Analytical Data
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Gene name
MINA
- Application
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Alternative Names
RIOX2;MDIG;MINA;MINA53;Ribosomal oxygenase 2
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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
Q8IUF8
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Expression Region
1-465aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL DSVVRLQFKD HIVLTVLPDQ DQSDETQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV
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Molecular Weight
55 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
MINA (Mina53) is a pivotal protein involved in various cellular processes, particularly in the regulation of ribosome biogenesis and cellular stress response. Initially identified in the context of the nucleolus, MINA has garnered attention due to its role in maintaining cellular homeostasis and facilitating the assembly of ribosomal components, essential for protein synthesis. Its expression is tightly regulated, with altered levels associated with several pathophysiological conditions, including cancer and cellular aging. Research into MINA has revealed its involvement in cell cycle regulation, apoptosis, and the response to oxidative stress, suggesting that it acts as a crucial mediator of cellular signaling pathways. Understanding the structural and functional aspects of MINA is essential for elucidating its biological roles and potential as a therapeutic target. Ongoing studies focus on the mechanisms by which MINA interacts with other cellular proteins, its post-translational modifications, and how these processes influence tumorigenesis and the development of other diseases. In recent years, advances in structural biology, including techniques like X-ray crystallography and cryo-electron microscopy, have facilitated deeper insights into MINA's conformational dynamics and binding properties. As research expands, MINA is increasingly recognized not only for its contribution to understanding fundamental cellular biology but also for its potential implications in designing novel interventions for diseases linked to dysregulated protein synthesis and ribosome assembly.
