|Application ||WB, IHC-P, E|
|Calculated MW||47300 Da|
|Antigen Region||333-364 aa|
|Other Names||Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma, Phosphatidylinositol 5-phosphate 4-kinase type II gamma, PI(5)P 4-kinase type II gamma, PIP4KII-gamma, PIP4K2C, PIP5K2C|
|Target/Specificity||This PIP5K2G antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 333-364 amino acids from the C-terminal region of human PIP5K2G.|
|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||PIP5K2G Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||May play an important role in the production of Phosphatidylinositol bisphosphate (PIP2), in the endoplasmic reticulum.|
|Cellular Location||Cytoplasm. Membrane. Note=Mostly found in the cytosol and surrounding plasma membrane. However, its presence in the endoplasmic reticulum seems to be a prerequisite for PIP2 synthesis (By similarity).|
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Provided below are standard protocols that you may find useful for product applications.
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.
Blume-Jensen P, et al. Nature 2001. 411: 355.
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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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