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。
PRAK Antibody
Purified Mouse Monoclonal Antibody
- 产品详情
- 实验流程
Application 
| WB, IHC, E |
|---|---|
| Primary Accession | Q8IW41 |
| Reactivity | Human |
| Host | Mouse |
| Clonality | Monoclonal |
| Clone Names | 7H10B4 |
| Isotype | IgG1 |
| Calculated MW | 54220 Da |
| Description | PRAK (p38-regulated /activated kinase), also referred to as mitogen-activated protein kinase (MAPK)-activated protein kinase (MAPKAPK)-5, is an ubiquitously expressed serine/threonine kinase regulated by p38α and p38β MAP kinases. Activated JNK, p38γ or p38δ are unable to induce phosphorylation of PRAK in vitro. Phosphorylation of PRAK occurs in vivo in response to p38 activation by stress-related extracellular stimuli including UV light, oxidation and proinflammatory cytokines. Two other substrates for p38, MAPKAPK-2 and MAPKAPK-3/3pK, share approximately 45% sequence homology with PRAK including the phosphorylation motif recognized by p38, Lys-X-Thr-Pro. Activated PRAK has been shown to specifically phosphorylate HSP 27 in vitro, suggesting that the protein may play a role in stress-induced small heat shock protein phosphorylation in vivo. |
| Immunogen | Purified recombinant fragment of PRAK expressed in E. Coli. |
| Formulation | Ascitic fluid containing 0.03% sodium azide. |
| Gene ID | 8550 |
|---|---|
| Other Names | MAP kinase-activated protein kinase 5, MAPK-activated protein kinase 5, MAPKAP kinase 5, MAPKAP-K5, MAPKAPK-5, MK-5, MK5, 2.7.11.1, p38-regulated/activated protein kinase, PRAK, MAPKAPK5, PRAK |
| Dilution | WB~~1/500 - 1/2000 IHC~~1/200 - 1/1000 E~~N/A |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | PRAK Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | MAPKAPK5 |
|---|---|
| Synonyms | PRAK |
| Function | Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement. |
| Cellular Location | Cytoplasm. Nucleus. Note=Translocates to the cytoplasm following phosphorylation and activation. Interaction with ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182, activates the protein kinase activity, followed by translocation to the cytoplasm Phosphorylation by PKA/PRKACA at Ser-115 also induces nuclear export |
| Tissue Location | Expressed ubiquitously. |
Research Areas
For Research Use Only. Not For Use In Diagnostic Procedures.
Application Protocols
Provided below are standard protocols that you may find useful for product applications.
REFERENCES
1. Paliga AJ. Natale DR. Watson AJ. Biol Cell. 2005, Aug, 97(8):629-40. 2. Wijtten PJ. Prak R. Lemme A. et al. Br Poult Sci. 2004, Aug, 45(4):504-11. 3. New L. Jiang Y. Han J. Mol Biol Cell. 2003, Jun, 14(6):2603-16. Epub 2003 Mar 20.
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