Cat: IPD-X41714

Recombinant Rat Trim2 Protein ,His

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Analytical Data

  • Gene name

    Trim2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (E3 ubiquitin-protein ligase TRIM2)(RING-type E3 ubiquitin transferase TRIM2)

  • Species

    Rat

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    D3ZQG6

  • Expression Region

    1-744aa

  • Molecular Weight

    85.5 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.

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Protein Description

Trim2, a member of the tripartite motif (TRIM) family of proteins, has garnered significant interest in recent years due to its potential roles in various cellular processes, including cell signaling, differentiation, and immune responses. This protein features a distinct structure characterized by a RING domain, one or two B-box domains, and a coiled-coil region, allowing it to function as an E3 ubiquitin ligase. The dysregulation of Trim2 has been linked to several pathological conditions, including neurodegenerative diseases and cancer, highlighting its importance in maintaining cellular homeostasis. Previous studies have indicated that Trim2 plays a crucial role in modulating the degradation of key signaling molecules, thereby influencing cellular functions and responses to external stimuli. Furthermore, research has suggested that Trim2 may facilitate autophagy and have implications in neuroinflammation and neuronal survival. As the understanding of Trim2's multifaceted roles expands, it presents a promising target for therapeutic interventions. Experimental approaches, including genetic manipulation and proteomic analyses, have been employed to elucidate Trim2's mechanisms of action and its interactions with various substrates. This emerging knowledge underscores the need for continued research into Trim2 and its involvement in health and disease, providing insights that could pave the way for novel therapeutic strategies in conditions where Trim2 activity is altered.

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