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。
TRPM7 (CHAK1) Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
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- 实验流程
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Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q96QT4 |
| Other Accession | Q9BXB2 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 212697 Da |
| Antigen Region | 45-74 aa |
| Gene ID | 54822 |
|---|---|
| Other Names | Transient receptor potential cation channel subfamily M member 7, Channel-kinase 1, Long transient receptor potential channel 7, LTrpC-7, LTrpC7, TRPM7, CHAK1, LTRPC7 |
| Target/Specificity | This TRPM7 (CHAK1) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 45-74 amino acids from the N-terminal region of human TRPM7 (CHAK1). |
| 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 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 | TRPM7 (CHAK1) Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | TRPM7 |
|---|---|
| Synonyms | CHAK1, LTRPC7 {ECO:0000303|PubMed:113855 |
| Function | Bifunctional protein that combines an ion channel with an intrinsic kinase domain, enabling it to modulate cellular functions either by conducting ions through the pore or by phosphorylating downstream proteins via its kinase domain. The channel is highly permeable to divalent cations, specifically calcium (Ca2+), magnesium (Mg2+) and zinc (Zn2+) and mediates their influx (PubMed:11385574, PubMed:12887921, PubMed:15485879, PubMed:24316671, PubMed:35561741, PubMed:36027648). Controls a wide range of biological processes such as Ca2(+), Mg(2+) and Zn(2+) homeostasis, vesicular Zn(2+) release channel and intracellular Ca(2+) signaling, embryonic development, immune responses, cell motility, proliferation and differentiation (By similarity). The C-terminal alpha-kinase domain autophosphorylates cytoplasmic residues of TRPM7 (PubMed:18365021). In vivo, TRPM7 phosphorylates SMAD2, suggesting that TRPM7 kinase may play a role in activating SMAD signaling pathways. In vitro, TRPM7 kinase phosphorylates ANXA1 (annexin A1), myosin II isoforms and a variety of proteins with diverse cellular functions (PubMed:15485879, PubMed:18394644). |
| Cellular Location | Cell membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q923J1}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q923J1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q923J1}. Note=Localized largely in intracellular Zn(2+)-storage vesicles. {ECO:0000250|UniProtKB:Q923J1} |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
TRPCs, mammalian homologs of the Drosophila transient receptor potential (trp) protein, are ion channels that are thought to mediate capacitative calcium entry into the cell. TRP-PLIK is a protein that is both an ion channel and a kinase. As a channel, it conducts calcium and monovalent cations to depolarize cells and increase intracellular calcium. As a kinase, it is capable of phosphorylating itself and other substrates. The kinase activity is necessary for channel function, as shown by its dependence on intracellular ATP and by the kinase mutants.[supplied by OMIM]
REFERENCES
Blume-Jensen P, et al. Nature 2001. 411: 355.
Cantrell D, J. Cell Sci. 2001. 114: 1439.
Jhiang S Oncogene 2000. 19: 5590.
Manning G, et al. Science 2002. 298: 1912.
Moller, D, et al. Am. J. Physiol. 1994. 266: C351-C359.
Robertson, S. et al. Trends Genet. 2000. 16: 368.
Robinson D, et al. Oncogene 2000. 19: 5548.
Van der Ven, P, et al. Hum. Molec. Genet. 1993. 2: 1889.
Vanhaesebroeck, B, et al. Biochem. J. 2000. 346: 561.
Van Weering D, et al. Recent Results Cancer Res. 1998. 154: 271.
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