Recombinant Human Small ubiquitin-related modifier 3 (SUMO3)
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中文名称:人SUMO3重组蛋白
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货号:CSB-YP022951HU
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规格:
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来源:Yeast
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其他:
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中文名称:人SUMO3重组蛋白
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货号:CSB-EP022951HU
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规格:
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来源:E.coli
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其他:
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中文名称:人SUMO3重组蛋白
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货号:CSB-EP022951HU-B
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规格:
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来源:E.coli
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共轭:Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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其他:
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中文名称:人SUMO3重组蛋白
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货号:CSB-BP022951HU
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规格:
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来源:Baculovirus
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其他:
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中文名称:人SUMO3重组蛋白
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货号:CSB-MP022951HU
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规格:
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来源:Mammalian cell
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其他:
产品详情
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纯度:>85% (SDS-PAGE)
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基因名:SUMO3
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Uniprot No.:
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别名:Small ubiquitin like modifier 3; Small ubiquitin related modifier 3; Small ubiquitin-related modifier 3; SMT3 homolog 1; SMT3 suppressor of mif two 3 homolog 1; SMT3 suppressor of mif two 3 homolog 3; SMT3, yeast, homolog 1; SMT3A; Smt3B; SMT3H1; SUMO-2; SUMO-3; sumo3; SUMO3_HUMAN; Ubiquitin like protein SMT3A; Ubiquitin-like protein SMT3B
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种属:Homo sapiens (Human)
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蛋白长度:Full length protein
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表达区域:1-92
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氨基酸序列MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR FDGQPINETD TPAQLEMEDE DTIDVFQQQT GG
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蛋白标签:Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially. -
产品提供形式:Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand. -
复溶:We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
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储存条件:Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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保质期:The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C. -
货期:Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
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注意事项:Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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Datasheet :Please contact us to get it.
相关产品
靶点详情
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功能:Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. Plays a role in the regulation of sumoylation status of SETX.
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基因功能参考文献:
- Data suggest that ATF5 is modified by SUMO2/3 at a conserved SUMO-targeting consensus site; this SUMOylation of ATF5 appears to be required for transport of ATF5 to centrosome. (ATF5 = activating transcription factor-5; SUMO = small ubiquitin-like modifier) PMID: 29326161
- SUMO3 abrogates PKR activation upon poly(I:C) transfection or viral infection. PMID: 29352251
- The hSUMO3 was cleaved from hrVEGF-A121 with SUMO protease. PMID: 29943150
- conclude that SUMO3-tagged hBMP2 is more suited for generation of soluble form of the protein and addition of SUMO3 tag does not affect the functional activity of hBMP2 PMID: 29574511
- findings demonstrate that SUMO2 and SUMO3 are specific and essential negative regulators of a noncanonical mechanism of IFN induction. PMID: 29891701
- Increased protein level of HSP27 through SUMO2/3-mediated SUMOylation plays crucial roles in the progression of primary hepatocellular carcinoma. PMID: 28665748
- Increased post-translational modification of proteins by SUMO-2/3 is a cytoprotective response against cell stress induced by ischaemia and reperfusion. PMID: 28747609
- Data suggest that PIASy exhibits a SIM (SUMO-interacting motif) in addition to the SIM identified in homologous proteins in other species; both SIMs are located near C terminus of PIASy, and both are required for full ligase activity of PIASy; hydrophobic core residues of the new SIM are essential in binding to SUMO-3. (PIASy = protein inhibitors of activated STAT y; SUMO-3 = small ubiquitin-like modifier 3) PMID: 28455449
- The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1gamma sumoylation and poly-SUMO chain elongation. PMID: 27247387
- FOXP2 can be modified with all three human SUMO proteins and that PIAS1 promotes this process. PMID: 26867680
- Data indicate that small ubiquitin-like modifiers SUMO1, SUMO2, or SUMO3 were found in nuclear speckles. PMID: 26223657
- Adenovirus E4-ORF3 targets PIAS3 and together with E1B-55K remodels SUMO2/SUMO3 Interactions in the nucleus and at virus genome replication domains. PMID: 26223632
- DBC1 modification by Small Ubiquitin-like Modifier 2/3 is crucial for p53 transactivation under genotoxic stress. PMID: 25406032
- Expression of SUMO1/2/3 is dramatically enhanced by interferons through an miRNA-based mechanism involving the Lin28/let-7. PMID: 24942926
- PHD3 SUMOylation occurs at a cluster of four lysines at the C-terminal end of the protein. Furthermore, PHD3 SUMOylation by SUMO2 or SUMO3 contributes to PHD3-mediated repression of HIF1-dependent transcriptional activity. PMID: 25380826
- The interactions of SLX4 with SUMO and ubiquitin increase its affinity for factors recognizing different DNA lesions or telomeres, helping to direct the SLX4 complex in distinct functional contexts. PMID: 25533185
- These findings demonstrated a role for the human adenovirus E4-ORF3 protein as a regulator of ubiquitin-like modifications and revealed new SUMO3 substrates induced by E4-ORF3. PMID: 25410875
- In human cells, Ehrlichia chaffeensis TRP120 was selectively conjugated with SUMO2/3 isoforms. PMID: 25047847
- SUMO-2/3 modification near protein-coding gene promoters occurs in order to maintain host immune-related gene unaltered during viral reactivation. PMID: 24267727
- K-Rta degrades SUMO-2/3 and SUMO-2/3 modified proteins, including promyelocytic leukemia (PML) and K-bZIP. PMID: 23990779
- Stress-induced phosphorylation of Thr486 in c-Myb by p38 mitogen-activated protein kinases attenuates conjugation of SUMO-2/3. PMID: 24257756
- We show that human RNF111/Arkadia is a new sumo targeted ligase, which used three adjacent sumo acting motifs for specific recognition of poly-SUMO2/3 chains. PMID: 23751493
- Overexpression of SUMO-1 and 3 enhanced accumulation of viral DNA, which correlated with an increase in viral replication. PMID: 23407422
- Only two missense variants were identified, both within SUMO3, however, these were both present in multiple affected individuals and a similar number of controls. PMID: 22492558
- Data suggest that SUMO1 and SUMO2/3 are highly enriched in neck area of sperm; SUMOs are also associated with redundant nuclear envelope, flagella, and some sperm head regions. PMID: 23077236
- findings show levels of SUMO1- and SUMO2/3-conjugated proteins are elevated in astrocytic tumors; findings highlight the pivotal role of SUMO conjugation in DNA damage repair processes PMID: 23078246
- SUMO3-conjugated IRF8 shows reduced mobility in live nuclei and binds poorly to the interleukin (IL)12p40 gene. PMID: 22942423
- SUMO-2/3 conjugates accumulating under the heat shock or MG132 treatment result largely from new protein synthesis. PMID: 22306003
- sumoylation of proteins during keratinocyte differentiation is a complex process which likely reflects and contributes to the biochemical changes that drive differentiation. PMID: 22291911
- The 15q24 microdeletion may thus represent the first genetic hit to initiate leukaemogenesis and implicates PML and SUMO3 as novel components of the leukaemogenic network in TMD/AMKL. PMID: 22296450
- Conjugation of SUMO-2/3 to p53 correlates with a reduction of both activation and repression of a subset of p53-target genes. PMID: 21900752
- Loop 1 insertion in SENP6 and SENP7 as a platform to discriminate between SUMO1 and SUMO2/3 isoforms in this subclass of the SUMO protease family. PMID: 21878624
- The expression of SUMO2 and SUMO3 is regulated differently by reactive oxygen species. PMID: 21291420
- SENP3-mediated de-conjugation of SUMO2/3 from promyelocytic leukemia is correlated with accelerated cell proliferation under mild oxidative stress. PMID: 20181954
- these findings suggest an expanded role of p150 as a SUMO2/3-interacting factor, and raise the intriguing possibility that p150 plays a role in promoting delivery of SUMO2/3 or SUMO2/3-modified proteins (or both) on chromatin fibers during replication. PMID: 19919826
- SUMO3 has a role in PIASy-enhanced modification of C-EPB alpha PMID: 12511558
- SUMO-1 shows patterns of utilization that are clearly discrete from the patterns of SUMO-2 and -3 throughout the cell cycle PMID: 15456902
- Dissimilarities between SUMO-3 and SUMO-1 in tertiary structure. PMID: 15723523
- c-Fos/c-Jun AP-1 dimer activity is downregulated by SUMO-1, SUMO-2, and SUMO-3 PMID: 16055710
- SMT3A expression was down-regulated in association with DNA synthesis induction after X-ray irradiation in basal cell nevus syndrome cells. PMID: 16154602
- Results describe the crystal structure of the central region of thymine-DNA glycosylase conjugated to SUMO-3. PMID: 16626738
- sumoylation has a role in keratinocyte differentiation PMID: 17164289
- SUMOylation is a key regulator of the mammalian cell cycle, with SUMO-2/3 modification of different proteins regulating distinct processes. PMID: 18374647
- SUMO-2/3 conjugation and the ubiquitin-proteasome system are tightly integrated and act in a cooperative manner. PMID: 18565875
- SUMO-2/3, though expressed similarly to SUMO-1, may function separately and independently during pachytene in men. PMID: 18694876
- BLM, the RecQ DNA helicase mutated in Bloom syndrome, is preferentially modified by SUMO-2/3 both in vitro and in vivo PMID: 18708356
- the acidic stretch of the SIM of MCAF1 plays an important role in the binding to SUMO-3. PMID: 18842587
- CTCF protein can be posttranslationally modified by the small ubiquitin-like protein SUMO. PMID: 19029252
- HSP27-induced HSF1 modification by SUMO-2/3 takes place downstream of the transcription factor phosphorylation on S303 and S307 and does not affect its DNA-binding ability PMID: 19597476
- Results show that nuclear actin is modified by SUMO2 and SUMO3 and that computational modeling and site-directed mutagenesis identified K68 and K284 as critical sites for SUMOylating actin. PMID: 19635839
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亚细胞定位:Cytoplasm. Nucleus. Nucleus, PML body.
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蛋白家族:Ubiquitin family, SUMO subfamily
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组织特异性:Expressed predominantly in liver.
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数据库链接:
HGNC: 11124
OMIM: 602231
KEGG: hsa:6612
STRING: 9606.ENSP00000330343
UniGene: Hs.474005
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