Cat: PAX2000-12149

Recombinant Human TRIM32 Protein,His

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Analytical Data

  • Gene name

    TRIM32

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    72 kda Tat interacting Protein; 72 kDa Tat-interacting Protein; BBS11 ; E3 ubiquitin-Protein ligase TRIM32; HT2A; LGMD2H ; Limb girdle muscular dystrophy 2H (autosomal recessive); Limb girdle muscular dystrophy 2H; Muscular dystrophy Hutterite type; TAT interactive Protein 72KD; TATIP ; TRI32_HUMAN; Trim32; Tripartite Motif Containing Protein 32; Tripartite motif-containing Protein 32; Zinc finger Protein HT2A

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q13049

  • Expression Region

    2-653 aa

  • AA Sequence

    AAAAASHLN LDALREVLEC PICMESFTEE QLRPKLLHCG HTICRQCLEK LLASSINGVR CPFCSKITRI TSLTQLTDNL TVLKIIDTAG LSEAVGLLMC RSCGRRLPRQ FCRSCGLVLC EPCREADHQP PGHCTLPVKE AAEERRRDFG EKLTRLRELM GELQRRKAAL EGVSKDLQAR YKAVLQEYGH EERRVQDELA RSRKFFTGSL AEVEKSNSQV VEEQSYLLNI AEVQAVSRCD YFLAKIKQAD VALLEETADE EEPELTASLP RELTLQDVEL LKVGHVGPLQ IGQAVKKPRT VNVEDSWAME ATASAASTSV TFREMDMSPE EVVASPRASP AKQRGPEAAS NIQQCLFLKK MGAKGSTPGM FNLPVSLYVT SQGEVLVADR GNYRIQVFTR KGFLKEIRRS PSGIDSFVLS FLGADLPNLT PLSVAMNCQG LIGVTDSYDN SLKVYTLDGH CVACHRSQLS KPWGITALPS GQFVVTDVEG GKLWCFTVDR GSGVVKYSCL CSAVRPKFVT CDAEGTVYFT QGLGLNLENR QNEHHLEGGF SIGSVGPDGQ LGRQISHFFS ENEDFRCIAG MCVDARGDLI VADSSRKEIL HFPKGGGYSV LIREGLTCPV GIALTPKGQL LVLDCWDHCI KIYSYHLRRY STP

  • Molecular Weight

    71.9 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

TRIM32, a member of the tripartite motif (TRIM) family of proteins, has garnered significant attention in the realm of molecular biology and neurobiology due to its diverse functional roles in cellular processes. Originally identified for its involvement in the regulation of muscle differentiation and its linkage to certain muscular dystrophies, TRIM32 has since been implicated in various cellular pathways, including apoptosis, autophagy, and immune responses. Notably, TRIM32's E3 ubiquitin ligase activity facilitates the post-translational modification of target proteins, thereby influencing their stability and function. Recent studies have highlighted its critical role in the pathogenesis of neurodegenerative diseases, particularly in the context of protein misfolding and aggregation, such as in cases of Parkinson's disease and Alzheimer's disease. Additionally, TRIM32 has been shown to interact with key molecular players in the central nervous system, suggesting its potential as a therapeutic target. The reconstitution of TRIM32 protein and subsequent functional assays can provide invaluable insights into its biological significance and pave the way for novel therapeutic strategies aimed at mitigating diseases associated with TRIM32 dysregulation. Thus, understanding the precise mechanisms and signaling pathways modulated by TRIM32 remains a vibrant area of research with implications across multiple fields of medicine and biology.

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