Cat: PA1000-9182

Recombinant Human RLN Protein,His

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Analytical Data

  • Gene name

    RLN

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    RLN;Rln;Rlx;Prorelaxin 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P04808

  • Expression Region

    23-53aa

  • AA Sequence

    VAAKWKDD VIKLCGRELV RAQIAICGMS TWS

  • 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

RLN (Relaxin) is a peptide hormone belonging to the insulin superfamily, primarily known for its roles in reproductive physiology and various physiological processes. Originally identified for its involvement in pregnancy, RLN facilitates uterine relaxation, aids in cervical ripening, and contributes to the remodeling of reproductive tissues. Beyond reproductive functions, emerging research highlights RLN's potential therapeutic applications in treating cardiovascular diseases, fibrosis, and metabolic disorders. The therapeutic use of RLN is driven by its action on specific receptors, influencing tissue remodeling and angiogenesis. Furthermore, RLN’s ability to modulate inflammation and promote wound healing has attracted considerable interest in regenerative medicine. Despite its promising clinical applications, the complex structure and function of RLN, coupled with its short half-life in circulation, pose challenges for effective therapeutic use. To address these challenges, researchers have focused on the development of recombinant RLN (rRLN) proteins, utilizing advanced genetic engineering techniques for improved stability and efficacy. The study of rRLN not only enhances our understanding of its biological mechanisms but also paves the way for innovative treatments that exploit RLN's multifaceted roles in various physiological and pathological contexts. The ongoing exploration into rRLN encapsulates the convergence of molecular biology, pharmacology, and therapeutics, emphasizing the need for continued research into its various applications and mechanisms of action.

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