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Recombinant Mouse Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (Inppl1), partial

Recombinant Mouse Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (Inppl1), partial

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Target Background

Product Details

Abbreviation

Inppl1

Purity

>85% (SDS-PAGE)

Target Names

Inppl1

Uniprot NO.

Q6P549

Alternative Names

Inppl1; Ship2; Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2; EC 3.1.3.86; AblSH3-binding protein; Inositol polyphosphate phosphatase-like protein 1; INPPL-1; SH2 domain-containing inositol 5'-phosphatase 2; SH2 domain-containing inositol phosphatase 2; SHIP-2

Species

Mus musculus (Mouse)

Source

Yeast

Expression Region

1-1257

Target Protein Sequence

MASVCGTPSP GGALGSPAPA WYHRDLSRAA AEELLARAGR DGSFLVRDSE SVAGAFALCV LYQKHVHTYR ILPDGEDFLA VQTSQGVPVR RFQTLGELIG LYAQPNQGLV CALLLPVEGE REPDPPDDRD ASDVEDEKPP LPPRSGSTSI SAPVGPSSPL PTPETPTTPA AESTPNGLST VSHEYLKGSY GLDLEAVRGG ASNLPHLTRT LVTSCRRLHS EVDKVLSGLE ILSKVFDQQS SPMVTRLLQQ QSLPQTGEQE LESLVLKLSV LKDFLSGIQK KALKALQDMS STAPPAPLQP SIRKAKTIPV QAFEVKLDVT LGDLTKIGKS QKFTLSVDVE GGRLVLLRRQ RDSQEDWTTF THDRIRQLIK SQRVQNKLGV VFEKEKDRTQ RKDFIFVSAR KREAFCQLLQ LMKNRHSKQD EPDMISVFIG TWNMGSVPPP KNVTSWFTSK GLGKALDEVT VTIPHDIYVF GTQENSVGDR EWLDLLRGGL KELTDLDYRP IAMQSLWNIK VAVLVKPEHE NRISHVSTSS VKTGIANTLG NKGAVGVSFM FNGTSFGFVN CHLTSGNEKT TRRNQNYLDI LRLLSLGDRQ LSAFDISLRF THLFWFGDLN YRLDMDIQEI LNYISRREFE PLLRVDQLNL EREKHKVFLR FSEEEISFPP TYRYERGSRD TYAWHKQKPT GVRTNVPSWC DRILWKSYPE THIICNSYGC TDDIVTSDHS PVFGTFEVGV TSQFISKKGL SKTSDQAYIE FESIEAIVKT ASRTKFFIEF YSTCLEEYKK SFENDAQSSD NINFLKVQWS SRQLPTLKPI LADIEYLQDQ HLLLTVKSMD GYESYGECVV ALKSMIGSTA QQFLTFLSHR GEETGNIRGS MKVRVPTERL GTRERLYEWI SIDKDDTGAK SKVPSVSRGS QEHRSGSRKP ASTETSCPLS KLFEEPEKPP PTGRPPAPPR AVPREEPLNP RLKSEGTSEQ EGVAAPPPKN SFNNPAYYVL EGVPHQLLPL EPPSLARAPL PPATKNKVAI TVPAPQLGRH RTPRVGEGSS SDEDSGGTLP PPDFPPPPLP DSAIFLPPNL DPLSMPVVRG RSGGEARGPP PPKAHPRPPL PPGTSPASTF LGEVASGDDR SCSVLQMAKT LSEVDYAPGP GRSALLPNPL ELQPPRGPSD YGRPLSFPPP RIRESIQEDL AEEAPCPQGG RASGLGEAGM GAWLRAIGLE RYEEGLVHNG WDDLEFLSDI TEEDLEEAGV QDPAHKRLLL DTLQLSK
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification.

Gene References into Functions

Inactivation of SHIP2 leads to increased microvilli formation and solute reabsorption by the renal proximal tubule and was associated with hyperactivated ezrin/radixin/moesin proteins and increased Rho-GTP. PMID:28302370
data suggest that endothelial SHIP2 is required to maintain normal systemic glucose homeostasis and prevent oxidative stress-induced endothelial dysfunction. PMID:28830894
The authors concluded that the FcgammaRIIb-SHIP2 axis links Abeta neurotoxicity to tau pathology by dysregulating phosphoinositide metabolism, providing insight into therapeutic potential against Alzheimer's disease. PMID:27834631
These findings suggest that palmitate contributes to SHIP2 overexpression in skeletal muscle via the mechanisms involving the activation of ceramide-JNK and NF-kappaB pathways. PMID:24924631
results suggest that SHIP2 contributes to the regulation of food intake mainly via the attenuation of insulin signalling in the hypothalamus of mice PMID:23286299
The catalytically-inactive Ship2 mutant protein in a context of reduced PtdIns(4,5)P2 3-kinase activity. PMID:22750293
Regulation of insulin signaling and glucose transporter 4 (GLUT4) exocytosis by phosphatidylinositol 3,4,5-trisphosphate (PIP3) phosphatase, skeletal muscle, and kidney enriched inositol polyphosphate phosphatase (SKIP). PMID:22247557
These results suggest that SHIP2 is a potent negative regulator of insulin/IGF-I actions in the brain, and excess amounts of SHIP2 may be related, at least in part, to brain dysfunction in insulin resistance with type 2 diabetes. PMID:20829391
The SHIP2 is a negative regulator of insulin signaling, our findings suggest the importance of the phosphoinositide metabolism at endocytic clathrin-coated pits in the regulation of insulin signal output. PMID:20679431
Association with the insulin resistance of diabetic db/db mice. PMID:12145149
The role of SHIP2 in controlling phosphatidylinositol 3,4,5-trisphosphate levels in platelets. PMID:12885297
SH2-containing inositol phosphatase 2 predominantly regulates Akt2, and not Akt1, phosphorylation at the plasma membrane in response to insulin in adipocytes PMID:14744864
SHIP2 plays an important role in the negative regulation of insulin signaling for protein synthesis and the impact of SHIP2 is altered, dependent on the acute or chronic exposure of excess concentrations of amino acids in culture. PMID:15044364
SHIP2 does not localize in lipid rafts in 3T3-L1 adipocytes PMID:15135055
Results suggest that inhibition of SHIP2 would be useful in the effort to ameliorate diet-induced obesity, but call into question a dominant role of SHIP2 in modulating glucose homeostasis. PMID:15654325
Inhibition of endogenous SHIP2 is effective in improving the state of insulin resistance caused by chronic insulin treatment. PMID:15654601
SHIP2 does not function as a suppressor of insulin signaling to glucose transport through the PI 3-kinase pathway in cultured 3T3-L1 adipocytes PMID:15824124
Data establish a link between SHIP2 and the acute control of phosphatidylinositol 3,4,5-trisphosphate levels in intact cells. PMID:15885100
a negative regulator of IgE-induced mast cell activation via a calcium-independent pathway PMID:17579026
Possibility of a specific inhibition of SHIP2 for the prevention and/or treatment of type 2 diabetes. PMID:17596404
The association of SHIP2 and the adaptor protein Aps has an impact on biochemical properties of both partners. PMID:17620296
SHIP2 add back experiments in SHIP2 -/- cells confirm its critical role as a lipid phosphatase in the control of PtdIns(3,4,5)P(3) level in response to H(2)O(2). PMID:17643961
increased abundance of SHIP2 in vivo contributes, at least in part, to the impairment of glucose metabolism and insulin sensitivity on a normal chow diet PMID:18039790
catalytically inactive dominant-negative SHIP2 (P686A-D690A-R691A; PDR/AAA) reduces preadipocyte proliferation by attenuating PDGFR signaling PMID:18814181
PTEN and SHIP2, the phosphatases widely implicated as negative regulators of insulin signaling, are responsible for dephosphorylation of FAK. PMID:19501627

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Subcellular Location

Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Cell projection, filopodium. Cell projection, lamellipodium. Nucleus. Nucleus speckle. Note=Translocates to membrane ruffles when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. Partly translocated via its SH2 domain which mediates interaction with tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor (FCGR2B). Tyrosine phosphorylation may also participate in membrane localization. Insulin specifically stimulates its redistribution from the cytosol to the plasma membrane. Recruited to the membrane following M-CSF stimulation. In activated spreading platelets, localizes with actin at filopodia, lamellipodia and the central actin ring.

Protein Families

Inositol 1,4,5-trisphosphate 5-phosphatase family

Tissue Specificity

Widely expressed.

Database Links

UNIGENE: Mm.476000

KEGG: mmu:16332

STRING: 10090.ENSMUSP00000048057

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