Analytical Data
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Gene name
EMC2
- Application
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Alternative Names
EMC2；KIAA0103；TTC35;ER membrane Protein complex subunit 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
Q15006
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Expression Region
2-297aa
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AA Sequence
AKVSELYDV TWEEMRDKMR KWREENSRNS EQIVEVGEEL INEYASKLGD DIWIIYEQVM IAALDYGRDD LALFCLQELR RQFPGSHRVK RLTGMRFEAM ERYDDAIQLY DRILQEDPTN TAARKRKIAI RKAQGKNVEA IRELNEYLEQ FVGDQEAWHE LAELYINEHD YAKAAFCLEE LMMTNPHNHL YCQQYAEVKY TQGGLENLEL SRKYFAQALK LNNRNMRALF GLYMSASHIA SNPKASAKTK KDNMKYASWA ASQINRAYQF AGRSKKETKY SLKAVEDMLE TLQITQS
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Molecular Weight
2-297aa
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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
EMC2 (ER membrane protein complex subunit 2) is a key component of the endoplasmic reticulum (ER) membrane protein complex, which plays a crucial role in the biogenesis and maintenance of membrane proteins. The study of EMC2 and its functionalities is pivotal due to its involvement in the process of folding and inserting proteins into the membrane, which is essential for cellular homeostasis and signaling pathways. Research indicates that mutations or dysfunctions in EMC2 can lead to various diseases, including neurodegenerative disorders and metabolic syndromes. Moreover, understanding the molecular mechanisms of EMC2 can provide insights into how cells manage stress responses and protein quality control, which is particularly relevant in the context of diseases associated with protein misfolding. Recent advancements in structural biology have enabled scientists to elucidate the three-dimensional structure of EMC2, revealing potential binding sites for substrates and helping to map out its interactions within the complex. This progress paves the way for therapeutic strategies aimed at correcting EMC2-related dysfunctions, making it a significant focus of ongoing biomedical research. Through these studies, researchers aim not only to unveil the intricate functions of EMC2 but also to explore its potential as a target for drug development in various pathologies.
