Analytical Data
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Gene name
PTPRR
- Application
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Alternative Names
PTPRR；ECPTP；PTPRQ；Receptor-type tyrosine-Protein phosphatase R
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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
Q05B41
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Expression Region
1-412aa
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AA Sequence
MILHRLKERFQLSLRQDKEKNQEIHLSPITLQPALSEAKTVHSMVQPEQAPKVLNVVVDPQGRGAPEIKATTATSVCPSPFKMKPIGLQKRRGSNVSLTLDMSSLGNIEPFVSIPTPREKVAMEYLQSASRILTRSQLRDVVASSHLLQSEFMEIPMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHALCLYESRLSAETVQ
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Molecular Weight
53.5 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
PTPRR, or Protein Tyrosine Phosphatase Receptor Type R, is a member of the receptor-type phosphatase family, which plays a crucial role in regulating various cellular processes, including cell growth, differentiation, and signal transduction. Research on PTPRR has garnered attention due to its involvement in several pathological conditions, particularly in cancer and neurodegenerative diseases. The protein is known to dephosphorylate specific tyrosine residues on target proteins, thereby influencing key signaling pathways. Recent studies have suggested that PTPRR may function as a tumor suppressor in certain contexts, with altered expression levels observed in various cancer types. Furthermore, its role in the central nervous system highlights its potential implications in neurological disorders. As such, characterizing the structure and function of PTPRR, including the development of recombinant protein variants, is vital for understanding its biological activity and therapeutic potential. The generation of PTPRR recombinant proteins allows researchers to investigate their enzymatic properties, interactions with other molecules, and role in signaling pathways, paving the way for potential clinical applications in targeted therapies and personalized medicine. Overall, the study of PTPRR and its recombinant forms is an expanding field that may lead to novel insights into the mechanisms of disease and opportunities for innovative treatment strategies.
