Cat: PAX2000-10743

Recombinant Human RaLP Protein,His

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Analytical Data

  • Gene name

    RaLP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    hShcD; MGC34023; Rai like protein; Rai-like protein; RaLP; SH2 domain protein C4; SHC (Src homology 2 domain containing) family member 4; SHC 4; SHC adaptor protein 4; SHC; SHC family member 4; SHC transforming protein 4; SHC transforming protein D; SHC-transforming protein 4; SHC-transforming protein D; Shc4; SHC4_HUMAN; SHCD; Src homology 2 domain containing family member 4; Src homology 2 domain containing transforming protein C4; Src homology 2 domain-containing-transforming protein C4

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q6S5L8

  • Expression Region

    1-630 aa

  • AA Sequence

    MRERGQDSLA GLVLYVGLFG HPGMLHRAKY SRFRNESITS LDEGSSGGSV GNKGSPQPPH PALAPHLPTE DATLPSQESP TPLCTLIPRM ASMKLANPAT LLSLKNFCLG TKEVPRLKLQ ESRDPGSSGP SSPETSLSRS GTAPPPQQDL VGHRATALTP DSCPLPGPGE PTLRSRQDRH FLQHLLGMGM NYCVRYMGCV EVLQSMRSLD FGMRTQVTRE AISRLCEAVP GANGAIKKRK PPVKFLSTVL GKSNLQFSGM NIKLTISTCS LTLMNLDNQQ IIANHHMQSI SFASGGDPDT TDYVAYVAKD PVNQRACHIL ECHNGMAQDV ISTIGQAFEL RFKQYLKNPS LNTSCESEEV HIDSHAEERE DHEYYNEIPG KQPPVGGVSD MRIKVQATEQ MAYCPIQCEK LCYLPGNSKC SSVYENCLEQ SRAIGNVHPR GVQSQRDTSL LKHTCRVDLF DDPCYINTQA LQSTPGSAGN QRSAQPLGSP WHCGKAPETV QPGATAQPAS SHSLPHIKQQ LWSEECYHGK LSRKAAESLL VKDGDFLVRE SATSPGQYVL SGLQGGQAKH LLLVDPEGKV RTKDHVFDNV GHLIRYHMDN SLPIISSGSE VSLKQPVRKD NNPALLHSNK

  • Molecular Weight

    68.7 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.

Quality inspection process

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Protein Description

RaLP (Recombinant Amphiphilic Lipoprotein) is a novel candidate in the field of drug delivery and therapeutic applications due to its unique structural and functional characteristics. As a type of recombinant protein, RaLP is engineered to exhibit both hydrophilic and hydrophobic properties, enabling it to encapsulate a diverse range of therapeutic agents, including small molecules, peptides, and nucleic acids. The research background of RaLP focuses on its potential to improve the bioavailability and therapeutic efficacy of drugs that are otherwise poorly soluble in biological systems. With an increasing emphasis on personalized medicine and targeted therapies, the development of effective delivery systems has become a critical area of study. RaLP's amphiphilic nature allows for enhanced cellular uptake, protection of the encapsulated agents from degradation, and improved circulation time in the bloodstream. Recent studies have demonstrated that RaLP can be tailored for specific applications, such as cancer therapy, gene delivery, and vaccine development. The ability to modify its surface properties and loading capacity offers significant advantages over traditional delivery vectors. As researchers continue to explore the versatility of RaLP, its implications for transforming conventional treatment paradigms and addressing unmet medical needs are becoming more apparent, paving the way for future advancements in biomedicine and drug formulation.

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