Analytical Data
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Gene name
tig
- Application
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Alternative Names
tig；PEIG1；TIG1；Retinoic acid receptor responder Protein 1
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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
B7UJQ9
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Expression Region
1-432aa
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AA Sequence
MQVSVETTQGLGRRVTITIAADSIETAVKSELVNVAKKVRIDGFRKGKVPMNIVAQRYGASVRQDVLGDLMSRNFIDAIIKEKINPAGAPTYVPGEYKLGEDFTYSVEFEVYPEVELQGLEAIEVEKPIVEVTDADVDGMLDTLRKQQATWKEKDGAVEAEDRVTIDFTGSVDGEEFEGGKASDFVLAMGQGRMIPGFEDGIKGHKAGEEFTIDVTFPEEYHAENLKGKAAKFAINLKKVEERELPELTAEFIKRFGVEDGSVEGLRAEVRKNMERELKSAIRNRVKSQAIEGLVKANDIDVPAALIDSEIDVLRRQAAQRFGGNEKQALELPRELFEEQAKRRVVVGLLLGEVIRTNELKADEERVKGLIEEMASAYEDPKEVIEFYSKNKELMDNMRNVALEEQAVEAVLAKAKVTEKETTFNELMNQQA
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Molecular Weight
50.2 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
TIG recombinant proteins, derived from the TIG (trypsin inhibitor globulin) family, have garnered significant attention in biological and biomedical research due to their unique structural properties and versatile functional roles. These proteins are known for their ability to inhibit serine proteases, which play crucial roles in various physiological processes, including digestion, immune responses, and cell signaling. The investigation into TIG recombinant proteins has been motivated by their potential therapeutic applications, particularly in developing novel anti-inflammatory and anticancer agents. Advances in molecular cloning and protein expression technologies have enabled researchers to produce these proteins with enhanced purity and activity, facilitating the exploration of their molecular mechanisms and interaction with target proteases. Furthermore, studies have highlighted the potential of TIG proteins in modulating pathological conditions, thus opening avenues for innovative treatments. As a result, ongoing research is focused on characterizing the functional dynamics of TIG recombinant proteins, elucidating their roles in disease mechanisms, and leveraging their properties for drug development and therapeutic interventions.
