SPOP Antibody, Biotin conjugated

說明書

中文名稱：

SPOP兔多克隆抗體, Biotin偶聯(lián)
貨號：

CSB-PA022601LD01HU
規(guī)格：

￥880
其他：

產(chǎn)品詳情
產(chǎn)品評價
相關(guān)產(chǎn)品
靶點(diǎn)詳情

產(chǎn)品詳情

產(chǎn)品名稱：

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

O43791
基因名：

SPOP
別名：

BTBD32 antibody; HIB homolog 1 antibody; Roadkill homolog 1 antibody; Speckle type POZ protein antibody; Speckle-type POZ protein antibody; SPOP antibody; SPOP_HUMAN antibody; TEF 2 antibody; TEF2 antibody
宿主：

Rabbit
反應(yīng)種屬：

Human
免疫原：

Recombinant Human Speckle-type POZ protein (48-374AA)
免疫原種屬：

Homo sapiens (Human)
標(biāo)記方式：

Biotin
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(chǎn)品提供形式：

Liquid
應(yīng)用范圍：

ELISA
Protocols：

ELISA 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(chǎn)品評價

靶點(diǎn)詳情

功能：

Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. In complex with CUL3, involved in ubiquitination and proteasomal degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with CUL3, involved in ubiquitination of MACROH2A1 and BMI1; this does not lead to their proteasomal degradation. Inhibits transcriptional activation of PDX1/IPF1 targets, such as insulin, by promoting PDX1/IPF1 degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOP has higher ubiquitin ligase activity than the complex that contains the heterodimer formed by SPOP and SPOPL. Involved in the regulation of bromodomain and extra-terminal motif (BET) proteins BRD2, BRD3, BRD4 stability.
基因功能參考文獻(xiàn)：
1. SPOP inhibits hepatocellular carcinoma (HCC) cell metastasis via ubiquitin-dependent SENP7 proteolysis and may thus serve as a new opinion for the prevention of HCC metastasis. PMID: 29777712
2. Our result suggests that SPOP expression in blood might have a sensitivity that is low for routine diagnostic use and for screening for Renal cell carcinoma (RCC). However, SPOP could be a potential tissue diagnostic biomarker in RCC. PMID: 30197334
3. Expression of the F133V mutation and wild-type SPOP was at much lower levels compared to that of F102C and Y87N mutations; however, at present, it is unknown if this also affects the biological activity of the SPOP protein. PMID: 28810879
4. PD-L1 protein abundance is regulated by cyclin D-CDK4 and the cullin 3-SPOP E3 ligase via proteasome-mediated degradation PMID: 29160310
5. methylation status of SPOP promoter can be used as a novel epigenetic biomarker and a therapeutic target in colorectal cancer. PMID: 28032859
6. these data highlight SPOP as an important regulator of luminal epithelial cell proliferation and c-MYC expression in prostate physiology, identify c-MYC as a novel bona fide SPOP substrate, and help explain the frequent inactivation of SPOP in human prostate adenocarcinoma. PMID: 28414305
7. Results elucidate the tumor-suppressor role of SPOP in prostate cancer in which it acts as a negative regulator of BET protein stability and also provide a molecular mechanism for resistance to BET inhibitors in individuals with prostate cancer bearing SPOP mutations. PMID: 28805820
8. SPOP mutation in endometrial cancer increased degradation of BRD2, BRD3 and BRD4 proteins. SPOP mutation in prostate cancer increased expression of BRD2, BRD3 and BRD4 proteins. PMID: 28805821
9. Prostate cancer-derived SPOP mutants failed to interact with Cdc20 to promote its degradation. As a result, SPOP-deficient prostate cancer cells with elevated Cdc20 expression became resistant to a pharmacological Cdc20 inhibitor. PMID: 27780719
10. While wild-type SPOP localizes to liquid nuclear speckles, self-association-deficient SPOP mutants have a diffuse distribution in the nucleus. SPOP oligomerizes through its BTB and BACK domains. PMID: 27220849
11. SPOP mutation activates both PI3K/mTOR and androgen receptor signaling, effectively uncoupling the normal negative feedback between these two pathways. PMID: 28292441
12. The levels of SPOP significantly decreased, while the levels of SIRT2 significantly increased in non-small cell lung cancer (NSCLC) cell lines, compared to normal bronchial epithelial cell line and NSCLC specimens, compared to the paired non-tumor lung tissue. PMID: 28073696
13. hese findings reveal novel molecular events underlying the regulation of INF2 function and localization, and provided insights in understanding the relationship between SPOP mutations and dysregulation of mitochondrial dynamics in prostate cancer. PMID: 28448495
14. Results show that SPOP is highly expressed in clear cell renal cell carcinoma (RCC) and associated with disease progression. In vitro, SPOP promotes the invasiveness of RCC. PMID: 27572476
15. Data indicate that a mutation in the SPOP gene may not be associated with breast cancer, particularly in Chinese women. PMID: 26505385
16. SPOP acts as a tumor suppressor by promoting senescence through degrading SENP7. PMID: 26527005
17. our findings emphasize the critical role of SPOP in the regulation of proliferation and migration in liver cancer PMID: 26156804
18. results suggest that SPOP plays a pivotal role in colorectal cancer (CRC) through mesenchymal-epithelial transition and matrix metalloproteases. PMID: 26022775
19. SPOP functions as a tumor suppressor to negatively regulate the stability of the ERG oncoprotein in prostate cancer. PMID: 26344095
20. Overcoming ERG resistance to SPOP-mediated degradation represents a viable strategy for treatment of prostate cancers expressing either mutated SPOP or truncated ERG. PMID: 26344096
21. Our study revealed novel molecular mechanisms underlying the regulation of ERa protein and provided insights in understanding the relationship between SPOP mutations and the development of endometrial cancer. PMID: 25766326
22. SPOP plays critical roles in suppressing gastric tumorigenesis through inhibiting Hh/Gli2 signaling pathway. It may provide an alternative strategy for developing therapeutic agents of gastric cancer in future. PMID: 25204354
23. SPOP mutations and novel variants were detected in 5 of 27 aggressive PCa and one of 22 less aggressive PCa PMID: 24994784
24. SPOP has potential use as novel biomarker of glioma and may serve as an independent predictive factor for prognosis of glioma patients. PMID: 25351530
25. This study reveals novel molecular events underlying the regulation of DDIT3 protein homeostasis and provides insight in understanding the relationship between SPOP mutations and ER stress dysregulation in prostate cancer. PMID: 24990631
26. SPOP mutations contribute to prostate cancer development by altering the steady-state levels of key components in the androgen-signaling pathway; mutations are also observed in endometrial cancers PMID: 25058385
27. studies highlight the AR axis as the key transcriptional output of SPOP in prostate adenocarcinoma and provide an explanation for the prostate-specific tumor suppressor role of wt-SPOP PMID: 25274033
28. The present study demonstrates that prognosis varies depending on SPOP expression and mutational status, hence, defining a new biotype of PCa associated with a worse prognosis. PMID: 25204806
29. miR-145 has a role in post-transcriptional regulation of SPOP expression in selected tissues. PMID: 24845504
30. Prostate-cancer-associated SPOP mutants cannot bind to and promote androgen receptor degradation. PMID: 24508459
31. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. PMID: 25278611
32. a novel mutation in SPOP that tracks with prostate cancer within a family and is predicted to be deleterious. Taken together, our results implicate SPOP as a candidate gene for hereditary prostate cancer PMID: 24796539
33. the Speckle-Type POZ Protein (SPOP) gene is mutated in prostate cancer in a manner that is not specific for ethnicity, clinical, or pathologic parameters PMID: 24563616
34. Results indicate that SPOP serves as a regulatory hub to promote ccRCC tumorigenesis. PMID: 24656772
35. Prevalence of SPOP gene mutation varies depending on cancer types. It is common in prostate cancer and endometrial cancer, and rare in breast cancer, lung cancer, liver cancer, and acute leukemias. PMID: 23654205
36. Crystal structure of the high-order SPOP oligomer is presented depicting a helical organization that could enhance the efficiency of substrate ubiquitination. PMID: 23999291
37. Dzip1-dependent stabilization of Spop/HIB is evolutionarily conserved and essential for proper regulation of Gli/Ci proteins in the Hh pathway. PMID: 24072710
38. Loss of expression of SPOP gene might play a role in cancer pathogenesis by altering tumor suppressor gene functions of SPOP. PMID: 23216165
39. SPOP plays a critical tumor suppressor role in prostate cancer cells, promoting the turnover of SRC-3 protein and suppressing androgen receptor transcriptional activity. PMID: 23559371
40. Adaptor protein self-assembly provides a graded level of regulation of the SPOP/Cul3 E3 ligase toward its multiple protein substrates. PMID: 22632832
41. These results suggest that the novel regulatory mechanism of BRMS1 by Cul3-SPOP complex is important for breast cancer progression. PMID: 22085717
42. Mutagenesis study suggests that the ability of SPOP to self-associate as well as its ability to bind with Daxx was important for the modulation of Daxx-mediated transcriptional repression. PMID: 15240113
43. SPOP/Cul3-ubiquitin ligase plays an essential role in the control of Daxx level and, thus, in the regulation of Daxx-mediated cellular processes, including transcriptional regulation and apoptosis PMID: 16524876
44. define a novel mechanism whereby the phosphoinositide phosphatidylinositol 5-phosphate leads to stimulation of Cul3-SPOP ubiquitin ligase activity PMID: 18218622
45. The study first proposes the proapoptotic aspect of the BTB/POZ domain of SPOP protein based on the finding that cells expressing the C-terminal fragment of SPOP containing the BTB/POZ domain underwent apoptosis. PMID: 18997279
46. study found that SPOP plays a conserved role in TNF-mediated JNK signaling and was highly expressed in 99% of clear cell renal cell carcinomas PMID: 19164706
47. The study provides a molecular understanding of how SPOP and other MATH-BTB proteins recruit substrates to Cul3 and how their dimerization and conformational variability may facilitate avid interactions with diverse substrates. PMID: 19818708
48. Here, we report that the E3 ubiquitin ligase consisting of SPOP and CULLIN3 is able to ubiquitinate the Polycomb group protein BMI1. PMID: 15897469
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亞細(xì)胞定位：

Nucleus. Nucleus speckle.
蛋白家族：

Tdpoz family
組織特異性：

Widely expressed.
數(shù)據(jù)庫鏈接：

HGNC: 11254

OMIM: 602650

KEGG: hsa:8405

STRING: 9606.ENSP00000240327

UniGene: Hs.463382

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