SUMO1 Recombinant Monoclonal Antibody

說明書

中文名稱：

SUMO1重組抗體
貨號：

CSB-RA022948A0HU
規格：

￥1320
圖片：
IHC image of CSB-RA022948A0HU diluted at 1:92.5 and staining in paraffin-embedded human adrenal gland tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4℃ overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

IHC image of CSB-RA022948A0HU diluted at 1:92.5 and staining in paraffin-embedded human liver cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4℃ overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

Immunoprecipitating SUMO1 in 293T whole cell lysate
Lane 1: Rabbit control IgG instead of CSB-RA022948A0HU in 293T whole cell lysate. For western blotting, a HRP-conjugated Protein G antibody was used as the secondary antibody (1/2000)
Lane 2: CSB-RA022948A0HU (3μg) + 293T whole cell lysate (500μg)
Lane 3: 293T whole cell lysate (20μg)

Overlay histogram showing Hela cells stained with CSB-RA022948A0HU (red line) at 1:50. The cells were fixed with 70% Ethylalcohol (18h) and then permeabilized with 0.3% Triton X-100 for 2 min. The cells were then incubated in 1x PBS /10% normal goat serum to block non-specific protein-protein interactions followed by primary antibody for 1 h at 4℃. The secondary antibody used was FITC goat anti-rabbit IgG (H+L) at 1/200 dilution for 1 h at 4℃. Control antibody (green line) was used under the same conditions. Acquisition of >10,000 events was performed.
其他：

產品詳情
產品評價
相關產品
靶點詳情

產品詳情

產品描述：

SUMO1 Recombinant Monoclonal Antibody（CSB-RA022948A0HU）是針對小泛素相關修飾蛋白1（SUMO1）開發的高特異性抗體，適用于研究蛋白質SUMO化修飾及其功能調控機制。SUMO1是類泛素蛋白家族成員之一，通過共價結合靶蛋白參與翻譯后修飾，廣泛調控蛋白質亞細胞定位、相互作用網絡及穩定性，在細胞周期調控、DNA損傷修復和轉錄調節等生物學過程中發揮重要作用。本抗體經多種平臺驗證，可特異性識別天然及重組SUMO1蛋白，適用于ELISA、免疫組化（IHC，推薦稀釋1:50-1:200）、流式細胞術（FC）和免疫沉淀（IP，推薦稀釋1:200-1:1000）等實驗，在不同樣本類型中展現出優異的重復性和批次間一致性。其重組單克隆特性確保了低交叉反應性和高親和力，適用于探究SUMO1在細胞應激反應、信號轉導異常或疾病相關蛋白質修飾中的作用，特別是在腫瘤發生、神經退行性疾病模型中研究SUMO化動態調控機制，為蛋白質相互作用及翻譯后修飾研究提供可靠工具。
Uniprot No.：

P63165
基因名：

SUMO1
別名：

DAP1 antibody; GAP modifying protein 1 antibody; GAP-modifying protein 1 antibody; GMP 1 antibody; GMP1 antibody; OFC10 antibody; PIC 1 antibody; PIC1 antibody; SENP2 antibody; Sentrin 1 antibody; Sentrin antibody; Small ubiquitin related modifier 1 antibody; Small ubiquitin-like modifier 1 antibody; Small ubiquitin-related modifier 1 antibody; SMT3 antibody; SMT3 homolog 3 antibody; SMT3 suppressor of mif two 3 homolog 1 antibody; SMT3, yeast, homolog 3 antibody; Smt3C antibody; SMT3H3 antibody; SUMO-1 antibody; SUMO1 antibody; SUMO1_HUMAN antibody; Ubiquitin homology domain protein PIC1 antibody; Ubiquitin Like 1 antibody; Ubiquitin like protein SMT3C antibody; Ubiquitin like protein UBL1 antibody; Ubiquitin-homology domain protein PIC1 antibody; Ubiquitin-like protein SMT3C antibody; Ubiquitin-like protein UBL1 antibody; UBL 1 antibody; UBL1 antibody
反應種屬：

Human
免疫原：

A synthesized peptide derived from human SUMO1
免疫原種屬：

Homo sapiens (Human)
標記方式：

Non-conjugated
克隆類型：

Monoclonal
抗體亞型：

Rabbit IgG
純化方式：

Affinity-chromatography
克隆號：

5G3
濃度：

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

Rabbit IgG in 10mM phosphate buffered saline , pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.
產品提供形式：

Liquid
應用范圍：

ELISA, IHC, FC, IP

推薦稀釋比：

Application	Recommended Dilution
IHC	1:50-1:200
IP	1:200-1:1000

Protocols：

ELISA Protocol
Immunohistochemistry (IHC) Protocol
Flow cytometry (FC) Protocol
Immunoprecipitation (IP) 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 that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3.
基因功能參考文獻：
1. SUMO1 expression results in a gain of PKR activity by increasing its activation. SUMO1 was able to activate PKR and eIF-2alpha in the absence of viral infection. PMID: 29352251
2. SPOP inhibits hepatocellular carcinoma (HCC) cell metastasis via ubiquitin-dependent SUMO1/SENP7 proteolysis and may thus serve as a new opinion for the prevention of HCC metastasis. PMID: 29777712
3. Study found a significant difference in the expression of Cx43 and SUMO1 between cancer stem cells and non-cancer stem cells in liver cancer. By the co-expression of Cx43 and SUMO1 in cancer stem cells, the gap junction intercellular communication of liver cancer stem cells was obviously improved. PMID: 29393359
4. Two SUMO modification sites existed in dopamine receptor D1, the phosphorylation of which, due to SUMO modification, can interact with PP2A, leading to the inhibition of D1 de-phosphorylation and normal function. PMID: 28770955
5. These results suggest that SUMO1 contributes to hepatocellular carcinoma progression by promoting p65 nuclear translocation PMID: 26993772
6. In summary, our study revealed a negative regulation of the UPR transducer ATF6 through post-translational SUMOylation. The information from this study will not only increase our understanding of the fine-tuning regulation of the UPR signaling but will also be informative to the modulation of the UPR for therapeutic benefits. PMID: 29061306
7. Molecular dynamics simulations showed that binding of the beta-grasp domain of SUMO1 induces significant conformational and dynamic changes in SENP1, including widening of the exosite cleft and quenching of nanosecond dynamics in all but a distal region. PMID: 27576863
8. Mutational analysis of functional sites showed that both peroxidase and PLA2 active sites were necessary for mutant Prdx6 function, and that Prdx6 phosphorylation (at T177 residue) was essential for optimum PLA2 activity.Mutant Prdx6 at its Sumo1 sites escapes and abates this adverse process by maintaining its integrity and gaining function PMID: 28055018
9. SUMO and p21Cip1 regulate the transit of proteins through the nucleolus; disruption of nucleolar export by DNA damage induces SUMO and p21Cip1 to act as hub proteins to form a multiprotein complex in the nucleolus. PMID: 28582471
10. This study reveals an essential role of SUMOylated FADD in Drp1- and caspase-10-dependent necrosis. PMID: 27799292
11. SUMO-1 gene silencing inhibits proliferation and promotes apoptosis of human gastric cancer cells. PMID: 28222440
12. the critical role of Cys52 in maintaining SUMO-1 conformation and function PMID: 27195426
13. Findings suggest SUMO-1 protein and PGE2 receptor subtype 4 (EP4) as two potential targets for new therapeutic or prevention strategies for endometrial cancers. PMID: 27230680
14. This study demonstrated that the rs12472035 polymorphism of SUMO1 was significantly associated with an increased risk of AD in male group. PMID: 27084229
15. FOXP2 can be modified with all three human SUMO proteins and that PIAS1 promotes this process. PMID: 26867680
16. Ang II-induced upregulation of ATF3 and SUMO1 in vitro and in vivo was blocked by Ang II type I receptor antagonist olmesartan. Moreover, Ang II induced ATF3 SUMOylation at lysine 42, which is SUMO1 dependent. PMID: 26850942
17. Data show that mutation of key residues in the binding site abolishes binding and that small ubiquitin-like modifier 1 (SUMO1) can simultaneously and non-cooperatively bind both the ZZ domain and a canonical SIM motif of CREB-binding protein (CBP/p300). PMID: 27129204
18. Roles for SUMO in pre-mRNA processing PMID: 26563097
19. SUMOylation at specific sites on PXR protein are involved in enhancement of transcription function of this receptor. PMID: 26549688
20. High DAP1 expression is associated with a 4-fold increase in the risk of lymph node metastases in squamous cell carcinoma of the oral cavity. PMID: 26400283
21. Knockdown of SUMO1 using specific siRNA influenced the accumulation of lipid droplets and reduced HCV replication. PMID: 26449956
22. The LKB1 K178R SUMO mutant had defective AMPK signaling and mitochondrial function, inducing death in energy-deprived cells. PMID: 26212320
23. Data suggest that small ubiquitin-related modifier protein SUMO1 modification of the promyelocytic leukemia protein (PML) RING domain promotes SUMO2 conjugation to Lys160. PMID: 26060329
24. Data identify PDGFRbeta as the hub gene in both inflammatory (IBC) and non-inflammatory breast neoplasm (non-IBC) and SUMO1 and COL1A1 the respective key genes for IBC and non-IBC suggesting they might play important role in the pathogenesis of the neoplasm. PMID: 26403314
25. PML IV/ARF interaction enhances p53 SUMO-1 conjugation, activation, and senescence. PMID: 26578773
26. Data indicate that small ubiquitin-like modifiers SUMO1, SUMO2, or SUMO3 were found in nuclear speckles. PMID: 26223657
27. These results confirm that the SUMO machinery is involved in TRIM5alpha-mediated retroviral restriction, and demonstrate that TRIM5alpha is a SUMO 1 and SUMO 2 substrate. PMID: 25880753
28. Under cell-free in vitro conditions, p35 is covalently modified by SUMO1. Sumoylation is a likely candidate mechanism for the rapid modulation of p35/Cdk5 activity in physiological situations as well as in disease. PMID: 25391294
29. SUMO1 modification stabilizes CDK6 protein and drives the cell cycle and glioblastoma progression. PMID: 24953629
30. SUMO1 accelerates the accumulation of autophagic vacuoles and promotes Abeta production. PMID: 25484073
31. Expression of SUMO1/2/3 is dramatically enhanced by interferons through an miRNA-based mechanism involving the Lin28/let-7. PMID: 24942926
32. SUMO-1 modification may affect the transcriptional activity of EGFR PMID: 26244656
33. The crystal structures of SUMO1 bound to unphosphorylated and tetraphosphorylated PML-SUMO-interacting motifs peptides indicate that three phosphoserines directly contact specific positively charged residues of SUMO1. PMID: 25497731
34. The expression of SUMO-1 in OLP was similar to normal mucosa and inflammatory fibrous hyperplasia, suggesting that alterations of this protein occur at later stages of carcinogenesis PMID: 23350884
35. reveals an unexpected role of SUMO-1 and SAFB in the stimulatory coupling of promoter binding, transcription initiation and RNA processing PMID: 25800734
36. MDM2 and SUMO-1 proteins are up-regulated in actinic cheilitis and lip cancer. PMID: 25241153
37. Identify DRP1, RanGAP1 and topoisomerase IIa as targets of SUMO1 in human ejaculated sperm, giving more insights on the role of SUMO1-ylation in sperm morphology and motility. PMID: 25118297
38. findings provide empirical evidence that SUMO1 genetic polymorphisms might be strongly involved in the etiology of NSCL/P, especially for rs12470401 T>C, rs16838917 A>G, rs12470529 A>G, and rs7572505 A>G polymorphisms. PMID: 25111678
39. Overexpression of SUMO-1 decreased phosphorylated GSK-3beta at Ser-9. Mutagenesis of tau at K340R or inhibition of tau SUMOylation by ginkgolic acid abolishes the effect of SUMO-1. PMID: 25378699
40. The mutation of the sumoylation site (Lys137) of PTBP2 markedly inhibited its modification by SUMO1. PMID: 24286314
41. SUMO potentiates the inhibition of protein synthesis induced by PKR in response to dsRNA. PMID: 25074923
42. These results show that DAP1 is a key regulator, of the induction of apoptosis and reduction of autophagy by subtilase cytotoxin (SubAB). PMID: 25183729
43. identified 295 SUMO1 and 167 SUMO2 sites on endogenous substrates of HeLa cells PMID: 25114211
44. Modification of TDG by small ubiquitin-like modifier (SUMO) proteins weakens its binding to abasic DNA. PMID: 24753249
45. SUMO-1 modification of RARA is a potent mechanism for balancing proliferation and differentiation by controlling the stability of RARA in cancer cells. PMID: 24819975
46. SUMO1P3 was significantly up-regulated in gastric cancer tissues. PMID: 23996296
47. SUMO chain-induced dimerization activates RNF4. PMID: 24656128
48. The mitosis-dependent dynamic SUMO-1 modification of NuMA might contribute to NuMA-mediated formation and maintenance of mitotic spindle poles during mitosis. PMID: 24309115
49. PIASxalpha is a novel SUMO E3 ligase for PTEN, and it positively regulates PTEN protein level in tumor suppression. PMID: 24344134
50. SUMO participates in transcriptional repression as both a covalent modification and through non-covalent interactions with E2 and E3 enzymes. PMID: 24174529
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相關疾?。?/div>
Non-syndromic orofacial cleft 10 (OFC10)
亞細胞定位：

Nucleus membrane. Nucleus speckle. Cytoplasm. Nucleus, PML body. Cell membrane. Nucleus.
蛋白家族：

Ubiquitin family, SUMO subfamily
數據庫鏈接：

HGNC: 12502

OMIM: 601912

KEGG: hsa:7341

STRING: 9606.ENSP00000376076

UniGene: Hs.81424

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