Cat: PA2000-1578

Recombinant Human SA Protein,His

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Analytical Data

  • Gene name

    SA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    SA;SA2;Cohesin subunit SA-2

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P33402

  • Expression Region

    1-732aa

  • AA Sequence

    MSRRKISSES FSSLGSDYLE TSPEEEGECP LSRLCWNGSR SPPGPLEPSP AAAAAAAAPA PTPAASAAAA AATAGARRVQ RRRRVNLDSL GESISRLTAP SPQTIQQTLK RTLQYYEHQV IGYRDAEKNF HNISNRCSYA DHSNKEEIED VSGILQCTAN ILGLKFEEIQ KRFGEEFFNI CFHENERVLR AVGGTLQDFF NGFDALLEHI RTSFGKQATL ESPSFLCKEL PEGTLMLHYF HPHHIVGFAM LGMIKAAGKK IYRLDVEVEQ VANEKLCSDV SNPGNCSCLT FLIKECENTN IMKNLPQGTS QVPADLRISI NTFCRAFPFH LMFDPSMSVL QLGEGLRKQL RCDTHKVLKF EDCFEIVSPK VNATFERVLL RLSTPFVIRT KPEASGSENK DKVMEVKGQM IHVPESNSIL FLGSPCVDKL DELMGRGLHL SDIPIHDATR DVILVGEQAK AQDGLKKRMD KLKATLERTH QALEEEKKKT VDLLYSIFPG DVAQQLWQGQ QVQARKFDDV TMLFSDIVGF TAICAQCTPM QVISMLNELY TRFDHQCGFL DIYKVETIGD AYCVAAGLHR KSLCHAKPIA LMALKMMELS EEVLTPDGRP IQMRIGIHSG SVLAGVVGVR MPRYCLFGNN VTLASKFESG SHPRRINVSP TTYQLLKREE SFTFIPRSRE ELPDNFPKEI PGICYFLEVR TGPKPPKPSL SSSRIKKVSY NIGTMFLRET SL

  • Molecular Weight

    81.7 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

SA (Streptavidin) recombinant proteins have gained significant attention in molecular biology and biochemistry due to their strong and specific binding affinity for biotin, a key vitamin involved in various enzymatic reactions. The study of SA recombinant proteins emerged from the need for reliable tools in protein purification, detection, and labeling techniques, particularly in the fields of biotechnology and diagnostics. Streptavidin, originally derived from the bacterium *Streptomyces avidinii*, forms a stable complex with biotin that is characterized by an exceptionally high affinity (Kd in the order of 10^-14 M), making it a valuable asset for applications such as ELISA, Western blotting, and the development of biosensors. Advances in recombinant DNA technology have allowed researchers to produce large quantities of recombinant streptavidin with tailored properties, enhancing its utility in various experimental settings. Furthermore, genetic engineering techniques enable the modification of SA to improve its properties, such as solubility, stability, and binding capabilities. These recombinant proteins are also employed in targeted drug delivery systems and imaging techniques, facilitating the visualization of cellular processes. Consequently, the continued study and optimization of SA recombinant proteins hold promise for advancing research methodologies and therapeutic applications, underscoring their importance in both basic and applied sciences.

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