Analytical Data
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Gene name
NRIP2
- Application
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Alternative Names
NRIP2；Nuclear receptor-interacting Protein 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
Q9BQI9
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Expression Region
1-281aa
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AA Sequence
MLFIFPLSLP WRPSCWKESC STGQRQAGRS REDSVTPPPS SPWPTPPAGA MSTKQEARRD EGEARTRGQE AQLRDRAHLS QQRRLKQATQ FLHKDSADLL PLDSLKRLGT SKDLQPRSVI QRRLVEGNPN WLQGEPPRMQ DLIHGQESRR KTSRTEIPAL LVNCKCQDQL LRVAVDTGTQ YNRISAGCLS RLGLEKRVLK ASAGDLAPGP PTQVEQLELQ LGQETVVCSA QVVDAESPEF CLGLQTLLSL KCCIDLEHGV LRLKAPFSEL PFLPLYQEPG Q
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Molecular Weight
31.3 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
Related Products
Protein Description
NRIP2, or Nuclear Receptor Interacting Protein 2, is a crucial player in the regulation of gene transcription and cellular signaling pathways. Its involvement in various biological processes, including metabolism, immune response, and cellular differentiation, has garnered significant attention in recent years. Research indicates that NRIP2 interacts with multiple nuclear receptors and co-regulators, thereby influencing the expression of target genes. Abnormalities in NRIP2 expression and function have been implicated in various diseases, including cancer and metabolic disorders, highlighting its potential as a therapeutic target. The characterization of NRIP2 recombinant protein is essential for understanding its biochemical properties, interaction mechanisms, and functional roles within the cell. Studies utilizing recombinant NRIP2 can provide insights into its structural features and aid in the development of novel strategies for modulating its activity in disease contexts. By exploring its interactions with other proteins and regulatory elements, researchers can elucidate the pathways influenced by NRIP2, contributing to a broader understanding of molecular mechanisms underlying health and disease. Thus, the study of NRIP2 recombinant protein represents a significant advancement in molecular biology and therapeutic development, paving the way for innovative treatments that harness the power of this important regulatory protein.
