Analytical Data
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Gene name
IDP
- Application
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Alternative Names
IDP；U8 snoRNA-decapping enzyme
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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
P48735
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Expression Region
40-452aa
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AA Sequence
A DKRIKVAKPV VEMDGDEMTR IIWQFIKEKL ILPHVDIQLK YFDLGLPNRD QTDDQVTIDS ALATQKYSVA VKCATITPDE ARVEEFKLKK MWKSPNGTIR NILGGTVFRE PIICKNIPRL VPGWTKPITI GRHAHGDQYK ATDFVADRAG TFKMVFTPKD GSGVKEWEVY NFPAGGVGMG MYNTDESISG FAHSCFQYAI QKKWPLYMST KNTILKAYDG RFKDIFQEIF DKHYKTDFDK NKIWYEHRLI DDMVAQVLKS SGGFVWACKN YDGDVQSDIL AQGFGSLGLM TSVLVCPDGK TIEAEAAHGT VTRHYREHQK GRPTSTNPIA SIFAWTRGLE HRGKLDGNQD LIRFAQMLEK VCVETVESGA MTKDLAGCIH GLSNVKLNEH FLNTTDFLDT IKSNLDRALG RQ
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Molecular Weight
50.9 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
IDP (Intrinsically Disordered Protein) research has gained significant attention in recent years due to its unique structural properties and functional versatility. Unlike traditional proteins that adopt stable three-dimensional structures, IDPs are characterized by a lack of fixed conformation, allowing them to exist in multiple states. This intrinsic disorder is associated with a wide range of biological functions, including regulation of cellular processes, signaling, and interactions with various biomolecules. IDPs play crucial roles in diverse cellular contexts, influencing processes such as gene expression, cell differentiation, and stress response. Their flexible nature enables them to act as molecular switches, responding dynamically to environmental changes. Moreover, disordered regions in proteins are often linked to various diseases, including neurodegenerative disorders and cancers, highlighting their importance in biomedical research. As our understanding of IDP dynamics and interactions deepens, novel therapeutic strategies targeting these proteins are being explored. The study of IDPs represents a paradigm shift in protein research, challenging traditional concepts of structure-function relationships and opening new avenues for drug discovery and the development of biomolecular tools.
