Cat: PA2000-9053

Recombinant Human LRFN1 Protein,GST

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Analytical Data

  • Gene name

    LRFN1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    KIAA1484; Leucine rich repeat and fibronectin type III domain containing 1; Leucine rich repeat and fibronectin type III domain containing protein 1; Leucine-rich repeat and fibronectin type III domain-containing protein 1; LRFN 1; lrfn1; LRFN1_HUMAN; SALM 2; SALM2; Synaptic adhesion like molecule 2; Synaptic adhesion-like molecule 2

  • Species

    Human

  • Source

    E. coli

  • Tag

    GST-tag at N-terminal

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9P244

  • Expression Region

    1-771aa

  • AA Sequence

    MAPGPFSSALLSPPPAALPFLLLLWAGASRGQPCPGRCICQNVAPTLTMLCAKTGLLFVPPAIDRRVVELRLTDNFIAAVRRRDFANMTSLVHLTLSRNTIGQVAAGAFADLRALRALHLDSNRLAEVRGDQLRGLGNLRHLILGNNQIRRVESAAFDAFLSTVEDLDLSYNNLEALPWEAVGQMVNLNTLTLDHNLIDHIAEGTFVQLHKLVRLDMTSNRLHKLPPDGLFLRSQGTGPKPPTPLTVSFGGNPLHCNCELLWLRRLTREDDLETCATPEHLTDRYFWSIPEEEFLCEPPLITRQAGGRALVVEGQAVSLRCRAVGDPEPVVHWVAPDGRLLGNSSRTRVRGDGTLDVTITTLRDSGTFTCIASNAAGEATAPVEVCVVPLPLMAPPPAAPPPLTEPGSSDIATPGRPGANDSAAERRLVAAELTSNSVLIRWPAQRPVPGIRMYQVQYNSSVDDSLVYRMIPSTSQTFLVNDLAAGRAYDLCVLAVYDDGATALPATRVVGCVQFTTAGDPAPCRPLRAHFLGGTMIIAIGGVIVASVLVFIVLLMIRYKVYGDGDSRRVKGSRSLPRVSHVCSQTNGAGTGAAQAPALPAQDHYEALREVESQAAPAVAVEAKAMEAETASAEPEVVLGRSLGGSATSLCLLPSEETSGEESRAAVGPRRSRSGALEPPTSAPPTLALVPGGAAARPRPQQRYSFDGDYGALFQSHSYPRRARRTKRHRSTPHLDGAGGGAAGEDGDLGLGSARACLAFTSTEWMLESTV

  • Molecular Weight

    108.7 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

LRFN1 (Leucine-rich repeat and fibronectin type III domain-containing protein 1) is a member of the leucine-rich repeat protein family, which plays critical roles in various biological processes, including cell adhesion, signal transduction, and immune responses. Research into LRFN1 has gained momentum due to its implication in several pathological conditions, including cancer and neurodegenerative diseases. It is known to interact with various cell surface receptors and extracellular matrix components, suggesting a significant role in modulating cellular microenvironments. A recombinant LRFN1 protein may serve as a valuable tool for studying its biological functions and interactions in vitro. Understanding the structure and function of LRFN1 through recombinant protein studies could elucidate its mechanisms in health and disease, potentially leading to novel therapeutic strategies. The production of LRFN1 as a recombinant protein allows for the exploration of its binding affinities, signaling pathways, and functional roles, providing insights that could inform further studies on its implications in disease contexts. Additionally, the manipulation of LRFN1 expression levels may offer a unique approach to investigate its contribution to critical cellular processes, enhancing our understanding of its relevance in developmental biology and pathology.

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