Analytical Data
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Gene name
IER2
- Application
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Alternative Names
IER2；ETR101；PIP92；Immediate early response gene 2 Protein
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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
Q9BTL4
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Expression Region
1-223aa
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AA Sequence
MEVQKEAQRIMTLSVWKMYHSRMQRGGLRLHRSLQLSLVMRSARELYLSAKVEALEPEVSLPAALPSDPRLHPPREAESTAETATPDGEHPFPEPMDTQEAPTAEETSACCAPRPAKVSRKRRSSSLSDGGDAGLVPSKKARLEEKEEEEGASSEVADRLQPPPAQAEGAFPNLARVLQRRFSGLLNCSPAAPPTAPPACEAKPACRPADSMLNVLVRAVVAF
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Molecular Weight
24.1 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
IER2 (Immediate Early Response 2) is a protein that plays a crucial role in cellular responses to various stimuli, including stress and growth factors. Initially identified as an immediate early gene, IER2 is involved in vital processes such as cell proliferation, differentiation, and apoptosis. Research has indicated that IER2 may be implicated in various physiological and pathological conditions, including cancer, where its expression levels are often altered. Understanding the molecular mechanisms underlying IER2 function is essential for deciphering its role in disease progression and developing potential therapeutic strategies. To further investigate IER2, researchers have focused on the generation of recombinant IER2 proteins, enabling in-depth studies of its structure, function, and interactions with other cellular components. By producing IER2 in a controlled laboratory setting, scientists can explore its biochemical properties and potential as a biomarker or therapeutic target. This recombinant approach also facilitates high-throughput screening for small molecules that may modulate IER2 activity, offering insights into its therapeutic potential. Overall, the study of recombinant IER2 is not only vital for understanding its biological significance but also holds promise for the development of innovative treatments for diseases associated with its dysregulation.
