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。
IRAK4 Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| IHC-P, WB, E |
|---|---|
| Primary Accession | Q9NWZ3 |
| Other Accession | Q8R4K2, Q1RMT8, NP_057207 |
| Reactivity | Human |
| Predicted | Bovine, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 51530 Da |
| Antigen Region | 5-36 aa |
| Gene ID | 51135 |
|---|---|
| Other Names | Interleukin-1 receptor-associated kinase 4, IRAK-4, Renal carcinoma antigen NY-REN-64, IRAK4 |
| Target/Specificity | This IRAK4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 5-36 amino acids from the N-terminal region of human IRAK4. |
| Dilution | IHC-P~~1:100~500 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 prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| 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 | IRAK4 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | IRAK4 |
|---|---|
| Function | Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways (PubMed:17878374). Is rapidly recruited by MYD88 to the receptor- signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin- binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates NCF1 and regulates NADPH oxidase activation after LPS stimulation suggesting a similar mechanism during microbial infections. |
| Cellular Location | 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
Protein kinases are enzymes that transfer a phosphate group from a phosphate donor, generally the g phosphate of ATP, onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. With more than 500 gene products, the protein kinase family is one of the largest families of proteins in eukaryotes. The family has been classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. The tyrosine-like kinase (TLK) group consists of 40 tyrosine and serine-threonine kinases such as MLK (mixed-lineage kinase), LISK (LIMK/TESK), IRAK (interleukin-1 receptor-associated kinase), Raf, RIPK (receptor-interacting protein kinase), and STRK (activin and TGF-beta receptors) families.
REFERENCES
Medvedev, A.E., et al., J. Exp. Med. 198(4):521-531 (2003).
Jiang, Z., et al., J. Biol. Chem. 278(13):10952-10956 (2003).
Picard, C., et al., Science 299(5615):2076-2079 (2003).
Li, S., et al., Proc. Natl. Acad. Sci. U.S.A. 99(8):5567-5572 (2002).
Suzuki, N., et al., Nature 416(6882):750-756 (2002).
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