Analytical Data
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Gene name
MPPED1
- Application
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Alternative Names
MPPED1; C22orf1; FAM1A; Metallophosphoesterase domain-containing protein 1; EC 3.1.-.-; Adult brain protein 239; 239AB
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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
O15442
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Expression Region
1-326 aa
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AA Sequence
MWRSRWDASV LKAEALALLP CGLGMAFSQS HVMAARRHQH SRLIIEVDEY SSNPTQAFTF YNINQGRFQP PHVQMVDPVP HDAPKPPGYT RFVCVSDTHS RTDPIQMPYG DVLIHAGDFT ELGLPSEVKK FNEWLGSLPY EYKIVIAGNH ELTFDQEFMA DLIKQDFYYF PSVSKLKPEN YENVQSLLTN CIYLQDSEVT VRGFRIYGSP WQPWFYGWGF NLPRGQALLE KWNLIPEGVD ILITHGPPLG FLDWVPKKMQ RVGCVELLNT VQRRVQPRLH VFGHIHEGYG VMADGTTTYV NASVCTVNYQ PVNPPIVIDL PTPRNS
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Molecular Weight
37.2 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
MPPED1 (M-phase phosphoprotein 1) is a protein involved in various cellular processes, particularly during the M-phase of the cell cycle. It has garnered interest in cancer research due to its potential role in mitotic regulation and cell proliferation. Recent studies suggest that MPPED1 may be implicated in oncogenic pathways, making it a candidate for understanding tumorigenesis and developing targeted therapies. Its expression is often dysregulated in various cancers, leading researchers to explore its functional significance in cell division and its interactions with other crucial proteins. The recombinant expression of MPPED1 allows for a detailed analysis of its biochemical properties and biological functions, thereby providing insights into its role in both normal physiology and disease states. Furthermore, studying MPPED1 in a controlled research setting can facilitate the discovery of novel therapeutic targets and strategies aimed at modulating its activity, especially in malignancies where its function is altered. The ability to produce and analyze recombinant MPPED1 protein is crucial for elucidating its structure-function relationships and understanding its contribution to cellular mechanisms that underlie cancer progression. This research direction not only helps in comprehending the fundamental aspects of cell cycle regulation but also paves the way for potential innovations in oncology, highlighting the importance of MPPED1 as a focus of scientific investigation.
