Cat: PA1000-2597

Recombinant Human PYGL Protein,His

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Analytical Data

  • Gene name

    PYGL

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PYGL;Glycogen phosphorylase. liver form

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P06737

  • Expression Region

    1-847aa

  • AA Sequence

    MGSSHHHHHHSSGLVPRGSHMGSEFELRRQASMAKPLTDQEKRRQISIRG IVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTVRDHLVGRW IRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGL DIEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFN QKIRDGWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWID TQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNLRDFNVGDYIQAVL DRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKASKFG STRGAGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKLPWSKAWEL TQKTFAYTNHTVLPEALERWPVDLVEKLLPRHLEIIYEINQKHLDRIVAL FPKDVDRLRRMSLIEEEGSKRINMAHLCIVGSHAVNGVAKIHSDIVKTKV FKDFSELEPDKFQNKTNGITPRRWLLLCNPGLAELIAEKIGEDYVKDLSQ LTKLHSFLGDDVFLRELAKVKQENKLKFSQFLETEYKVKINPSSMFDVQV KRIHEYKRQLLNCLHVITMYNRIKKDPKKLFVPRTVIIGGKAAPGYHMAK MIIKLITSVADVVNNDPMVGSKLKVIFLENYRVSLAEKVIPATDLSEQIS TAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRIDD VAALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPKQPDLFKDIINMLFY HDRFKVFADYEAYVKCQDKVSQLYMNPKAWNMVLKNIAASGKFSSDRTIK EYAQNIWNVEPSDLKISLSNESNKVNGN

  • Molecular Weight

    101 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 the PYGL protein, a key enzyme involved in glycogen metabolism, has gained significant attention due to its fundamental role in regulating glucose homeostasis. PYGL, or glycogen phosphorylase, catalyzes the breakdown of glycogen into glucose-1-phosphate, a critical step in providing energy during periods of fasting or intense physical activity. Dysregulation of PYGL has been linked to various metabolic disorders, including diabetes and glycogen storage diseases, highlighting the importance of understanding its function and regulation. Recent advances in recombinant protein technology have facilitated the production of PYGL for further research, enabling scientists to investigate its structural properties, enzymatic activity, and interaction with regulatory molecules. This research not only promises to augment our understanding of glycogen metabolism but also holds potential for the development of therapeutic strategies aimed at managing metabolic diseases. Through recombination techniques and functional assays, researchers are exploring the biochemical characteristics of PYGL, assessing how mutations impact its activity, and identifying potential inhibitors or activators that could serve as drug candidates. Ultimately, the comprehensive study of PYGL and its reconstituted forms may pave the way for innovative approaches to tackle metabolic disorders associated with glycogen metabolism.

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