|Application ||WB, IHC|
|Calculated MW||49967 Da|
|Other Names||Tyrosine-protein phosphatase non-receptor type 1, Protein-tyrosine phosphatase 1B, PTP-1B, PTPN1, PTP1B|
|Target/Specificity||A synthetic peptide corresponding to residues surrounding serine 386 of human PTP1B was used as an immunogen. This antibody detects both phosphorylated and nonphosphorylated PTP1B.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PTP1B Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET.|
|Cellular Location||Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Note=Interacts with EPHA3 at the cell membrane|
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Provided below are standard protocols that you may find useful for product applications.
The non-transmembrane protein tyrosine phosphatase, PTP1B, comprises 435 amino acids, of which the C-terminal 114 residues have been implicated in controlling both localization and function of this enzyme. Increased phosphorylation of PTP1B is seen to accompany the transition from G2 to M phase of the cell cycle. Immunofluorescence experiments indicate that PTP-1B is localized predominantly in the endoplasmic reticulum (ER). Subcellular fractionation is consistent with this localization and establishes that PTP-1B is tightly associated with microsomal membranes, with its phosphatase domain oriented towards the cytoplasm. The finding of a tyrosine phosphatase on the ER suggests new possibilities for cellular events controlled by tyrosine phosphorylation (2). It has also been shown that PTP1B is a novel substrate for Akt and that phosphorylation of PTP1B by Akt at Ser(50) may negatively modulate its phosphatase activity creating a positive feedback mechanism for insulin signaling (3).
1. Flint AJ, et al. EMBO J 12(5):1937-46, 1993
2. Frangioni JV, et al. Cell 68(3):545-60, 1992
3. Ravichandran LV, et al Mol Endocrinol 5(10):1768-80, 2001.
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