Analytical Data
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Gene name
PRRG2
- Application
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Alternative Names
PRRG2；PRGP2；TMG2；Transmembrane gamma-carboxyglutamic acid 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
O14669
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Expression Region
1-86aa
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AA Sequence
MRGHPSLLLL YMALTTCLDT SPSEETDQEV FLGPPEAQSF LSSHTRIPRA NHWDLELLTP GNLERECLEE RCSWEEAREY FEDNTL
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Molecular Weight
36 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
PRRG2, or Proline Rich Gla (G-carboxyglutamic acid) 2, is a protein that has garnered attention in recent years due to its potential roles in various biological processes and disease mechanisms. Research has shown that PRRG2 is involved in cellular signaling pathways, particularly those related to the cellular response to stress and apoptosis. Its expression patterns suggest a critical function in the central nervous system, where it may play a role in neuronal survival and differentiation. Additionally, studies have indicated that PRRG2 may be implicated in the progression of certain cancers and neurodegenerative diseases. The recombinant form of PRRG2 has become a valuable tool in these studies, allowing scientists to investigate its biochemical properties, interactions with other proteins, and functional roles in live systems. By producing and characterizing PRRG2 in vitro, researchers aim to elucidate its mechanisms of action and potential therapeutic targets, paving the way for innovative treatments in conditions where PRRG2 is a contributing factor. As the understanding of PRRG2 expands, it holds promise for enhancing our knowledge of complex biological networks and developing new strategies for therapeutic intervention.
