Cat: PA1000-9561

Recombinant mouse LRIG1 Protein,His

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Analytical Data

  • Gene name

    LRIG1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    LRIG1;LIG1;Leucine-rich repeats and immunoglobulin-like domains Protein 1

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P70193

  • Expression Region

    1-794aa

  • AA Sequence

    MARPGPGVLG APRLAPRLLL WLLLLLLQWP ESAGAQAGPR APCAAACTCA GDSLDCSGRG LATLPRDLPS WTRSLNLSYN RLSEIDSAAF EDLTNLQEVY LNSNELTAIP SLGAASIGVV SLFLQHNKIL SVDGSQLKSY LSLEVLDLSS NNITEIRSSC FPNGLRIREL NLASNRISIL ESGAFDGLSR SLLTLRLSKN RITQLPVKAF KLPRLTQLDL NRNRIRLIEG LTFQGLDSLE VLRLQRNNIS RLTDGAFWGL SKMHVLHLEY NSLVEVNSGS LYGLTALHQL HLSNNSISRI QRDGWSFCQK LHELILSFNN LTRLDEESLA ELSSLSILRL SHNAISHIAE GAFKGLKSLR VLDLDHNEIS GTIEDTSGAF TGLDNLSKLT LFGNKIKSVA KRAFSGLESL EHLNLGENAI RSVQFDAFAK MKNLKELYIS SESFLCDCQL KWLPPWLMGR MLQAFVTATC AHPESLKGQS IFSVLPDSFV CDDFPKPQII TQPETTMAVV GKDIRFTCSA ASSSSSPMTF AWKKDNEVLA NADMENFAHV RAQDGEVMEY TTILHLRHVT FGHEGRYQCI ITNHFGSTYS HKARLTVNVL PSFTKIPHDI AIRTGTTARL ECAATGHPNP QIAWQKDGGT DFPAARERRM HVMPDDDVFF ITDVKIDDMG VYSCTAQNSA GSVSANATLT VLETPSLAVP LEDRVVTVGE TVAFQCKATG SPTPRITWLK GGRPLSLTER HHFTPGNQLL VVQNVMIDDA GRYTCEMSNP LGTERAHSQL SILPTPGCRK DGTT

  • Molecular Weight

    85 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

LRIG1 (leucine-rich repeat and Ig-like domains 1) is a critical regulator of cellular signaling pathways, particularly those involved in cell proliferation and differentiation. As a member of the LRIG family, LRIG1 functions primarily as a negative regulator of receptor tyrosine kinases (RTKs), including the epidermal growth factor receptor (EGFR). This regulation is crucial in maintaining cellular homeostasis and preventing uncontrolled cell growth, which is often associated with cancer. Loss of LRIG1 expression has been linked to various malignancies, indicating its potential role as a tumor suppressor. The recombinant protein of LRIG1 has garnered significant interest in research due to its potential therapeutic applications and its role in cancer biology. By studying LRIG1 in its recombinant form, researchers can elucidate its mechanism of action, interaction with other proteins, and effects on RTK signaling pathways. Additionally, recombinant LRIG1 can be utilized in functional assays to investigate its physiological roles and therapeutic potential. Understanding the structure-function relationship of LRIG1 may pave the way for novel cancer treatment strategies, highlighting its importance in targeted therapy development and personalized medicine approaches. Overall, the investigation of LRIG1 as a recombinant protein opens new avenues for understanding its biological significance and therapeutic potential, emphasizing the need for continued research in this area.

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