Cat: IPD-X23131

Recombinant Mouse SHP-2 Protein (HEK293),His

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Analytical Data

  • Gene name

    SHP-2

  • 简介

    SHP-2 Protein functions downstream of diverse receptor and cytoplasmic tyrosine kinases, participating in signal transduction from the cell surface to the nucleus.It positively regulates the MAPK pathway and dephosphorylates key proteins like GAB1, ARHGAP35, EGFR, ROCK2, CDC73, and SOX9.Additionally, SHP-2 dephosphorylates NEDD9/CAS-L to modulate cellular processes.SHP-2 Protein, Mouse (HEK293, His) is the recombinant mouse-derived SHP-2 protein, expressed by HEK293 , with C-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Tyrosine-protein phosphatase non-receptor type 11; SH-PTP2; SHP-2; Ptpn11

  • Species

    Mouse

  • Source

    HEK293

  • Tag

    C-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P35235-2

  • Expression Region

    M1-R593

  • AA Sequence

    MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIVDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIKYSLVDQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQRSFR

  • Protein Length

    Full Length of Isoform-2

  • Molecular Weight

    65 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

RBP4, or retinol-binding protein 4, is a protein that plays a crucial role in vitamin A transport and metabolism in the human body. Its primary function is to bind retinol, the alcohol form of vitamin A, and facilitate its delivery to tissues, thereby contributing to various physiological functions, including vision, immune response, and skin health. Recent research has highlighted RBP4's potential involvement in metabolic disorders, such as obesity and type 2 diabetes, as elevated levels of RBP4 in the bloodstream have been correlated with insulin resistance and dyslipidemia. Given its significance in these metabolic pathways, RBP4 has emerged as a potential biomarker for assessing metabolic health and as a target for therapeutic interventions. The production of recombinant RBP4 proteins has become critical for advancing research into its structure-function relationship, elucidating its biological roles, and exploring its implications in diseases. By utilizing recombinant DNA technology, researchers can produce RBP4 in sufficient quantities for various assays, enabling in-depth studies of its interactions with retinol and other cellular components. This research is expected to yield insights that could inform the development of novel strategies for diagnosing and treating metabolic disorders linked to RBP4 dysregulation. Overall, the study of recombinant RBP4 proteins is a promising avenue that bridges the gap between basic science and clinical application, enhancing our understanding of vitamin A metabolism and its impact on human health.

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