|Application ||WB, IHC-P, IF, FC, E|
|Other Accession||Q6P9X4, O70274|
|Calculated MW||19127 Da|
|Antigen Region||32-59 aa|
|Other Names||Protein tyrosine phosphatase type IVA 2, HU-PP-1, OV-1, PTP(CAAXII), Protein-tyrosine phosphatase 4a2, Protein-tyrosine phosphatase of regenerating liver 2, PRL-2, PTP4A2, PRL2, PTPCAAX2|
|Target/Specificity||This PTP4A2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 32-59 amino acids from the Central region of human PTP4A2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|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||PTP4A2 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Promotes tumors. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB.|
|Cellular Location||Cell membrane. Early endosome. Cytoplasm.|
|Tissue Location||Ubiquitously expressed, with highest levels in skeletal muscle, heart and thymus. Overexpressed in prostate tumor tissue.|
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Provided below are standard protocols that you may find useful for product applications.
PTP4A2 belongs to a small class of the protein tyrosine phosphatase (PTP) family. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. PTPs in this class contain a protein tyrosine phosphatase catalytic domain and a characteristic C-terminal prenylation motif. This PTP has been shown to primarily associate with plasmic and endosomal membrane through its C-terminal prenylation. This PTP was found to interact with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), and thus may function as a regulator of GGT II activity.
Ewing,R.M., et.al., Mol. Syst. Biol. 3, 89 (2007)
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