Analytical Data
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Gene name
SSU72
- Application
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Alternative Names
SSU72;RNA polymerase II subunit A C-terminal domain phosphatase SSU72
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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
Q9NP77
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Expression Region
1-194aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMPSSPLRVAVVCSSNQNRSMEAHNILS KRGFSVRSFGTGTHVKLPGPAPDKPNVYDFKTTYDQMYNDLLRKDKELYT QNGILHMLDRNKRIKPRPERFQNCKDLFDLILTCEERVYDQVVEDLNSRE QETCQPVHVVNVDIQDNHEEATLGAFLICELCQCIQHTEDMENEIDELLQ EFEEKSGRTFLHTVCFY
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Molecular Weight
25 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
SSU72, a dual-specificity phosphatase, has garnered significant interest in the field of molecular biology due to its role in regulating various cellular processes, particularly those related to gene expression and RNA processing. It is known to dephosphorylate RNA polymerase II, thereby influencing transcriptional regulation and the mRNA maturation process. Understanding SSU72's function is crucial, as dysregulation of its activity is implicated in numerous diseases, including cancer. The recombinant production of SSU72 enables researchers to study its biochemical properties, structure-function relationships, and interactions with other cellular proteins in a controlled environment. Utilizing techniques such as site-directed mutagenesis and X-ray crystallography, scientists aim to elucidate the enzyme's mechanistic pathways and identify potential therapeutic targets. Additionally, the SSU72 protein serves as a valuable model for investigating dual-specificity phosphatases more broadly, contributing to a deeper understanding of their complex roles in cellular signaling networks. Given the therapeutic implications of modulating phosphatase activity, continued research into SSU72 and its recombinant forms is essential, paving the way for novel strategies in treating diseases linked to aberrant phosphatase function.
