Recombinant Mouse Tyrosine-Protein Phosphatase Non-Receptor Type 6 (PTPN6) Protein (His)

Name: Recombinant Mouse Tyrosine-Protein Phosphatase Non-Receptor Type 6 (PTPN6) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07320P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Tyrosine-Protein Phosphatase Non-Receptor Type 6 (PTPN6) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P29351
Target Symbol	PTPN6
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MVRWFHRDLSGPDAETLLKGRGVPGSFLARPSRKNQGDFSLSVRVDDQVTHIRIQNSGDFYDLYGGEKFATLTELVEYYTQQQGILQDRDGTIIHLKYPLNCSDPTSERWYHGHISGGQAESLLQAKGEPWTFLVRESLSQPGDFVLSVLNDQPKAGPGSPLRVTHIKVMCEGGRYTVGGSETFDSLTDLVEHFKKTGIEEASGAFVYLRQPYYATRVNAADIENRVLELNKKQESEDTAKAGFWEEFESLQKQEVKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKNQLLGPDENSKTYIASQGCLDATVNDFWQMAWQENTRVIVMTTREVEKGRNKCVPYWPEVGTQRVYGLYSVTNSREHDTAEYKLRTLQISPLDNGDLVREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMESISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIETTKKKLEIIQSQKGQESEYGNITYPPAVRSAHAKASRTSSKHKEEVYENVHSKSKKEEKVKKQRSADKEKNKGSLKRK
Expression Range	1-595aa
Protein Length	Full Length
Mol. Weight	71.6 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	Protein-tyrosine phosphatase family, Non-receptor class 2 subfamily
Database References	KEGG: mmu:15170 STRING: 10090.ENSMUSP00000004377 UniGene: PMID: 29074590 These findings show a novel role for Shp-1 in the regulation of IEC growth and secretory lineage allocation, possibly via modulation of PI3K/Akt-dependent signaling pathways. PMID: 28465325 These findings suggest that protein tyrosine phosphatase SHP-1 may act as a positive regulator of osteoblast differentiation through direct association with and dephosphorylation of GSK3beta. PMID: 27614023 data establish SHP-1 as a critical player in setting the threshold downstream of TCR signaling and identify a novel function of SHP-1 as a regulator of T cell susceptibility to Treg-mediated suppression in vitro and in vivo PMID: 28550200 Results are consistent with predicted/observed reduction in the Lyn-SHIP-1-PTEN-SHP-1 axis function in B cells from systemic lupus PMID: 27114609 Our data show that SHP1 is required for the survival of mature thymocytes and the generation of the functional T-cell repertoire, as its absence leads to a reduction in the numbers of CD4(+) and CD8(+) naive T cells in the peripheral lymphoid compartments. PMID: 27354309 Our study suggests that metformin exerts its insulin sensitizing effects via inhibition of SHP-1 activity and expression. PMID: 28389241 we found that THEMIS directly regulated the catalytic activity of the tyrosine phosphatase SHP-1. PMID: 28250424 Studies indicate that SHP1 and SYK crosstalk as a critical regulator of MyD88 post-translational modifications and IL-1-driven inflammation. PMID: 28410990 Our findings uncover an important role for PP6 as an indispensable guardian of genomic integrity of the lengthy prophase I oocyte arrest, maintenance of primordial follicle pool, and thus female fertility. PMID: 27930667 The goal of this study was to analyze differentially expressed genes in the bone marrow of mice with NDLD to gain insight into the role of Ptpn6 in myelopoietic bone marrow pathology, and the mechanisms by which Ptpn6 insufficiency in the hematopoietic cells can lead to the development of skin lesions. PMID: 27020408 In addition to their role in NK cell activation by hematopoietic cells, the SLAM-SAP-SHP1 pathways influence responsiveness toward nonhematopoietic targets by a process akin to NK cell 'education'. PMID: 26878112 The prostate of mev/mev mice exhibits signs of aberrant differentiation and the resulting phenotype may be related to the loss of function of SHP-1. Prostatic anomalies in these mice affect, together with defects in sperm maduration, for their sterility. PMID: 24819344 These studies reveal critical pathways controlled by SHP-1 in oligodendrocytes that relate to susceptibility of SHP-1-deficient mice to both developmental defects in myelination and to inflammatory demyelinating diseases PMID: 25919645 SHP-1 regulates Cbl-b-mediated T cell responses by controlling its tyrosine phosphorylation and ubiquitination PMID: 26416283 The inhibitory activity of SHP-1 is needed for setting the threshold of natural killer cell reactivity. PMID: 25355530 Shp1 signalling is required for the establishment of a life-long protective humoral immunity. PMID: 24978161 Shp1 binds and controls PIPKIgamma activity and, thereby, modulates phosphatidylinositol (4,5)-bisphosphate levels and adhesion. PMID: 26101325 CCN1-integrin binding increased the expression of and association between SHP-1 and VEGF-R2, which leads to rapid dephosphorylation of VEGF-R2 tyrosine, thus preventing endothelial cell hyperproliferation. PMID: 26002917 pY motifs from known SHP-1 and SHP-2-binding proteins show that many of the pY motifs contain a hydrophobic or positively charged residue(s) at the pY+4 and pY+5 positions PMID: 16702225 SHP-1 appears to alter multiple aspects of macrophage biology that control virus replication, chemokine responsiveness, and inflammatory activity, that directly relate to virus-induced demyelinating disease. PMID: 19951174 our data reveal SHP-1 as a critical modifier of Treg function PMID: 20952680 these findings demonstrate that infiltrating macrophages in SHP-1-deficient mice play a crucial role in promoting viral replication and contribute to increased proinflammatory gene expression leading to demyelination. PMID: 18987138 there is a critical role for the tyrosine phosphatase activity of SHP-1 for induction of IL-12p40 production in macrophages in response to TLR ligands PMID: 20145200 In mouse liver, transcriptional activation of SHP1 gene by Prep1 attenuates insulin signal transduction and reduces glucose storage. PMID: 20864515 data reveal that PD-L1 is a critical modulator of Tregs' ability to suppress iALI, and this appears to involve SHP-1 activation. PMID: 25057927 Data indicate a pathological role for protein tyrosine phosphatase non-receptor type 6 SHP-1 in promoting inflammatory macrophage differentiation and myofiber damage in virus-infected skeletal muscle. PMID: 25681345 SHP-1 enzyme and Th2/Th1 paradigm may play a critical role in the maintenance of nasal immune homeostasis and in the regulation of allergic rhinitis. PMID: 25090641 SHP-1 contributes to nephrin deactivation in podocytes exposed to high glucose levels. PMID: 25404734 These results indicate that JBP regulates the expressions of SHP-1, Wnt3a, and AP-1 proteins in chemically damaged mice. PMID: 24841652 an SHP-1-centered feedback system wherein SHP-1 modulates CD40-induced p38MAPK activation threshold and reciprocal ERK-1/2 activation, establishing itself as a critical regulator of CD40 signaling reciprocity PMID: 25187664 STAT3 was a substrate for SHP-1 by co-immunoprecipitation. PMID: 24466030 We demonstrated that the association and oxidation of c-Src and SHP-1 by ROS are key steps in enhancing OC survival, which are responsible for increased bone loss when ovarian function ceases. PMID: 24824657 in DKO pre-B cells, the kinase Zap70 is associated with the pre-BCR, suggesting that Zap70 is important to promote B cell maturation in the absence of Syk and SHP-1. PMID: 24899508 a novel role for hepatocyte Shp1 in the regulation of PPARgamma and hepatic lipid metabolism. PMID: 24327268 The endothelial tyrosine phosphatase SHP-1 plays an important role for vascular hemostasis in vivo, which is crucial in TNF alpha -induced endothelial inflammation. PMID: 23766558 our results show for the first time that SHP-1 acts as a positive regulator of LPS-induced IL-10 production in splenic macrophages PMID: 23904162 Activation of Shp1-deficient CD4+ T cells results in skewing to the Th2 lineage and increased IL-4 production. PMID: 23797092 FGFRL1 does not function as a decoy receptor in beta-cells, but rather it enhances ERK1/2 signaling through association of SHP-1 with the receptor's intracellular SH2-binding motif. PMID: 23640895 Shp1 and Shp2 are major regulators of megakaryocyte development, platelet production, and function. PMID: 23509158 high levels of SHP-1 expression in glomeruli cause insulin resistance and podocyte loss PMID: 23531619 SHP-1 plays a critical role as a negative regulator in allergic inflammation, in allergen induced anaphylaxis, and seems to be required for normal basophil development. PMID: 23390550 Advanced glycation end product Nepsilon-carboxymethyllysine induces endothelial cell injuryinvolving SHP-1-regulated VEGFR-2 dephosphorylation. PMID: 22553146 dendritic cells functionally educate iNKT cells by tuning SHP-1 expression to limit reactivity. PMID: 23427253 Data indicate the amounts of Ptpn6 (Shp1) and MyD88 protein were reduced in dendritic cells of Ptpn6fl/flMyd88fl/flItgax-cre mice. PMID: 23521885 Selective target recognition of the SHP-1 knockdown natural killer (NK) cells revealed also possible involvement of the SHP-1 phosphatase in regulating other NK functions in mature NK cells. PMID: 22952938 findings show that most proliferating Germinal center (GC) B cells did not demonstrate active B cell receptor(BCR)signaling; signaling was limited by increased phosphatase activity; both SHP-1 and SHIP-1 were hyperphosphorylated in GC cells and remained colocalized with BCRs after ligation; SHP-1 was required for GC maintenance PMID: 22555432 SHP-1 is recruited early to phagosomes and that it is required for the acquisition of macrophage lysosomal features and acidification. PMID: 22826316 These studies suggest that abrogating SHP-1 in effector T cells may improve the efficacy of tumor elimination by T cell therapy without affecting the ability of the effector cells to persist and provide a long-term response. PMID: 22798667 Hyperglycemia and diabetes can cause glomerular podocyte apoptosis and endothelial dysfunction partly due to increased PKCdelta/p38 MAPK activation and the expression of SHP-1 to cause VEGF resistance, independent of NF-kappaB activation. PMID: 22499584

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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