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。
SF3B1 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | O75533 |
| Other Accession | O57683, Q99NB9, NP_036565.2 |
| Reactivity | Human, Rat, Mouse |
| Predicted | Mouse, Xenopus |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 145830 Da |
| Antigen Region | 374-402 aa |
| Gene ID | 23451 |
|---|---|
| Other Names | Splicing factor 3B subunit 1, Pre-mRNA-splicing factor SF3b 155 kDa subunit, SF3b155, Spliceosome-associated protein 155, SAP 155, SF3B1, SAP155 |
| Target/Specificity | This SF3B1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 374-402 amino acids from the N-terminal region of human SF3B1. |
| Dilution | WB~~1:1000 IHC-P~~1:100~500 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 | SF3B1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | SF3B1 {ECO:0000303|PubMed:30567737, ECO:0000312|HGNC:HGNC:10768} |
|---|---|
| Function | Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:12234937, PubMed:27720643, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B1 is part of the SF3B subcomplex, which is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA (PubMed:12234937). Sequence independent binding of SF3A and SF3B subcomplexes upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). May also be involved in the assembly of the 'E' complex (PubMed:10882114). Also acts as a component of the minor spliceosome, which is involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932). Together with other U2 snRNP complex components may also play a role in the selective processing of microRNAs (miRNAs) from the long primary miRNA transcript, pri-miR-17-92 (By similarity). |
| Cellular Location | Nucleus. Nucleus speckle. Note=During mitosis, transiently dispersed from the nuclear speckles to the cytoplasm |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
This gene encodes subunit 1 of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and a 12S RNA unit, forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a complex binds pre-mRNA upstream of the intron's branch site in a sequence independent manner and may anchor the U2 snRNP to the pre-mRNA. Splicing factor 3b is also a component of the minor U12-type spliceosome. The carboxy-terminal two-thirds of subunit 1 have 22 non-identical, tandem HEAT repeats that form rod-like, helical structures. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq].
REFERENCES
Corsini, L., et al. J. Biol. Chem. 284(1):630-639(2009)
Tanuma, N., et al. J. Biol. Chem. 283(51):35805-35814(2008)
Pessa, H.K., et al. Proc. Natl. Acad. Sci. U.S.A. 105(25):8655-8660(2008)
Kuwasako, K., et al. Proteins 71(4):1617-1636(2008)
Avila, M.L., et al. Biochem. Biophys. Res. Commun. 364(1):26-32(2007)
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