Cat: PA2000-8373

Recombinant Human HSPA12A Protein,GST

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Analytical Data

  • Gene name

    HSPA12A

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    FLJ13874; Heat shock 70 kDa protein 12A; heat shock 70kD protein 12A; heat shock 70kDa protein 12A; HS12A_HUMAN; Hspa12a; KIAA0417

  • Species

    Human

  • Source

    E. coli

  • Tag

    GST-tag at N-terminal

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O43301

  • Expression Region

    2-675aa

  • AA Sequence

    ADKEAGGSD GPRETAPTSA YSSPARSLGD TGITPLSPSH IVNDTDSNVS EQQSFLVVVA VDFGTTSSGY AYSFTKEPEC IHVMRRWEGG DPGVSNQKTP TTILLTPERK FHSFGYAARD FYHDLDPNEA KQWLYLEKFK MKLHTTGDLT MDTDLTAANG KKVKALEIFA YALQYFKEQA LKELSDQAGS EFENSDVRWV ITVPAIWKQP AKQFMRQAAY QAGLASPENS EQLIIALEPE AASIYCRKLR LHQMIELSSK AAVNGYSGSD TVGAGFTQAK EHIRRNRQSR TFLVENVIGE IWSELEEGDK YVVVDSGGGT VDLTVHQIRL PEGHLKELYK ATGGPYGSLG VDYEFEKLLY KIFGEDFIEQ FKIKRPAAWV DLMIAFESRK RAAAPDRTNP LNITLPFSFI DYYKKFRGHS VEHALRKSNV DFVKWSSQGM LRMSPDAMNA LFKPTIDSII EHLRDLFQKP EVSTVKFLFL VGGFAEAPLL QQAVQAAFGD QCRIIIPQDV GLTILKGAVL FGLDPAVIKV RRSPLTYGVG VLNRYVEGKH PPEKLLVKDG TRWCTDVFDK FISADQSVAL GELVKRSYTP AKPSQLVIVI NIYSSEHDNV SFITDPGVKK CGTLRLDLTG TSGTAVPARR EIQTLMQFGD TEIKATAIDI ATSKSVKVGI DFLNY

  • Molecular Weight

    74.9 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

HSPA12A, also known as Heat Shock Protein 12A, is a member of the Hsp70 family of chaperone proteins, which play critical roles in protein folding, cellular stress response, and the maintenance of cellular homeostasis. The study of HSPA12A has gained significant interest in recent years due to its potential implications in various physiological and pathological processes, including cancer progression, neurodegenerative diseases, and aging. Unlike other Hsp70 family members, HSPA12A exhibits unique expression patterns and functions, making it a candidate for therapeutic intervention and biomarker identification. Researchers are particularly interested in understanding its role in protecting cells from stressors, such as heat shock and oxidative stress, and its involvement in modulating inflammatory responses. Furthermore, the development of recombinant HSPA12A proteins has facilitated the exploration of its biochemical properties and interactions with client proteins, enhancing the understanding of its mechanisms of action. This research is critical for elucidating the protective roles of HSPA12A in cellular stress responses and its potential applications in disease treatment and prevention. The ongoing investigation into HSPA12A and its recombinant forms could yield insights into novel therapeutic strategies aimed at enhancing cellular resilience and combating various diseases associated with protein misfolding and stress.

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