Analytical Data
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Gene name
PSKH2
- Application
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Alternative Names
PSKH2Serine/threonine-protein kinase H2; EC 2.7.11.1; Protein serine kinase H2; PSK-H2
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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
Q96QS6
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Expression Region
1-385 aa
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AA Sequence
MGCGASRKVV PGPPALAWAK HEGQNQAGVG GAGPGPEAAA QAAQRIQVAR FRAKFDPRVL ARYDIKALIG TGSFSRVVRV EQKTTKKPFA IKVMETRERE GREACVSELS VLRRVSHRYI VQLMEIFETE DQVYMVMELA TGGELFDRLI AQGSFTERDA VRILQMVADG IRYLHALQIT HRNLKPENLL YYHPGEESKI LITDFGLAYS GKKSGDWTMK TLCGTPEYIA PEVLLRKPYT SAVDMWALGV ITYALLSGFL PFDDESQTRL YRKILKGKYN YTGEPWPSIS HLAKDFIDKL LILEAGHRMS AGQALDHPWV ITMAAGSSMK NLQRAISRNL MQRASPHSQS PGSAQSSKSH YSHKSRHMWS KRNLRIVESP LSALL
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Molecular Weight
43.0 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
PSKH2, or protein serine kinase H2, is a serine/threonine kinase that plays a pivotal role in various cellular processes, including cell cycle regulation and apoptosis. The study of PSKH2 has gained traction due to its implications in cancer biology and other diseases. Research indicates that PSKH2 is involved in phosphorylating key substrates that regulate essential signaling pathways, such as those related to cell growth and survival. Understanding the structure and function of PSKH2 is crucial, as its dysregulation has been linked to tumorigenesis and poor prognosis in several cancers. The recombinant expression of PSKH2 allows researchers to investigate its biochemical properties and identify potential inhibitors that could serve as therapeutic agents. Furthermore, the ability to produce PSKH2 in a recombinant system facilitates the exploration of its interaction with other proteins, contributing to a deeper understanding of its role in cellular signaling networks. As cancer therapy increasingly focuses on targeted approaches, elucidating the functions of PSKH2 could pave the way for novel treatments aimed at disrupting its aberrant activity in cancer cells. Overall, the ongoing research into PSKH2 as a recombinant protein holds promise for both basic science and potential clinical applications in oncology.
