Cat: PA2000-1450

Recombinant Human CUL2 Protein,His

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Analytical Data

  • Gene name

    CUL2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CUL2;Cullin-2

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q13617

  • Expression Region

    1-745aa

  • AA Sequence

    MSLKPRVVDF DETWNKLLTT IKAVVMLEYV ERATWNDRFS DIYALCVAYP EPLGERLYTE TKIFLENHVR HLHKRVLESE EQVLVMYHRY WEEYSKGADY MDCLYRYLNT QFIKKNKLTE ADLQYGYGGV DMNEPLMEIG ELALDMWRKL MVEPLQAILI RMLLREIKND RGGEDPNQKV IHGVINSFVH VEQYKKKFPL KFYQEIFESP FLTETGEYYK QEASNLLQES NCSQYMEKVL GRLKDEEIRC RKYLHPSSYT KVIHECQQRM VADHLQFLHA ECHNIIRQEK KNDMANMYVL LRAVSTGLPH MIQELQNHIH DEGLRATSNL TQENMPTLFV ESVLEVHGKF VQLINTVLNG DQHFMSALDK ALTSVVNYRE PKSVCKAPEL LAKYCDNLLK KSAKGMTENE VEDRLTSFIT VFKYIDDKDV FQKFYARMLA KRLIHGLSMS MDSEEAMINK LKQACGYEFT SKLHRMYTDM SVSADLNNKF NNFIKNQDTV IDLGISFQIY VLQAGAWPLT QAPSSTFAIP QELEKSVQMF ELFYSQHFSG RKLTWLHYLC TGEVKMNYLG KPYVAMVTTY QMAVLLAFNN SETVSYKELQ DSTQMNEKEL TKTIKSLLDV KMINHDSEKE DIDAESSFSL NMNFSSKRTK FKITTSMQKD TPQEMEQTRS AVDEDRKMYL QAAIVRIMKA RKVLRHNALI QEVISQSRAR FNPSISMIKK CIEVLIDKQY IERSQASADE YSYVA

  • Molecular Weight

    86.9 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

CUL2 (Cullin 2) is a key component of the cullin-RING E3 ubiquitin ligase complex, which plays a crucial role in the ubiquitin-proteasome system for protein degradation. This system is essential for regulating various cellular processes, including cell cycle progression, signal transduction, and response to stress. Abnormalities in CUL2 function have been linked to several diseases, including cancer, where disrupted protein degradation can lead to the accumulation of oncogenic factors. Research on CUL2 has gained momentum due to its implications in disease mechanisms and potential therapeutic applications. The study of CUL2 recombinant proteins is vital for understanding its structure and function, allowing researchers to elucidate how it interacts with substrate proteins and other components of the E3 ligase complex. Additionally, the generation of recombinant CUL2 provides a platform for the development of inhibitors that can modulate its activity, offering a novel avenue for drug discovery in cancer and other disorders. Understanding the biochemical properties and the regulation of CUL2 is also critical for deciphering its role in the broader context of ubiquitin signaling pathways, further emphasizing the importance of CUL2 in maintaining cellular homeostasis. Overall, CUL2 serves as a significant focus in molecular biology and biochemistry, contributing to the potential development of targeted therapies aimed at restoring normal cellular functions disrupted in disease states.

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