|Application ||WB, IHC-P, E|
|Calculated MW||35144 Da|
|Antigen Region||1-30 aa|
|Other Names||Serine/threonine-protein phosphatase 6 catalytic subunit, PP6C, Serine/threonine-protein phosphatase 6 catalytic subunit, N-terminally processed, PPP6C, PPP6|
|Target/Specificity||This PPP6C antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human PPP6C.|
|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||PPP6C Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Catalytic subunit of protein phosphatase 6 (PP6) (PubMed:17079228, PubMed:29053956). PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL2 receptor stimulation (PubMed:10227379). N-terminal domain restricts G1 to S phase progression in cancer cells, in part through control of cyclin D1 (PubMed:17568194). During mitosis, regulates spindle positioning (PubMed:27335426). Downregulates MAP3K7 kinase activation of the IL1 signaling pathway by dephosphorylation of MAP3K7 (PubMed:17079228). Participates also in the innate immune defense against viruses by desphosphorylating RIG-I/DDX58, an essential step that triggers RIG- I/DDX58-mediated signaling activation (PubMed:29053956).|
|Cellular Location||Mitochondrion. Cytoplasm|
|Tissue Location||Ubiquitously expressed in all tissues tested with highest expression levels in testis, heart, kidney, brain, stomach, liver and skeletal muscle and lowest in placenta, lung colon and spleen.|
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Provided below are standard protocols that you may find useful for product applications.
PPP6C belongs to the PPP phosphatase family, PP-V subfamily. Reversible phosphorylation of proteins on serine and threonine residues is an important biochemical event that regulates a broad variety of intracellular processes. The phosphorylation state is determined by the well-controlled balance of activities of serine/threonine-specific protein kinases and protein phosphatases, including PPP6C. Expression levels are highest in testis, heart, and skeletal muscle and lowest in placenta, lung, and kidney. PPP6C can complement mutations in the S. cerevisiae Sit4 and S. pombe ppe1 genes, indicating that PPP6C is the functional homolog of yeast Sit4p and ppe1. Since Sit4p is required for the G1 to S transition of the cell cycle and ppe1 is involved in cell shape control and mitotic division, it has been suggested that PPP6C functions in cell cycle regulation.
Yang, J., et al., EMBO J. 24(1):1-10 (2005).
Zhou, G., et al., J. Biol. Chem. 279(45):46595-46605 (2004).
Huang, S., et al., J. Biol. Chem. 279(35):36490-36496 (2004).
Swingle, M.R., et al., J. Biol. Chem. 279(32):33992-33999 (2004).
Wechsler, T., et al., Proc. Natl. Acad. Sci. U.S.A. 101(5):1247-1252 (2004).
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