Analytical Data
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Gene name
MIDN
- Application
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Alternative Names
Midnolin; Midbrain nucleolar protein; MIDN
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Species
Human
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Source
E. coli
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Tag
C-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q504T8
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Expression Region
M1-A468
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AA Sequence
MEPQPGGARSCRRGAPGGACELGPAAEAAPMSLAIHSTTGTRYDLAVPPDETVEGLRKRLSQRLKVPKERLALLHKDTRLSSGKLQEFGVGDGSKLTLVPTVEAGLMSQASRPEQSVMQALESLTETQVSDFLSGRSPLTLALRVGDHMMFVQLQLAAQHAPLQHRHVLAAAAAAAAARGDPSIASPVSSPCRPVSSAARVPPVPTSPSPASPSPITAGSFRSHAASTTCPEQMDCSPTASSSASPGASTTSTPGASPAPRSRKPGAVIESFVNHAPGVFSGTFSGTLHPNCQDSSGRPRRDIGTILQILNDLLSATRHYQGMPPSLAQLRCHAQCSPASPAPDLAPRTTSCEKLTAAPSASLLQGQSQIRMCKPPGDRLRQTENRATRCKVERLQLLLQQKRLRRKARRDARGPYHWSPSRKAGRSDSSSSGGGGSPSEASGLGLDFEDSVWKPEVNPDIKSEFVVA
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Protein Length
Full Length
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Molecular Weight
60 kDa, based on SDS-PAGE under reducing conditions
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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
MIDN (Midline 1) is a protein that has drawn considerable attention in recent years due to its potential role in various biological processes and diseases. Initially identified as a midline morphogen in embryonic development, MIDN's function extends beyond developmental biology, influencing cellular differentiation and migration. Recent studies have implicated MIDN in the modulation of inflammatory responses, tumorigenesis, and neurodegenerative diseases, highlighting its potential as a therapeutic target. The reorganization of MIDN into recombinant proteins has become a focal point in research, allowing for detailed investigation of its structure-function relationships. By producing MIDN in a controlled environment, researchers aim to elucidate its interactions at the molecular level and assess its implications in pathological conditions. These efforts are critical for understanding how MIDN contributes to disease mechanisms and developing novel strategies for intervention. The advancement of recombinant DNA technology and protein expression systems has facilitated the production of MIDN derivatives, providing valuable tools for probing its biological significance and exploring potential applications in drug development and gene therapy. As research progresses, MIDN is poised to become a vital component in the formulation of innovative therapeutic approaches, underscoring the importance of continued exploration into its multifaceted roles in health and disease.
