Analytical Data
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Gene name
TRSPAP1
- Application
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Alternative Names
1110007F05Rik; AA387999; FLJ20503; PRO1902; RP4 669K10.4; SECp43; tRNA selenocysteine 1-associated Protein 1; tRNA selenocysteine associated Protein 1; tRNA selenocysteine-associated Protein 1; Trnau1ap; TRSPAP1; TSAP1_HUMAN; WI1 2643G14.2
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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
Q9NX07
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Expression Region
1-287 aa
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AA Sequence
MAASLWMGDL EPYMDENFIS RAFATMGETV MSVKIIRNRL TGIPAGYCFV EFADLATAEK CLHKINGKPL PGATPAKRFK LNYATYGKQP DNSPEYSLFV GDLTPDVDDG MLYEFFVKVY PSCRGGKVVL DQTGVSKGYG FVKFTDELEQ KRALTECQGA VGLGSKPVRL SVAIPKASRV KPVEYSQMYS YSYNQYYQQY QNYYAQWGYD QNTGSYSYSY PQYGYTQSTM QTYEEVGDDA LEDPMPQLDV TEANKEFMEQ SEELYDALMD CHWQPLDTVS SEIPAMM
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Molecular Weight
32.4 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
TRSPAP1 (Tryptophan-rich protein 1) is a protein of increasing interest in the field of molecular biology and biochemistry due to its potential role in various physiological and pathological processes. Originally identified in studies focused on tryptophan metabolism and its implications in neurobiology, TRSPAP1 has garnered attention for its involvement in cellular signaling pathways, particularly in response to stress and inflammation. Research has suggested that TRSPAP1 may play a significant role in modulating immune responses and cellular homeostasis, making it a candidate for further investigation in immunological disorders and neurodegenerative diseases. Moreover, its unique structure, characterized by an abundance of tryptophan residues, raises questions about its functionality in protein-protein interactions and potential effects on cellular processes. Current studies aim to elucidate the biochemical properties of TRSPAP1, explore its expression patterns in various tissues, and determine its functional significance in health and disease. Consequently, understanding TRSPAP1's mechanisms of action could reveal novel insights into therapeutic targets for conditions linked to inflammatory and metabolic dysregulation. As research progresses, the potential implications of TRSPAP1 in clinical applications continue to expand, highlighting the importance of this protein in both basic and applied biomedical sciences.
