Recombinant Human RanBP2 Protein

Beta LifeScience SKU/CAT #: BLA-7633P

Recombinant Human RanBP2 Protein

Beta LifeScience SKU/CAT #: BLA-7633P
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Product Overview

Host Species Human
Accession P49792
Synonym 358 kDa nucleoporin ANE1 E3 SUMO-protein ligase RanBP2 IIAE3 Nuclear pore complex protein Nup358 Nucleoporin 358 Nucleoporin Nup358 NUP358 p270 RAN binding protein 2 Ran-binding protein 2 RANBP2 RBP2_HUMAN Transformation related protein 2 TRP 1 TRP 2 TRP1 TRP2
Description Recombinant Human RanBP2 Protein was expressed in E.coli. It is a Protein fragment
Source E.coli
Purity >75% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity The specific activity of this protein was 73 nmol/min/mg in SUMOylation assay using SUMO2 (1-93) as substrate.
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single-stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity.
Subcellular Location Nucleus. Nucleus membrane. Nucleus, nuclear pore complex. Nucleus envelope.
Protein Families RanBP2 E3 ligase family
Database References
Associated Diseases Encephalopathy, acute, infection-induced, 3 (IIAE3)

Gene Functions References

  1. We describe three in vitro reconstituted disassembly intermediates, which show binding of a Crm1 export complex via two FG-repeat patches, cargo-release by RanBP2's Ran-binding domains and retention of free Crm1 at RanBP2 after Ran-GTP hydrolysis. PMID: 27160050
  2. RAN binding protein 2 increase the sumoylation of cyclin-dependent kinase inhibitor 1B in cholangiocarcinoma cell line QBC939. PMID: 28882106
  3. Importin-beta and CRM1 control a RANBP2 spatiotemporal switch essential for mitotic kinetochore function. PMID: 28600321
  4. Translocation of p53 is regulated by androgen-dependent sumoylation mediated by the G3BP2-interacting SUMO-E3 ligase, RanBP2. G3BP2 knockdown results in reduced tumor growth and increased nuclear p53 accumulation in mouse xenograft models of prostate cancer with or without long-term androgen deprivation. PMID: 28692047
  5. These our results reveal spatio-temporal regulation in the recruitment of nucleoporins and translation factors to cytoplasmic viral factories , and particularly the importance of Nup358 in vaccinia virus infection. PMID: 28963881
  6. NUSAP1 contributes to accurate chromosome segregation by acting as a co-factor for RanBP2-RanGAP1-UBC9 during cell division. PMID: 28900032
  7. Nup358-AGO interaction is important for miRNA-mediated gene silencing and identifies SIM as a new interacting motif for the AGO family of proteins. PMID: 28039207
  8. recurrent or familial ANE without the RANBP2 mutation has a more severe outcome and greater predilection for male sex than that with the RANBP2 mutation. This suggests that there are unknown gene mutations linked to ANE. PMID: 27882739
  9. Based on the literature review of ANE1 with RANBP2 mutation, we propose a threshold for RANBP2 mutation tes PMID: 25522933
  10. findings indicate that RanGDP and not RanGTP is the physiological target for the RanBP2 SUMO E3 ligase complex PMID: 26251516
  11. Taken together, topographic and functional interactions between dynactin, importin-beta and RanBP2 are involved in nuclear translocation of IGF-1R. PMID: 24909165
  12. analysis of the RANBP2-ALK gene fusion identified in ALK-positive diffuse large B-cell lymphoma with a unique nuclear membrane staining of ALK protein PMID: 24470379
  13. Nup358, a nucleoporin that forms the cytoplasmic filaments of the nuclear pore complex, plays an important role in the nuclear import of hTERT. PMID: 24586428
  14. Our data show that Nup358 supports nuclear transport functions important for cellular homeostasis and for HIV-1 nuclear import PMID: 24586169
  15. Case Report/Review: RANBP2-ALK gene rearrangement in inflammatory myofibroblastic tumors. PMID: 24034896
  16. RANBP2-ALK fusion combined with monosomy 7 may be related to a unique clonal hematologic disorder of childhood and adolescence, characterized by myelomonocytic leukemia and a poor prognosis [case report/ review] PMID: 24613277
  17. Mitotic arrest and the following cell death were caused by depletion of RanBP2. PMID: 24113188
  18. Isomerization by NUP358 may be preserved by HIV-1 to target the nuclear pore and synchronize nuclear entry with capsid uncoating. PMID: 23902822
  19. The translation of a subset of mRNAs encoding secretory proteins is potentiated by RanBP2. PMID: 23630457
  20. These findings reveal novel roles of Ranbp2 in the modulation of intrinsic and extrinsic cell death mechanisms and pathways PMID: 23818861
  21. The structure reveals that the C-terminal domain adopts a cyclophilin-like fold with a non-canonical active-site configuration. PMID: 23353830
  22. Knockdown of RANBP2 specifically affected the late step of nuclear entry, inducing cytoplasmic granules enriched with phosphorylated components. This suggests a novel regulatory mechanism for nuclear speckle formation involving RANBP2 and phosphorylation. PMID: 22262462
  23. Nup358 functions as a cargo- and receptor-specific assembly platform, increasing the efficiency of nuclear import of proteins through various mechanisms. PMID: 21995724
  24. Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2. PMID: 22194619
  25. A critical function of RanBP2 is to capture recycling RanGTP-importin-beta complexes at cytoplasmic fibrils to allow for adequate classical nuclear localization signal-mediated cargo import. PMID: 21859863
  26. Data show that Epac1 directly interacts with the zinc fingers of RanBP2, tethering Epac1 to the nuclear pore complex, revealing a novel mechanism of Epac1 regulation and an unexpected link between the NPC and cAMP signaling. PMID: 21670213
  27. This study measures for the first time the activation entropy and enthalpy of ubiquitin-like modifications and finds that the E3 ligase, RanBP2, confers a large entropic effect to lower the activation energy, thereby accelerating the reactions. PMID: 21568279
  28. RanBP2 is a host factor that is involved in the nuclear import of HIV-1 PIC (DNA), but is not critical to the nuclear export of the viral mRNAs or nucleo-cytoplasmic shuttling of Rev PMID: 21179483
  29. Data establish a subset of RANBP2-type zinc fingers as a new family of ssRNA-binding motifs. PMID: 21256132
  30. Untreated recurrent acute necrotising encephalopathy associated with RANBP2 missense mutation, and normal outcome in a Caucasian boy. PMID: 20473521
  31. ANE may, in some instances, represent a familial disorder or may be the result of an inherited predisposition due to a mutation in the RANBP2 gene. It also broadens the phenotype of neurological problems in individuals that harbour a RANBP2 mutation. PMID: 19807769
  32. Both the patient and her mother, who had also had postviral polyneuritis in the past, harbour a mutation in Ran-binding protein 2 (RANBP2); this occurred de novo in the mother and confers genetic susceptibility to ANE. PMID: 19811512
  33. Oxidative stress up-regulated the binding of Crm1 to Ran and affected multiple repeat-containing nucleoporins by changing their localization, phosphorylation, O-glycosylation, or interaction with other transport components. PMID: 19828735
  34. Here, we define a Pro-Glu-Asp-Ser-Thr-rich element containing 129 amino acid residues, designated IR1+2, on the human nucleoporin RanBP2/Nup358, which binds directly to Ubc9 with high affinity both in vitro and in vivo PMID: 11709548
  35. The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase PMID: 12032081
  36. identification of RanBP2-mediated transport pathways with restricted neuronal and subcellular localization PMID: 12191015
  37. RanBP2 sumoylates MDM2 during nuclear translocation in human cells PMID: 12393906
  38. Without Nup358, chromosome congression and segregation are severely perturbed. Meanwhile, the assembly of other kinetochore components is strongly inhibited. PMID: 12963708
  39. RanGAP1 remains associated with RanBP2/Nup358 and the SUMO E2-conjugating enzyme Ubc9 in mitosis. PMID: 15037602
  40. Ubc9- small ubiquitin-like modifier (SUMO-1) thioester could be recruited to RanBP2 via SUMO-1 in the absence of strong binding between Ubc9 and RanBP2 PMID: 15608651
  41. Nup358/RanBP2 acts as an E3 by binding both SUMO and Ubc9 to position the SUMO-E2-thioester in an optimal orientation to enhance conjugation PMID: 15931224
  42. the intracellular levels of RanBP2 and its functional activity may be modulated by Parkin-mediated ubiquitination and proteasomal pathways PMID: 16332688
  43. The Trp2 allele is an age-dependent risk factor for the severity of disc degeneration in younger patients with symptomatic herniated nucleus pulposus of the lumbar spine. PMID: 16586133
  44. Our data imply that SUMO E3 proteins like RanBP2 facilitate spatio-temporal SUMOylation for certain nuclear structure and function. PMID: 16688858
  45. ent-15-oxokaurenoic acid inhibits mitotic chromosome movement and binds the kinetochore protein ran-binding protein 2 PMID: 17168522
  46. binding of the kinesin-binding domain of RanBP2 to KIF5B and KIF5C determines mitochondria localization and function PMID: 17887960
  47. Biopsy samples from 288 patients suffering from LDD with and without relapse were analyzed by PCR restriction fragment analysis and direct sequencing. The mutated Trp2 allele was not detected in the patients' samples of the present study. PMID: 18080148
  48. These data suggest a dual function of the Nup358-RanGAP1 complex as a coordinator of importin beta recycling and reformation of novel import complexes. PMID: 18305100
  49. Silencing of the RANBP2 E3 ligase reverts HDAC 4 repression by blocking its own sumoylation PMID: 18691615
  50. Data describe a mitotic SUMO2/3 conjugation-deconjugation cycle of Borealin and further assign a regulatory function of RanBP2 and SENP3 in the mitotic SUMO pathway. PMID: 18946085


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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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