Recombinant Human E3 Ubiquitin-Protein Ligase Rbx1 (RBX1) Protein (GST)

Name: Recombinant Human E3 Ubiquitin-Protein Ligase Rbx1 (RBX1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09196P
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 Rbx1 (RBX1) 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	P62877
Target Symbol	RBX1
Synonyms	BA554C12.1; E3 ubiquitin-protein ligase RBX1; FLJ60363; MGC13357; MGC1481; OTTHUMP00000028983; Protein ZYP; Rbx 1; Rbx1; RBX1_HUMAN; Regulator of cullins 1; Ring box 1; Ring box 1 E3 ubiquitin protein ligase; RING box protein 1; RING finger protein 75; RING finger protein; RING-box protein 1; Ringbox protein 1 ; RNF 75; RNF75; ROC 1; ROC1; ZYP protein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH
Expression Range	1-108aa
Protein Length	Full Length
Mol. Weight	39.3kDa
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	E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Recruits the E2 ubiquitin-conjugating enzyme CDC34 to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and CUL3, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	RING-box family
Database References	HGNC: 9928 OMIM: 603814 KEGG: hsa:9978 STRING: 9606.ENSP00000216225 UniGene: PMID: 28685749 SESN2 is critical to protect cells against detrimental effect of mitochondrial damage and RBX1 is a negative regulator of SESN2 which hampers its stabilization. PMID: 29294217 RBX-1 overexpression in bladder UCC is associated with high tumor grade and advanced stage and represents biological potential of invasiveness and aggressive disease. PMID: 28946546 The crystal structure of a pentameric CRL2(VHL) complex, composed of Cul2, Rbx1, Elongin B, Elongin C, and pVHL reveals how Rbx1 interacts with Cullin 2. PMID: 28591624 Study demonstrated that ROC1 was overexpressed in esophageal squamous cell carcinomas, which was positive associated with poor prognosis of esophageal cancer patients. PMID: 28418860 p97 negatively regulates NRF2 through the canonical pathway by extracting ubiquitylated NRF2 from the KEAP1-CUL3 E3 complex. PMID: 28115426 Regulation of substrate ubiquitination and polyubiquitination takes place through Rbx1 rotations. PMID: 28082425 High RBX1 expression was related to poor tumor differentiation, advanced TNM stage, and lymph node metastasis in non-small cell lung cancer. PMID: 27566015 Data show that melanoma antigen, family C, 2 protein (MAGE-C2) binds with RING-box protein 1 (Rbx1) and Cullin 1, and regulates cyclin E stability in melanoma cells. PMID: 26540345 ROC1 has an important role in the malignant progression of bladder transitional cell carcinoma via the mTOR/DEPTOR pathway. PMID: 26742010 Nedd8(Q40E) cannot induce the same structural effect on Cul1-Rbx1 as wild-type Nedd8. PMID: 26632597 RBX1 E3 ubiquitin protein expression responsible with multiple genetic mechanism in the development of head and neck cancer. PMID: 24596130 This work sheds new light on the roles of NEDD8 lysines on neddylation cascades and provides a dominant negative mutant for the study of neddylation and its biological functions. PMID: 25918018 These findings indicate that Rbx1 and Rbx2 can both activate Cul5-Vif E3 ligase in vitro, but they may undergo a more delicate selection mechanism in vivo. PMID: 25912140 upregulation of miR-194 can inhibit proliferation, migration, and invasion of GC cells, possibly by targeting RBX1. Aberrant expression of miR-194 and RBX1 is correlated to GC patient survival time. PMID: 25412959 RBX1 expression level was associated with the proliferation of gastric cancer. PMID: 24292229 Studied the DNA-level mechanisms affecting KEAP1/CUL3/RBX1 E3-ubiquitin ligase complex as a regulator of NRF2 levels in ovarian cancer. PMID: 25114896 eEF1A1 may mediate SAMHD1 turnover by targeting it to the proteosome for degradation through association with Cullin4A and Rbx1. PMID: 25423367 data suggest a new paradigm for Hsp90-modulated assembly of a Cul3/DBC2 E3 ubiquitin ligase complex that may extend to other E3 ligase complexes. PMID: 24608665 CUL4A-DDB1-Rbx1 E3 ligase controls the quality of the PTS2 receptor Pex7p. PMID: 24989250 A genome-wide association study on a southern European population identified a new Crohn's disease susceptibility locus at RBX1-EP300. PMID: 22936669 Overexpression of RBX1 protein contributes to tumor progression and poor prognosis of non-muscle-invasive bladder cancer (NMIBC). PMID: 23609182 ROC1 knockdown significantly inhibited the growth of liver cancer cells by sequentially and independently inducing autophagy and p21-dependent cell senescence. PMID: 22935614 a model by which N-terminal cleavage of RBX1 impairs its activity and promotes susceptibility to ER stress induction. PMID: 22822056 Structural and biochemical analyses reveal that GLMN adopts a HEAT-like repeat fold that tightly binds the E2-interacting surface of RBX1, inhibiting CRL-mediated chain formation by the E2 CDC34. PMID: 22748924 Numb regulates glioma stem cell fate and growth by altering epidermal growth factor receptor and Skp1-Cullin-F-box ubiquitin ligase activity PMID: 22553175 Glomulin binds Rbx1 and regulates cullin-1 RING ligase-mediated turnover of Fbw7. PMID: 22405651 the SCF complex (Skp1/Cul1/F-box protein/Roc1) intervenes in the surveillance of Cdh1 cellular abundance in S-phase PMID: 16123585 Results indicate that FBW5-DDB1-CUL4-ROC1 is an E3 ubiquitin ligase regulating TSC2 protein stability and TSC complex turnover. PMID: 18381890 Data show that REDD1 is subject to ubiquitin-mediated degradation mediated by the CUL4A-DDB1-ROC1-beta-TRCP E3 ligase complex and through the activity of glycogen synthase kinase 3beta. PMID: 19557001 KLHL20-Cul3-ROC1 is an E3 ligase for DAPK ubiquitination PMID: 20389280 A new conformation of RBX1 involved in the e2-to-substrate ubiquitin-like protein transfer is discussed. PMID: 21765416 ROC1 expression is negatively correlated with cyclin D1 expression, demonstrating its importance in the degradation of cyclin D1 in melanomas. PMID: 21300445 in human cancer cells, RBX1 silencing causes the accumulation of DNA replication licensing proteins CDT1 and ORC1, leading to DNA double-strand breaks, DDR, G(2) arrest, and, eventually, aneuploidy PMID: 21115485 Data show that CRN7 interacted with Cullin1 and Roc1 to form a novel SCF-like E3 complex. PMID: 21130766 Nrf2 regulates Cul3-Rbx1 by controlling regulation of expression and induction of Cul3-Rbx1 PMID: 20452971 The data suggest that RBX1 could potentially be developed into biomarkers of resistance to acyl sulfonamide-based cancer drugs. This will require clinical validation in a series of patients treated with R3200. PMID: 19723642 crystal structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF complex PMID: 11961546 findings report that HIV-1 Vif interacts with cellular proteins Cul5, elongins B and C, and Rbx1 to form an Skp1-cullin-F-box (SCF)-like complex PMID: 14564014 DET1 promotes ubiquitination and degradation of c-Jun by assembling a multisubunit ubiquitin ligase containing DNA Damage Binding Protein-1 (DDB1), cullin 4A (CUL4A), Regulator of Cullins-1 (ROC1), and constitutively photomorphogenic-1 PMID: 14739464 Keap1 negatively regulates Nrf2 function in part by targeting Nrf2 for ubiquitination by the CUL3-ROC1 ligase and subsequent degradation by the proteasome PMID: 15601839 This study uncovers CUL4-DDB-ROC1 as a histone ubiquitin ligase and demonstrate that histone H3 and H4 ubiquitylation participates in the cellular response to DNA damage. PMID: 16678110 ROC1 protein binds to the proinactive form of pro-caspase 3 and shortens the half life of the enzyme. PMID: 17217622 VprBP depletion abolished the in vivo interaction of Merlin and Roc1-Cullin4A-DDB1, which resulted in Merlin stabilization and inhibited ERK and Rac activation PMID: 18332868 CUL1 ECTD (extreme C-terminal domain; spanning the C-terminal 50 amino acids), did not contribute to CUL1's stable association with ROC1. PMID: 18723677 SCCRO recruits Ubc12 approximately NEDD8 to the CAND1-Cul1-ROC1 complex but that this is not sufficient to dissociate or overcome the inhibitory effects of CAND1 on cullin neddylation PMID: 18826954 ROC1 silencing triggers multiple death and growth arrest pathways to effectively suppress tumor cell growth, suggesting that ROC1 may serve as a potential anticancer target PMID: 19509229

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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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