Recombinant Human Ruvb-Like 2 (RUVBL2) Protein (His-SUMO)

Name: Recombinant Human Ruvb-Like 2 (RUVBL2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-02402P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Ruvb-Like 2 (RUVBL2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9Y230
Target Symbol	RUVBL2
Synonyms	48 kDa TATA box-binding protein-interacting protein; 48 kDa TBP-interacting protein; 48-kDa TATA box-binding protein-interacting protein; 48-kDa TBP-interacting protein; 51 kDa erythrocyte cytosolic protein; CGI-46; EC=3.6.1.-; ECP-51; ECP51; Erythrocyte cytosolic protein; 51-KD; INO80 complex subunit J; INO80J; MGC144733; MGC144734; MGC52995; mp47; p47; p47 protein; Repressing pontin 52; Reptin 52; REPTIN; RuvB (E coli homolog)-like 2; RUVB; E. coli; homolog-like 2; RuvB-like 2 (E. coli); RuvB-like 2; RuvB-like protein 2; RUVB2; RUVB2_HUMAN; RUVBL2; RVB2; TAP54-beta; TATA box-binding protein-interacting protein; 48-KD; TBP-interacting protein; 48-KD; TIH2; TIP48; TIP49b; TIP60-associated protein 54-beta; wu:fi25f01; zreptin
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	ATVTATTKVPEIRDVTRIERIGAHSHIRGLGLDDALEPRQASQGMVGQLAARRAAGVVLEMIREGKIAGRAVLIAGQPGTGKTAIAMGMAQALGPDTPFTAIAGSEIFSLEMSKTEALTQAFRRSIGVRIKEETEIIEGEVVEIQIDRPATGTGSKVGKLTLKTTEMETIYDLGTKMIESLTKDKVQAGDVITIDKATGKISKLGRSFTRARDYDAMGSQTKFVQCPDGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDEVHMLDIESFSFLNRALESDMAPVLIMATNRGITRIRGTSYQSPHGIPIDLLDRLLIVSTTPYSEKDTKQILRIRCEEEDVEMSEDAYTVLTRIGLETSLRYAIQLITAASLVCRKRKGTEVQVDDIKRVYSLFLDESRSTQYMKEYQDAFLFNELKGETMDTS
Expression Range	2-463aa
Protein Length	Full Length of Mature Protein
Mol. Weight	67.0kDa
Research Area	Epigenetics And Nuclear Signaling
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	Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome -DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome. Proposed core component of the chromatin remodeling INO80 complex which exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding. Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. May also inhibit the transcriptional activity of ATF2. Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes. May play a role in regulating the composition of the U5 snRNP complex.
Subcellular Location	Nucleus matrix. Nucleus, nucleoplasm. Cytoplasm. Membrane. Dynein axonemal particle. Note=Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol. Although it is also present in the cytoplasm and associated with the cell membranes.
Protein Families	RuvB family
Database References	HGNC: 10475 OMIM: 604788 KEGG: hsa:10856 STRING: 9606.ENSP00000473172 UniGene: PMID: 28561026 Mep1A is overexpressed in most hepatocellular carcinomas and induces tumor cell migration and invasion. Mep1A expression is regulated by Reptin, and Mep1A mediates Reptin-induced migration. PMID: 27999200 Reptin silencing did not affect the tyrosine phosphorylation of the insulin receptor nor of IRS1, but it enhanced the tyrosine phosphorylation of the p85 subunit of PI3K. PMID: 28833338 Overall, POLG interactome mapping identifies novel proteins which support mitochondrial biogenesis and a potential novel mitochondrial isoform of Ruvbl2. PMID: 27845271 The authors report that HIV-1 exploits the host factor RuvB-like 2 (RVB2) to balance relative expression of Gag and Env for efficient production of infectious virions. PMID: 26211835 by means of molecular docking approaches we first modeled the structures of hetero-hexameric TIP49 ( TIP49a and TIP49b )complexes with short ds-DNA fragments (20 base pairs with different GC content) within the central channel of hexameric ring PMID: 26863765 Data suggest that overexpression of Reptin in hepatocellular carcinoma (HCC) could be a factor of resistance to treatment. PMID: 25875766 RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils. PMID: 26303906 results reveal a novel mechanism for the control of NF-kappaB pathway by cytoplasmic Reptin PMID: 25957047 The results suggests that a potential mechanism for the role of RuvBL1-RuvBL2 in maintaining genome integrity is through controlling the cellular abundance of Fanconi anaemia core complex. PMID: 25428364 Reptin and Pontin oligomerization and activity are modulated through histone H3 N-terminal tail interaction. PMID: 25336637 these findings suggest that YY1-RuvBL1-RuvBL2 complexes could contribute to functions beyond transcription, and we show that YY1 and the ATPase activity of RuvBL2 are required for RAD51 foci formation during homologous recombination. PMID: 24990942 The Reptin is unable to bind with membrane-associated APPL proteins. PMID: 23891720 Anti-RuvBL1/2 antibody is a novel systemic scleroderma-related autoantibody associated with a unique combination of clinical features, including myositis overlap and diffuse cutaneous involvement. PMID: 24023044 Data suggest that reptin may prove to be a valuable target for prevention and treatment of renal cell carcinoma. PMID: 22341977 Data indicate that the RVB1/2 chromatin-remodeling complex is required for efficient Pol II recruitment and initiation at IFN-alpha-stimulated genes (ISGs) promoters and is recruited through interaction with the STAT2 transactivation domain. PMID: 23878400 We demonstrate that leukemogenic activity of MLL-AF9 requires RUVBL2 (RuvB-like 2), an AAA+ ATPase family member that functions in a wide range of cellular processes, including chromatin remodeling and transcriptional regulation. PMID: 23403462 Two coexisting conformations, compact and stretched, are revealed by analysis of cryo-electron microscopy structures of the RuvBL1-RuvBL2 complex. PMID: 23002137 The hexameric crystal structure of TIP49b confirms the validity of molecular models. PMID: 22748767 First insight into the mechanism of action of pontin and reptin in the assembly of macromolecular complexes. PMID: 22923768 Ectopic expression of RUVBL2 decreases the levels of ARF, whereas knockdown of RUVBL2 results in a marked increase in ARF levels. In addition, RUVBL2 down-regulates the levels of p53 in an ARF-dependent manner. PMID: 22285491 truncation of domain II led to a substantial increase in ATP consumption of RuvBL1, RuvBL2 and their complex. In addition, we present evidence that DNA unwinding of the human RuvBL proteins can be auto-inhibited by domain II PMID: 21933716 data firmly implicate RuvBl2 in Ets2 mediated regulation of hTERT in colon cancer which has functional and clinical consequences PMID: 21763315 RUVBL1 and RUVBL2 control the abundance of Phosphatidylinositol 3-kinase (PI3K)-related protein kinases (PIKKs), and stimulate the formation of PIKK-containing molecular complexes, such as those involved in nonsense-mediated mRNA decay. PMID: 20371770 In vivo Reptin depletion leads to tumor growth arrest and may prove a valuable target in hepatocellular carcinoma. PMID: 20346530 hTERT transcription requires constitutive expression of Reptin and its cooperation with c-MYC PMID: 20509972 Reptin, a chromatin-remodeling factor, is methylated at lysine 67 in hypoxic conditions by the methyltransferase G9a. PMID: 20603076 TIP49b hexamers were found to be inactive for ATP hydrolysis and DNA unwinding, suggesting that, in cells, protein factors that remain unknown might be required to recycle these into an active form. PMID: 20553504 Several experimental approaches were used to investigate the molecular architecture of the RuvBL1-RuvBL2 complex and the role of the ATPase-insert domain (domain II) for its assembly and stability. PMID: 20412048 The relocation of endogenous TIP48 to the midzone/midbody under physiological conditions suggests a novel and distinct function for TIP48 in mitosis and possible involvement in the exit of mitosis. PMID: 16157330 similar to the yeast INO80 complex, the hINO80 complex of Tip49a and Tip49b exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding PMID: 16230350 sumoylation status of reptin modulates the invasive activity of cancer cells with metastatic potential PMID: 16699503 The results point to biochemical differences between TIP48 and TIP49, which may explain the structural differences between the two hexameric rings and could be significant for specialised functions that the proteins perform individually. PMID: 17157868 RUVBL2 is overexpressed in a large majority of HCCs. RUVBL2 overexpression enhances tumorigenicity, and RUVBL2 is required for tumor cell viability. These results argue for a major role of RUVBL2 in liver carcinogenesis. PMID: 17657734 Study identifies the ATPases pontin and reptin as telomerase components through affinity purification of TERT from human cells. PMID: 18358808 Crystal structure has been solved and the solutions obtained show that the RuvBL1-RuvBL2 complex forms a dodecamer. PMID: 18765919 RPAP3 interacts with Reptin to modulate UV-induced DNA damage by regulating H2AX phosphorylation PMID: 19180575 RBL2 inhibits influenza virus replication by suppressing influenza A virus polymerases. PMID: 19369355 In human embryonic stem cells the Reptin52 expression increase in cell nuclei during cell differentiation. PMID: 19444951 RVB1 and RVB2 function within multiple protein complexes is reviewed. PMID: 19524533 Reptin and Pontin protein levels are strictly controlled by a posttranslational mechanism involving proteasomal degradation of newly synthesized proteins. PMID: 19877184

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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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