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。
Mouse Csnk2a2 Antibody (N-term) 精选
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| WB, E |
|---|---|
| Primary Accession | O54833 |
| Other Accession | P19784, P21869, P20427, NP_034104.1 |
| Reactivity | Human, Mouse |
| Predicted | Bovine, Chicken, Rat, Canine, Rabbit |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 41215 Da |
| Antigen Region | 4-32 aa |
| Gene ID | 13000 |
|---|---|
| Other Names | Casein kinase II subunit alpha', CK II alpha', Csnk2a2 |
| Target/Specificity | This Mouse Csnk2a2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 4-32 amino acids from the N-terminal region of mouse Csnk2a2. |
| 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 | Mouse Csnk2a2 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | Csnk2a2 |
|---|---|
| Function | Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser- 392' of p53/TP53 following UV irradiation. Phosphorylates a number of DNA repair proteins in response to DNA damage, such as MDC1, RAD9A, RAD51 and HTATSF1, promoting their recruitment to DNA damage sites. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. May phosphorylate histone H2A on 'Ser-1'. |
| Cellular Location | Nucleus. Cytoplasm. Note=Interaction with SIRT6 prevents translocation into the nucleus. |
| Tissue Location | Highly expressed in brain, testis and mature epididymal spermatozoa. Weakly expressed in kidney, liver, lung, spleen and thymus (at protein level). |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha and alpha' chains contain the catalytic site. Participates in Wnt signaling. CK2 phosphorylates 'Ser-389' of p53/TP53 following UV irradiation (By similarity).
REFERENCES
Pastori, V., et al. Biochim. Biophys. Acta 1802 (7-8), 583-592 (2010) :
Cobb, L.J., et al. Mol. Endocrinol. 23(10):1624-1633(2009)
Mueller, T., et al. Hum. Mol. Genet. 18(17):3334-3343(2009)
Maier, B., et al. Genes Dev. 23(6):708-718(2009)
Kang, H., et al. PLoS ONE 4 (8), E6611 (2009) :
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