Analytical Data
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Gene name
STRAP
- Application
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Alternative Names
STRAP；MAWD；UNRIP；Serine-threonine kinase receptor-associated Protein
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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
Q9Y3F4
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Expression Region
1-350aa
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AA Sequence
MAMRQTPLTCSGHTRPVVDLAFSGITPYGYFLISACKDGKPMLRQGDTGDWIGTFLGHKGAVWGATLNKDATKAATAAADFTAKVWDAVSGDELMTLAHKHIVKTVDFTQDSNYLLTGGQDKLLRIYDLNKPEAEPKEISGHTSGIKKALWCSEDKQILSADDKTVRLWDHATMTEVKSLNFNMSVSSMEYIPEGEILVITYGRSIAFHSAVSLDPIKSFEAPATINSASLHPEKEFLVAGGEDFKLYKYDYNSGEELESYKGHFGPIHCVRFSPDGELYASGSEDGTLRLWQTVVGKTYGLWKCVLPEEDSGELAKPKIGFPETTEEELEEIASENSDCIFPSAPDVKA
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Molecular Weight
65.4 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
Related Products
Protein Description
STRAP (Serine/Threonine-Protein Kinase Activator) is a protein that has garnered significant interest in recent years due to its role in various cellular processes, including cell growth, differentiation, and apoptosis. It serves as a cofactor for several signaling pathways, particularly those involving kinases that are crucial in the regulation of the cell cycle and stress responses. The dysregulation of STRAP has been implicated in numerous diseases, including cancer, where it can influence tumor progression and sensitivity to therapy. Researchers have focused on understanding the structure and function of STRAP, as well as its interactions with other proteins, to elucidate its biological roles further. Furthermore, characterizing STRAP as a recombinant protein allows for the use of advanced techniques to study its properties in vitro and in vivo. This research is critical for developing novel therapeutic strategies targeting STRAP-related pathways, potentially leading to improved treatments for various malignancies and other diseases characterized by abnormal cell signaling. The exploration of STRAP not only enhances our understanding of fundamental biological processes but also provides insight into its potential as a biomarker or therapeutic target.
