Cat: PA2000-9728

Recombinant Human NLN Protein,His

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Analytical Data

  • Gene name

    NLN

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    AGTBP; Angiotensin binding protein; Angiotensin-binding protein; DKFZp564F123; EC 3.4.24.16; EP24.16; FLJ23002; KIAA1226; MEP; Microsomal endopeptidase; mitochondrial; Mitochondrial oligopeptidase M; MOP; NEUL_HUMAN; neurolysin (metallopeptidase M3 family); Neurolysin; Neurolysin. mitochondrial precursor; Neurotensin endopeptidase; Nln

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9BYT8

  • Expression Region

    38-704 aa

  • AA Sequence

    SSY TVAGRNVLRW DLSPEQIKTR TEELIVQTKQ VYDAVGMLGI EEVTYENCLQ ALADVEVKYI VERTMLDFPQ HVSSDKEVRA ASTEADKRLS RFDIEMSMRG DIFERIVHLQ ETCDLGKIKP EARRYLEKSI KMGKRNGLHL PEQVQNEIKS MKKRMSELCI DFNKNLNEDD TFLVFSKAEL GALPDDFIDS LEKTDDDKYK ITLKYPHYFP VMKKCCIPET RRRMEMAFNT RCKEENTIIL QQLLPLRTKV AKLLGYSTHA DFVLEMNTAK STSRVTAFLD DLSQKLKPLG EAEREFILNL KKKECKDRGF EYDGKINAWD LYYYMTQTEE LKYSIDQEFL KEYFPIEVVT EGLLNTYQEL LGLSFEQMTD AHVWNKSVTL YTVKDKATGE VLGQFYLDLY PREGKYNHAA CFGLQPGCLL PDGSRMMAVA ALVVNFSQPV AGRPSLLRHD EVRTYFHEFG HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDVD SLRRLSKHYK DGSPIADDLL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NTSLDAASEY AKYCSEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFYSC FKKEGIMNPE VGMKYRNLIL KPGGSLDGMD MLHNFLKREP NQKAFLMSRG LHAP

  • Molecular Weight

    80.6 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

The study of NLN (Neurolysin) recombinant protein has garnered significant attention in recent years due to its potential implications in neurobiology and therapeutic interventions. NLN is a zinc-dependent endopeptidase that plays a crucial role in the metabolism of neuropeptides and the regulation of neuroinflammation. It is predominantly expressed in the central nervous system, where it influences neuronal signaling and cellular responses. Researchers are particularly interested in the enzyme's involvement in neurodegenerative diseases, such as Alzheimer's and Parkinson's, as well as its potential role in modulating pain and mood disorders. The ability to produce NLN in a recombinant form allows for detailed structural and functional studies, enabling scientists to investigate its enzymatic mechanisms and identify potential inhibitors or modulators that could lead to therapeutic applications. Moreover, understanding NLN's interactions with various substrates could unveil new pathways in neurobiology and pave the way for innovative treatments targeting neurological disorders. The advancements in recombinant DNA technology and protein purification methods significantly facilitate these research endeavors, enhancing the ability to characterize NLN and explore its promise in clinical contexts.

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