDRSVVTVAHLRPVPRIMRNMLSKLQIACDNAVFGCSAVVRLDNLMSHLSDCEHNPKRPVTCEQGCGLEMPKDELPNHNCIKHLRSVVQQQQTRIAELEKTSAEHKHQLAEQKRDIQLLKAYMRAIRSVNPNLQNLEETIEYNEILEWVNSLQPARVTRWGGMISTPDAVLQAVIKRSLVESGCPASIVNELIENAHERSWPQGLATLETRQMNRRYYENYVAKRIPGKQAVVVMACENQHMGDDMVQEPGLVMIFAHGVEEI
Expression Range	1-317aa
Protein Length	Full Length
Mol. Weight	62.9kDa
Research Area	Cell Biology
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

Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins. Polyubiquitinates MYD88. Negatively regulates MYD88-dependent production of proinflammatory cytokines. Can promote TRIF-dependent production of type I interferon and inhibits infection with vesicular stomatitis virus. Promotes also activation of TBK1 and IRF3. Involved in the ubiquitination of erythropoietin (EPO) and interleukin-3 (IL-3) receptors. Thus, through maintaining basal levels of cytokine receptors, RNF41 is involved in the control of hematopoietic progenitor cell differentiation into myeloerythroid lineages. Contributes to the maintenance of steady-state ERBB3 levels by mediating its growth factor-independent degradation. Involved in the degradation of the inhibitor of apoptosis BIRC6 and thus is an important regulator of cell death by promoting apoptosis. Acts also as a PRKN modifier that accelerates its degradation, resulting in a reduction of PRKN activity, influencing the balance of intracellular redox state. The RNF41-PRKN pathway regulates autophagosome-lysosome fusion during late mitophagy. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control.

Database References

HGNC: 18401

KEGG: hsa:10193

STRING: 9606.ENSP00000342755

UniGene: PMID: 29180353

Over-expression of miR-497 promotes the proliferation of glioma cells U87 by targeting Nrdp1. PMID: 28871945

Authors conclude that the planar cell polarity (PCP) pathway contributes significantly to the motility and hence the invasiveness of glioblastoma multiforme (GBM) cells, and that Nrdp1 acts as a negative regulator of PCP signaling by inhibiting Dvl through a novel polyubiquitination mechanism. PMID: 28481871

Data suggest that PHLPP1 plays an important role in assembly of kinetochores by counteracting RNF41-mediated SGT1 degradation. (PHLPP1 = PH domain and leucine rich repeat protein phosphatase 1; RNF41 = ring finger protein 41; SGT1 = suppressor of G2 allele of SKP1) PMID: 28696259

Results show low expression level of NRDP1 in colorectal neoplasm independently of tumor stage. PMID: 27648936

findings suggest that HBx promotes the progression of hepatocellular carcinoma by decreasing the stability of Nrdp1, which results in up-regulation of ErbB3 PMID: 26846102

the association between RNF41 polymorphisms and congenital heart disease in the Chinese Mongolian population PMID: 27323192

Nrdp1S is a tumour suppressor that which potentiates the Nrdp1-mediated ubiquitination and degradation of ErbB3. An Nrdp1S deficiency may also be an important factor in the loss of Nrdp1. PMID: 26612725

HPV 16 E2 can modulate ErbB-3 by interacting with Nrdp-1, which is involved in the regulation of this receptor, via ubiquitination and degradation. PMID: 26963794

The results of this study suggested that Nrdp1-mediated ErbB3 degradation suppresses glioma migration and invasion and that loss of Nrdp1 may amplify ErbB3 signaling to contribute to glioma migration and invasion. PMID: 26088461

ABPN downregulates multiple components of the EGFR/ErbB3 signaling pathway through Nrdp1 activation. PMID: 26464195

Nrdp1 may serve as a useful biomarker for the clinical outcome and efficacy of adjuvant anthracyclines-based chemotherapy in breast cancer. PMID: 25519010

Lower expression of Nrdp1 in human glioma contributes tumor progression by reducing apoptosis. PMID: 25355637

Phosphorylation of RNF41 by Par-1b regulates basolateral membrane targeting of laminin-111 receptors. PMID: 24259665

Balanced reciprocal cross-regulation of RNF41 and USP8 determines whether receptors are sorted for lysosomal degradation or recycling, this way regulating basal cytokine receptor levels. PMID: 23750007

Coiled-coil domain deletion abrogates Nrdp1 oligomerization and suppresses Nrdp1 but not ErbB3 ubiquitination and degradation. PMID: 24519943

Data demonstrate that Nrdp1 preferentially associates with the nascent form of ErbB3 to accelerate its degradation, and that the two proteins colocalize at the endoplasmic reticulum. PMID: 21576364

these data provide insights into understanding the potential role of Nrdp1 in cell growth, apoptosis and oxidative stress, and in the pathogenesis of Parkinson's disease. PMID: 21693106

RNF41 interacts with JAK2-associated cytokine receptor complexes and modulates their cell surface exposure and signalling. PMID: 21378310

Post-transcriptional mechanisms contribute to the suppression of the ErbB3 negative regulator protein Nrdp1 in mammary tumors. PMID: 20628057

Observations point to a model of CRPC development in which progression of PCa to castration resistance is associated with the inability of AR to transcriptionally regulate Nrdp1, and predict that inhibition of ErbB3 during AW may impair CRPC development. PMID: 20587519

This study do not support the hypothesis of a major role for the Nrdp1 gene in PD development in the Chinese population. PMID: 19800834

RNF41 mRNA measured by real time reverse-transcriptase polymerase chain reaction reaction quantifies heart allograft apoptosis in graft rejection. PMID: 20098290

Nrdp1 can be important in the initiation of apoptosis by catalyzing ubiquitination and degradation of BRUCE. PMID: 14765125

Results indicate that Nrdp1 is a specific target for the USP8 deubiquitinating enzyme and are consistent with a model where USP8 augments Nrdp1 activity by mediating its stabilization PMID: 15314180

The USP8 recognition domain of NRDP1 has a novel protein fold that interacts with a conserved peptide loop of the rhodanese domain. PMID: 17035239

Neuregulin 1-induced protein stability cascade involving USP8 and Nrdp1 mediates the down-regulation of ErbB3 PMID: 17210635

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.

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