Analytical Data
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Gene name
GPRIN2
- Application
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Alternative Names
GPRIN2; KIAA0514G protein-regulated inducer of neurite outgrowth 2; GRIN2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60269
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Expression Region
1-461aa
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AA Sequence
MSSSHPEPGPWAPLSPRLQPLSQSSSSLLGEGREQRPELHKTASSTMWQAQLGEASTRPQAPEEEGNPPESMKPARASGPKARPSAGGHWRSSTVGNVSTMGGGDLCRLRAPSAAAMQRSHSDLVRSTQMRGHSGARKASLSCSALGSSPVHRAQLQPGGTSGQGGQAPAGLERDLAPEDETSNSAWMLGASQLSVPPLDLGDTTAHSSSAQAEPKAAEQLATTTCHALPPAALLCGMREMREVGAGGCCHALPATGILAFPKLVASVSESGLQAQHGVKIHCRLSGGLPGHSHCCAHLWGPAGLVPEPGSRTKDVWTMTSANDLAPAEASPLSAQDAGVQAAPVAACKAVATSPSLEAPAALHVFPEVTLGSSLEEAPSPVRDVRWDAEGMTWEVYGAAVDPEVLGVAIQKHLEMQFEQLQRAPASEDSLSVEGRRGPLRAVMQSLRRPSCCGCSGAAPE
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Molecular Weight
74.1 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
GPRIN2, or G-protein Regulation and Interacting Protein 2, is a protein implicated in modulating various cellular processes, including signal transduction and cytoskeletal dynamics. Research into GPRIN2 has gained momentum due to its potential role in cellular signaling pathways, particularly those associated with G-protein-coupled receptors (GPCRs), which are crucial in numerous physiological responses and disease mechanisms. Abnormalities in GPRIN2 expression have been linked to various pathological conditions, including cancer and neurodegenerative diseases. The study of GPRIN2 recombinant proteins has provided valuable insights into its structural and functional characteristics, enabling scientists to explore its interactions with other cellular proteins and its regulatory functions. Advances in recombinant protein technology, such as the use of expression systems like E. coli and yeast, have facilitated the production of GPRIN2 for biochemical assays and structural studies. Understanding GPRIN2's role at the molecular level may reveal novel therapeutic targets for diseases where GPCR signaling is disrupted. Moreover, the elucidation of its interaction partners can provide a deeper understanding of the cellular signaling networks, enhancing our knowledge of both normal physiology and disease pathology. Thus, the ongoing research on GPRIN2 recombination proteins is critical for advancing our understanding of GPCR-related diseases and developing targeted interventions.
