Analytical Data
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Gene name
PRAK
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简介
PRAK/MAPKAPK5 protein, a serine/threonine kinase, responds to cellular stress and pro-inflammatory cytokines and acts as a tumor suppressor through MAP kinases (including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta) activated by phosphorylation. Initially located in the nucleus, upon activation, it moves to the cytoplasm and phosphorylates the heat shock protein HSP27. PRAK Protein, Human (sf9, Strep) is the recombinant human-derived PRAK protein, expressed by Sf9 insect cells, with C-Strep labeled tag.
- Application
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Species
Human
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Source
Baculovirus
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Tag
C-Strep
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
NP_003659
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Expression Region
M1-Q471
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Protein Length
Full Length
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Molecular Weight
35-45 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
PRAK (p53-regulated protein kinase) is a crucial serine/threonine kinase that plays a significant role in cellular responses to stress and has been implicated in various physiological processes, including cell survival, differentiation, and apoptosis. Originally identified as a target of the tumor suppressor protein p53, PRAK is involved in the activation of the MKK3/MKK6-p38 MAPK signaling pathway, which modulates the cellular response to stressors such as DNA damage, inflammation, and oxidative stress. Research on PRAK has gained momentum due to its potential implications in cancer biology, where its regulatory functions can influence tumor progression and treatment responses. Additionally, understanding the precise molecular mechanisms through which PRAK exerts its effects can facilitate the development of targeted therapies that may enhance cancer treatment efficacy. Recent studies have also highlighted PRAK’s involvement in other diseases, including neurodegenerative disorders and metabolic syndromes, suggesting broader biological significance beyond cancer. Given its multifaceted roles, the study of PRAK and its interactions within cellular signaling networks is essential for elucidating its contributions to both health and disease, making it a compelling target for future therapeutic interventions and biomarker development.
