癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
CPSF3 Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| WB, E |
|---|---|
| Primary Accession | Q9UKF6 |
| Other Accession | Q9QXK7, P79101, NP_057291.1 |
| Reactivity | Human |
| Predicted | Bovine, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 77486 Da |
| Antigen Region | 192-221 aa |
| Gene ID | 51692 |
|---|---|
| Other Names | Cleavage and polyadenylation specificity factor subunit 3, 3127-, Cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF 73 kDa subunit, mRNA 3'-end-processing endonuclease CPSF-73, CPSF3, CPSF73 |
| Target/Specificity | This CPSF3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 192-221 amino acids from the Central region of human CPSF3. |
| Dilution | WB~~1:1000 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | CPSF3 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | CPSF3 |
|---|---|
| Synonyms | CPSF73 |
| Function | Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as an mRNA 3'-end-processing endonuclease (PubMed:30507380). Also involved in the histone 3'-end pre-mRNA processing (PubMed:30507380). U7 snRNP- dependent protein that induces both the 3'-endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner. Required for entering/progressing through S-phase of the cell cycle (PubMed:30507380). Required for the selective processing of microRNAs (miRNAs) during embryonic stem cell differentiation via its interaction with ISY1 (By similarity). Required for the biogenesis of all miRNAs from the pri-miR-17-92 primary transcript except miR-92a (By similarity). Only required for the biogenesis of miR-290 and miR-96 from the pri-miR-290-295 and pri-miR-96-183 primary transcripts, respectively (By similarity). |
| Cellular Location | Nucleus. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Most eukaryotic mRNA precursors (pre-mRNAs) undergo extensive maturational processing, including cleavage and polyadenylation at the 3-prime end. CPSF3 encodes the 73-kD subunit of the cleavage and polyadenylation specificity factor (CPSF) and is the pre-mRNA 3-prime-end-processing endonuclease (Mandel et al., 2006 [PubMed 17128255]).
REFERENCES
Rozenblatt-Rosen, O., et al. Proc. Natl. Acad. Sci. U.S.A. 106(3):755-760(2009)
Zhu, Z.H., et al. Oncogene 28(1):41-51(2009)
Yang, X.C., et al. Mol. Cell. Biol. 29(1):31-42(2009)
Kolev, N.G., et al. EMBO Rep. 9(10):1013-1018(2008)
de la Vega, L., et al. J. Mol. Biol. 372(2):317-330(2007)
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