Cat: IPD-X27235

Recombinant Mouse LRIG1 Protein (HEK293),His

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Analytical Data

  • Gene name

    LRIG1

  • 简介

    The LRIG1 protein acts as a negative feedback regulator of receptor tyrosine kinase signaling by promoting receptor ubiquitination and accelerating intracellular degradation.Its extracellular LRR and Ig-like domains can interact with EGFR/ERBB1, ERBB2, ERBB3 and ERBB4.LRIG1 Protein, Mouse (HEK293, His) is the recombinant mouse-derived LRIG1 protein, expressed by HEK293 , with C-6*His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    rMuLeucine-rich repeats and immunoglobulin-like domains protein 1/LRIG1, His; Leucine-rich repeats and immunoglobulin-like domains protein 1; LIG-1; Lrig1

  • Species

    Mouse

  • Source

    HEK293

  • Tag

    C-6*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P70193

  • Expression Region

    A35-T794

  • AA Sequence

    AQAGPRAPCAAACTCAGDSLDCSGRGLATLPRDLPSWTRSLNLSYNRLSEIDSAAFEDLTNLQEVYLNSNELTAIPSLGAASIGVVSLFLQHNKILSVDGSQLKSYLSLEVLDLSSNNITEIRSSCFPNGLRIRELNLASNRISILESGAFDGLSRSLLTLRLSKNRITQLPVKAFKLPRLTQLDLNRNRIRLIEGLTFQGLDSLEVLRLQRNNISRLTDGAFWGLSKMHVLHLEYNSLVEVNSGSLYGLTALHQLHLSNNSISRIQRDGWSFCQKLHELILSFNNLTRLDEESLAELSSLSILRLSHNAISHIAEGAFKGLKSLRVLDLDHNEISGTIEDTSGAFTGLDNLSKLTLFGNKIKSVAKRAFSGLESLEHLNLGENAIRSVQFDAFAKMKNLKELYISSESFLCDCQLKWLPPWLMGRMLQAFVTATCAHPESLKGQSIFSVLPDSFVCDDFPKPQIITQPETTMAVVGKDIRFTCSAASSSSSPMTFAWKKDNEVLANADMENFAHVRAQDGEVMEYTTILHLRHVTFGHEGRYQCIITNHFGSTYSHKARLTVNVLPSFTKIPHDIAIRTGTTARLECAATGHPNPQIAWQKDGGTDFPAARERRMHVMPDDDVFFITDVKIDDMGVYSCTAQNSAGSVSANATLTVLETPSLAVPLEDRVVTVGETVAFQCKATGSPTPRITWLKGGRPLSLTERHHFTPGNQLLVVQNVMIDDAGRYTCEMSNPLGTERAHSQLSILPTPGCRKDGTT

  • Protein Length

    Extracellular Domain

  • Molecular Weight

    94 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.

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Protein Description

LRIG1 (Leucine-rich repeats and immunoglobulin-like domains 1) is a membrane protein that plays a crucial role in cell signaling and regulation, particularly in the context of development and cancer. It is known to negatively regulate receptor tyrosine kinases (RTKs), which are critical for various cellular processes, including proliferation, differentiation, and survival. Dysregulation of RTKs is often implicated in tumorigenesis, making LRIG1 an area of interest for cancer research. Studies have shown that LRIG1 expression is frequently downregulated in multiple cancer types, suggesting its potential role as a tumor suppressor. Consequently, researchers have focused on the characterization of LRIG1's structure and function, including the production of recombinant LRIG1 protein. This recombinant protein is pivotal for elucidating the mechanisms by which LRIG1 interacts with RTKs and other signaling pathways. Furthermore, understanding LRIG1's inhibitory effects could provide insights into novel therapeutic strategies that leverage its tumor-suppressive properties. The development of LRIG1-based therapies may offer new avenues for enhancing the efficacy of existing cancer treatments and improving patient outcomes. Overall, the study of LRIG1 recombinant protein holds promise for advancing our understanding of cancer biology and therapeutic intervention.

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