Recombinant Human E3 Sumo-Protein Ligase Ranbp2 (RANBP2) Protein (His-B2M)

Name: Recombinant Human E3 Sumo-Protein Ligase Ranbp2 (RANBP2) Protein (His-B2M)
Brand: Beta LifeScience
SKU: BLC-09228P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human E3 Sumo-Protein Ligase Ranbp2 (RANBP2) Protein (His-B2M) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P49792
Target Symbol	RANBP2
Synonyms	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
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-B2M
Target Protein Sequence	PTEESSINYTFKTPEKAKEKKKPEDSPSDDDVLIVYELTPTAEQKALATKLKLPPTFFCYKNRPDYVSEEEEDDEDFETAVKKLNGKLYLDGSEKCRPLEENTADNEKECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELQKVQEAQKSQTEEITSTTDSVYTGGTEVMVPSFCKSEEPDSITKS
Expression Range	2601-2802aa
Protein Length	Partial
Mol. Weight	36.8kDa
Research Area	Others
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 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	HGNC: 9848 OMIM: 601181 KEGG: hsa:5903 STRING: 9606.ENSP00000283195 UniGene: PMID: 27160050 RAN binding protein 2 increase the sumoylation of cyclin-dependent kinase inhibitor 1B in cholangiocarcinoma cell line QBC939. PMID: 28882106 Importin-beta and CRM1 control a RANBP2 spatiotemporal switch essential for mitotic kinetochore function. PMID: 28600321 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 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 NUSAP1 contributes to accurate chromosome segregation by acting as a co-factor for RanBP2-RanGAP1-UBC9 during cell division. PMID: 28900032 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 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 Based on the literature review of ANE1 with RANBP2 mutation, we propose a threshold for RANBP2 mutation tes PMID: 25522933 findings indicate that RanGDP and not RanGTP is the physiological target for the RanBP2 SUMO E3 ligase complex PMID: 26251516 Taken together, topographic and functional interactions between dynactin, importin-beta and RanBP2 are involved in nuclear translocation of IGF-1R. PMID: 24909165 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 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 Our data show that Nup358 supports nuclear transport functions important for cellular homeostasis and for HIV-1 nuclear import PMID: 24586169 Case Report/Review: RANBP2-ALK gene rearrangement in inflammatory myofibroblastic tumors. PMID: 24034896 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 Mitotic arrest and the following cell death were caused by depletion of RanBP2. PMID: 24113188 Isomerization by NUP358 may be preserved by HIV-1 to target the nuclear pore and synchronize nuclear entry with capsid uncoating. PMID: 23902822 The translation of a subset of mRNAs encoding secretory proteins is potentiated by RanBP2. PMID: 23630457 These findings reveal novel roles of Ranbp2 in the modulation of intrinsic and extrinsic cell death mechanisms and pathways PMID: 23818861 The structure reveals that the C-terminal domain adopts a cyclophilin-like fold with a non-canonical active-site configuration. PMID: 23353830 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 Nup358 functions as a cargo- and receptor-specific assembly platform, increasing the efficiency of nuclear import of proteins through various mechanisms. PMID: 21995724 Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2. PMID: 22194619 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 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 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 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 Data establish a subset of RANBP2-type zinc fingers as a new family of ssRNA-binding motifs. PMID: 21256132 Untreated recurrent acute necrotising encephalopathy associated with RANBP2 missense mutation, and normal outcome in a Caucasian boy. PMID: 20473521 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 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 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 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 The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase PMID: 12032081 identification of RanBP2-mediated transport pathways with restricted neuronal and subcellular localization PMID: 12191015 RanBP2 sumoylates MDM2 during nuclear translocation in human cells PMID: 12393906 Without Nup358, chromosome congression and segregation are severely perturbed. Meanwhile, the assembly of other kinetochore components is strongly inhibited. PMID: 12963708 RanGAP1 remains associated with RanBP2/Nup358 and the SUMO E2-conjugating enzyme Ubc9 in mitosis. PMID: 15037602 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 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 the intracellular levels of RanBP2 and its functional activity may be modulated by Parkin-mediated ubiquitination and proteasomal pathways PMID: 16332688 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 Our data imply that SUMO E3 proteins like RanBP2 facilitate spatio-temporal SUMOylation for certain nuclear structure and function. PMID: 16688858 ent-15-oxokaurenoic acid inhibits mitotic chromosome movement and binds the kinetochore protein ran-binding protein 2 PMID: 17168522 binding of the kinesin-binding domain of RanBP2 to KIF5B and KIF5C determines mitochondria localization and function PMID: 17887960 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 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 Silencing of the RANBP2 E3 ligase reverts HDAC 4 repression by blocking its own sumoylation PMID: 18691615 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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