Analytical Data
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Gene name
TRABD
- Application
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Alternative Names
TRABD; TTG2; PP2447; TraB domain-containing Protein; Protein TTG2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H4I3
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Expression Region
1-376 aa
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AA Sequence
MDGEEQQPPH EANVEPVVPS EASEPVPRVL SGDPQNLSDV DAFNLLLEMK LKRRRQRPNL PRTVTQLVAE DGSRVYVVGT AHFSDDSKRD VVKTIREVQP DVVVVELCQY RVSMLKMDES TLLREAQELS LEKLQQAVRQ NGLMSGLMQM LLLKVSAHIT EQLGMAPGGE FREAFKEASK VPFCKFHLGD RPIPVTFKRA IAALSFWQKV RLAWGLCFLS DPISKDDVER CKQKDLLEQM MAEMIGEFPD LHRTIVSERD VYLTYMLRQA ARRLELPRAS DAEPRKCVPS VVVGVVGMGH VPGIEKNWST DLNIQEIMTV PPPSVSGRVS RLAVKAAFFG LLGYSLYWMG RRTASLVLSL PAAQYCLQRV TEARHK
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Molecular Weight
42.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
TRABD (TGF-β Receptor-Associated Protein with a Binds Domain) is a protein implicated in various cellular processes, including the regulation of immune responses and cellular signaling pathways. Recent studies have highlighted its crucial role in the modulation of TGF-β signaling, which is significant in cancer progression, fibrosis, and immune system disorders. Given that TGF-β signaling frequently becomes dysregulated in many diseases, understanding the function and mechanisms of TRABD can provide novel insights into potential therapeutic targets. Researchers have begun to explore the structural characteristics of TRABD through recombinant protein expression, allowing for detailed functional assays and interaction studies. Moreover, the generation of TRABD recombinant proteins is pivotal for elucidating its binding partners, post-translational modifications, and effects on downstream signaling pathways. The ongoing investigation into TRABD's role in health and disease is likely to reveal new avenues for targeted interventions in conditions where TGF-β signaling plays a detrimental role. Consequently, TRABD has emerged as a significant focus in molecular biology and therapeutic development, highlighting the importance of recombinant protein studies in advancing our understanding of complex biological systems.
