SUMO3 Antibody

中文名稱：

SUMO3兔多克隆抗體
貨號：

CSB-PA05509A0Rb
規格：

￥440
圖片：
Immunohistochemistry of paraffin-embedded human ovarian cancer using CSB-PA05509A0Rb at dilution of 1:100

Immunofluorescent analysis of Hela cells using CSB-PA05509A0Rb at dilution of 1:100 and Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L)
其他：

產品詳情
產品評價
相關產品
靶點詳情

產品詳情

產品名稱：

Rabbit anti-Homo sapiens (Human) SUMO3 Polyclonal antibody
Uniprot No.：

P55854
基因名：

SUMO3
別名：

Small ubiquitin like modifier 3 antibody; Small ubiquitin related modifier 3 antibody; Small ubiquitin-related modifier 3 antibody; SMT3 homolog 1 antibody; SMT3 suppressor of mif two 3 homolog 1 antibody; SMT3 suppressor of mif two 3 homolog 3 antibody; SMT3, yeast, homolog 1 antibody; SMT3A antibody; Smt3B antibody; SMT3H1 antibody; SUMO-2 antibody; SUMO-3 antibody; sumo3 antibody; SUMO3_HUMAN antibody; Ubiquitin like protein SMT3A antibody; Ubiquitin-like protein SMT3B antibody
宿主：

Rabbit
反應種屬：

Human
免疫原：

Recombinant Human Small ubiquitin-related modifier 3 protein (1-92AA)
免疫原種屬：

Homo sapiens (Human)

標記方式：

Non-conjugated

本頁面中的產品，SUMO3 Antibody (CSB-PA05509A0Rb)，的標記方式是Non-conjugated。對于SUMO3 Antibody，我們還提供其他標記。見下表：

標記方式	貨號	產品名稱	應用
HRP	CSB-PA05509B0Rb	SUMO3 Antibody, HRP conjugated	ELISA
FITC	CSB-PA05509C0Rb	SUMO3 Antibody, FITC conjugated
Biotin	CSB-PA05509D0Rb	SUMO3 Antibody, Biotin conjugated	ELISA

克隆類型：

Polyclonal
抗體亞型：

IgG
純化方式：

>95%, Protein G purified
濃度：

It differs from different batches. Please contact us to confirm it.
保存緩沖液：

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
產品提供形式：

Liquid
應用范圍：

ELISA, IHC, IF

推薦稀釋比：

Application	Recommended Dilution
IHC	1:20-1:200
IF	1:50-1:200

Protocols：

ELISA Protocol
Immunohistochemistry (IHC) Protocol
Immunofluorescence (IF) Protocol
儲存條件：

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
貨期：

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
用途：

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

產品評價

靶點詳情

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.
基因功能參考文獻：
1. 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
2. SUMO3 abrogates PKR activation upon poly(I:C) transfection or viral infection. PMID: 29352251
3. The hSUMO3 was cleaved from hrVEGF-A121 with SUMO protease. PMID: 29943150
4. 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
5. findings demonstrate that SUMO2 and SUMO3 are specific and essential negative regulators of a noncanonical mechanism of IFN induction. PMID: 29891701
6. Increased protein level of HSP27 through SUMO2/3-mediated SUMOylation plays crucial roles in the progression of primary hepatocellular carcinoma. PMID: 28665748
7. Increased post-translational modification of proteins by SUMO-2/3 is a cytoprotective response against cell stress induced by ischaemia and reperfusion. PMID: 28747609
8. 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
9. The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1gamma sumoylation and poly-SUMO chain elongation. PMID: 27247387
10. FOXP2 can be modified with all three human SUMO proteins and that PIAS1 promotes this process. PMID: 26867680
11. Data indicate that small ubiquitin-like modifiers SUMO1, SUMO2, or SUMO3 were found in nuclear speckles. PMID: 26223657
12. 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
13. DBC1 modification by Small Ubiquitin-like Modifier 2/3 is crucial for p53 transactivation under genotoxic stress. PMID: 25406032
14. Expression of SUMO1/2/3 is dramatically enhanced by interferons through an miRNA-based mechanism involving the Lin28/let-7. PMID: 24942926
15. 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
16. 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
17. 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
18. In human cells, Ehrlichia chaffeensis TRP120 was selectively conjugated with SUMO2/3 isoforms. PMID: 25047847
19. SUMO-2/3 modification near protein-coding gene promoters occurs in order to maintain host immune-related gene unaltered during viral reactivation. PMID: 24267727
20. K-Rta degrades SUMO-2/3 and SUMO-2/3 modified proteins, including promyelocytic leukemia (PML) and K-bZIP. PMID: 23990779
21. Stress-induced phosphorylation of Thr486 in c-Myb by p38 mitogen-activated protein kinases attenuates conjugation of SUMO-2/3. PMID: 24257756
22. 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
23. Overexpression of SUMO-1 and 3 enhanced accumulation of viral DNA, which correlated with an increase in viral replication. PMID: 23407422
24. 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
25. 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
26. 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
27. SUMO3-conjugated IRF8 shows reduced mobility in live nuclei and binds poorly to the interleukin (IL)12p40 gene. PMID: 22942423
28. SUMO-2/3 conjugates accumulating under the heat shock or MG132 treatment result largely from new protein synthesis. PMID: 22306003
29. sumoylation of proteins during keratinocyte differentiation is a complex process which likely reflects and contributes to the biochemical changes that drive differentiation. PMID: 22291911
30. 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
31. 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
32. 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
33. The expression of SUMO2 and SUMO3 is regulated differently by reactive oxygen species. PMID: 21291420
34. SENP3-mediated de-conjugation of SUMO2/3 from promyelocytic leukemia is correlated with accelerated cell proliferation under mild oxidative stress. PMID: 20181954
35. 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
36. SUMO3 has a role in PIASy-enhanced modification of C-EPB alpha PMID: 12511558
37. SUMO-1 shows patterns of utilization that are clearly discrete from the patterns of SUMO-2 and -3 throughout the cell cycle PMID: 15456902
38. Dissimilarities between SUMO-3 and SUMO-1 in tertiary structure. PMID: 15723523
39. c-Fos/c-Jun AP-1 dimer activity is downregulated by SUMO-1, SUMO-2, and SUMO-3 PMID: 16055710
40. SMT3A expression was down-regulated in association with DNA synthesis induction after X-ray irradiation in basal cell nevus syndrome cells. PMID: 16154602
41. Results describe the crystal structure of the central region of thymine-DNA glycosylase conjugated to SUMO-3. PMID: 16626738
42. sumoylation has a role in keratinocyte differentiation PMID: 17164289
43. SUMOylation is a key regulator of the mammalian cell cycle, with SUMO-2/3 modification of different proteins regulating distinct processes. PMID: 18374647
44. SUMO-2/3 conjugation and the ubiquitin-proteasome system are tightly integrated and act in a cooperative manner. PMID: 18565875
45. SUMO-2/3, though expressed similarly to SUMO-1, may function separately and independently during pachytene in men. PMID: 18694876
46. BLM, the RecQ DNA helicase mutated in Bloom syndrome, is preferentially modified by SUMO-2/3 both in vitro and in vivo PMID: 18708356
47. the acidic stretch of the SIM of MCAF1 plays an important role in the binding to SUMO-3. PMID: 18842587
48. CTCF protein can be posttranslationally modified by the small ubiquitin-like protein SUMO. PMID: 19029252
49. 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
50. 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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亞細胞定位：

Cytoplasm. Nucleus. Nucleus, PML body.
蛋白家族：

Ubiquitin family, SUMO subfamily
組織特異性：

Expressed predominantly in liver.
數據庫鏈接：

HGNC: 11124

OMIM: 602231

KEGG: hsa:6612

STRING: 9606.ENSP00000330343

UniGene: Hs.474005

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