Recombinant Human NOL3 Protein

Beta LifeScience SKU/CAT #: BL-2041NP

Recombinant Human NOL3 Protein

Beta LifeScience SKU/CAT #: BL-2041NP
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Product Overview

Description Recombinant Human Nucleolar Protein 3 is produced by our E.coli expression system and the target gene encoding Met1-Ser208 is expressed.
Accession O60936
Synonym Nucleolar Protein 3; Apoptosis Repressor With CARD; Muscle-Enriched Cytoplasmic Protein; Myp; Nucleolar Protein of 30 kDa; Nop30
Gene Background Nucleolar protein 3 is encoded by NOL3 gene. Multiple transcript variants encoding different isoforms have been found for this gene. So far, Nucleolar protein 3 has show to have two Isoforms. Isoform 1 may be involved in RNA splicing. Isoform 2 functions as an apoptosis repressor that blocks multiple modes of cell death. It inhibits extrinsic apoptotic pathways through two different ways. Firstly, it by interacting with FAS and FADD upon FAS activation blocking death-inducing signaling complex (DISC) assembly. Secondly by interacting with CASP8 in a mitochondria localization- and phosphorylation-dependent manner, limiting the amount of soluble CASP8 available for DISC-mediated activation. It has been shown to down-regulate the enzyme activities of caspase 2, caspase 8 and tumor protein p53.
Molecular Mass 22.63 KDa
Apmol Mass 29 KDa, reducing conditions
Formulation Supplied as a 0.2 μm filtered solution of 20mM PB, 150mm NaCl, 1mM DTT, 1mM EDTA, 10% Glycerol, pH7.0.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Biological Activity Not tested
Storage Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function May be involved in RNA splicing.; Functions as an apoptosis repressor that blocks multiple modes of cell death. Inhibits extrinsic apoptotic pathways through two different ways. Firstly by interacting with FAS and FADD upon FAS activation blocking death-inducing signaling complex (DISC) assembly. Secondly by interacting with CASP8 in a mitochondria localization- and phosphorylation-dependent manner, limiting the amount of soluble CASP8 available for DISC-mediated activation. Inhibits intrinsic apoptotic pathway in response to a wide range of stresses, through its interaction with BAX resulting in BAX inactivation, preventing mitochondrial dysfunction and release of pro-apoptotic factors. Inhibits calcium-mediated cell death by functioning as a cytosolic calcium buffer, dissociating its interaction with CASP8 and maintaining calcium homeostasis. Negatively regulates oxidative stress-induced apoptosis by phosphorylation-dependent suppression of the mitochondria-mediated intrinsic pathway, by blocking CASP2 activation and BAX translocation. Negatively regulates hypoxia-induced apoptosis in part by inhibiting the release of cytochrome c from mitochondria in a caspase-independent manner. Also inhibits TNF-induced necrosis by preventing TNF-signaling pathway through TNFRSF1A interaction abrogating the recruitment of RIPK1 to complex I. Finally through its role as apoptosis repressor, promotes vascular remodeling through inhibition of apoptosis and stimulation of proliferation, in response to hypoxia. Inhibits too myoblast differentiation through caspase inhibition.
Subcellular Location [Isoform 1]: Nucleus, nucleolus.; [Isoform 3]: Cytoplasm.; [Isoform 2]: Cytoplasm. Mitochondrion. Sarcoplasmic reticulum. Membrane; Lipid-anchor.
Database References
Associated Diseases Myoclonus, familial cortical (FCM)
Tissue Specificity Highly expressed in heart and skeletal muscle. Detected at low levels in placenta, liver, kidney and pancreas.

Gene Functions References

  1. Results show that in response to DNA damage, p53 total levels increase proportionally to the strength of the damage; however, p53 tetramers are formed at a constant rate under the control of ARC protein. PMID: 25344068
  2. role of apoptosis repressor with a CARD domain (ARC) in the therapeutic resistance of renal cell carcinoma PMID: 28464919
  3. a novel genetic primary myelofibrosis-like mouse model and identify a tumor suppressor role for NOL3 in the pathogenesis of myeloid malignancies. PMID: 28232469
  4. Increased ARC expression is associated with liver metastasis of colorectal cancer. PMID: 26721253
  5. RUNX3, miR-185 and ARC regulate the sensitivity of gastric cancer cells to chemotherapy. PMID: 24763054
  6. ARC is regulated via BIRC2/MAP3K14 signalling and its overexpression in AML or MSCs can function as a resistant factor to birinapant-induced leukaemia cell death. PMID: 25079338
  7. high expression of ARC plays an important role in the pathogenesis of nasopharyngeal carcinoma and leads to X-radiation and cisplatin resistance in nasopharyngeal carcinoma. PMID: 23877130
  8. ARC is a previously unrecognized inhibitor of apoptosis in beta-cells and that its protective effects are mediated through suppression of the ER stress response pathway. PMID: 22933109
  9. This study utilized unbiased, genome-wide approaches to identify a NOL3 mutation that likely causes Familial cortical myoclonus. PMID: 22926851
  10. HIF-1alpha directly bound to hypoxia-responsive element located at -419 to -414 of ARC gene, which is essential for HIF-1-induced expression. PMID: 22475487
  11. Data show that ARC promotes breast carcinogenesis by driving primary tumor growth, invasion, and metastasis as well as by promoting chemoresistance in invasive cells. PMID: 22037876
  12. ARC, previously unlinked to pulmonary hypertension, is a critical determinant of vascular remodeling in this syndrome. PMID: 22082675
  13. Results suggest that ARC expression levels are highly prognostic in AML and that ARC is a potential therapeutic target in AML. PMID: 21041716
  14. Ras induces ARC in epithelial cancers, and ARC plays a role in the oncogenic actions of Ras PMID: 20392691
  15. These results suggest that the antiapoptotic effect of apoptotic repressor with caspase recruitment domain is, in part, due to inhibition of voltage-gated potassium channels in cardiomyocytes. PMID: 12734105
  16. calcium binding mediates regulation of caspase 8 and cell death by ARC PMID: 15509781
  17. Unexpectedly, ARC was localized almost exclusively to the nuclei of cancer cells, which was unlike the cytoplasmic localization of ARC in non-cancer cells PMID: 15848180
  18. ARC was present in the cytoplasm and nuclei of epithelial cells in invasive ductal carcinoma PMID: 15861191
  19. is downregulated in human failing myocardium PMID: 16505176
  20. nuclear apoptosis repressor with caspase recruitment domain (ARC)is induced in cancer cells and negatively regulates p53 PMID: 18087040
  21. the high level of ARC protein and the constitutive phosphorylation of ARC in cancer cells may play an important role in the protection of cancer cells against oxidative stress PMID: 18172857
  22. Transfection of cDNA encoding ARC into Me1007 cells inhibited both caspase-8 activation and apoptosis induced by thapsigargin or tunicamycin. PMID: 18245485
  23. ARC is a novel marker of human colon cancer and suggest that it may be a general feature of epithelial cancers. PMID: 18469522
  24. the balance between antiapoptotic ARC and proapoptotic caspase-8 is the only one to be disturbed during carcinogenesis and tumour progression of renal cell carcinomas PMID: 18516683
  25. ARC undergoes poly-ubiquitination and subsequent proteasome-dependent degradation. Mutation of ARC's lysine residues prevents this and enhances its pro-survival effects. PMID: 17142452
  26. ARC holds multiple death pathways in check by non-homotypic death-fold interactions. Loss of ARC disinhibits these, leading to accelerated DISC assembly and Bax activation and may be an apoptotic trigger in heart failure and ischemia-reperfusion. PMID: 15383280
  27. The CARD of ARC binds the Bax C-terminus, preventing Bax activation and activation of the intrinsic mitochondrial pathway PMID: 15383280
  28. ARC is recruited to the Fas DISC. By interacting with Fas and FADD through CARD-DD and CARD-DED interactions, ARC prevents DISC assembly and procaspase-8 activation. PMID: 15383280


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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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