Analytical Data
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Gene name
ECHDC1
- Application
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Alternative Names
ECHDC1;Ethylmalonyl-CoA decarboxylase
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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
Q9NTX5
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Expression Region
1-307aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MALKQEMAKS LLKTASLSGR TKLLHQTGLS LYSTSHGFYE EEVKKTLQQF PGGSIDLQKE DNGIGILTLN NPSRMNAFSG VMMLQLLEKV IELENWTEGK GLIVRGAKNT FSSGSDLNAV KSLGTPEDGM AVCMFMQNTL TRFMRLPLIS VALVQGWALG GGAEFTTACD FRLMTPESKI RFVHKEMGII PSWGGTTRLV EIIGSRQALK VLSGALKLDS KNALNIGMVE EVLQSSDETK SLEEAQEWLK QFIQGPPEVI RALKKSVCSG RELYLEEALQ NERDLLGTVW GGPANLEAIA KKGKFNKGGAEFTTACD FRLMTPESKI RFVHKEMGII PSWGGTTRLV EIIGSRQALK VLSGALKLDS KNALNIGMVE EVLQSSDETK SLEEAQEWLK QFIQGPPEVI RALKKSVCSG RELYLEEALQ NERDLLGTVW GGPANLEAIA KKGKFNK
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Molecular Weight
36 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
ECHDC1, or enoyl-CoA hydratase domain-containing protein 1, is a crucial enzyme involved in the metabolic pathways of fatty acids, particularly in the peroxisomal β-oxidation route. Research has highlighted its role in the catabolism of very long-chain fatty acids, linking it to various metabolic disorders and mitochondrial dysfunctions. Mutations in the ECHDC1 gene have been associated with conditions such as childhood-onset insulin resistance and neurological disorders. The recombinant production of ECHDC1 has garnered interest among researchers aiming to understand its biochemical properties and structural characteristics, which can elucidate its specific functions within cellular metabolism. By studying the protein in a controlled laboratory setting, scientists can explore its enzyme kinetics, substrate specificity, and interaction with other metabolic enzymes. This research holds potential implications for the development of therapeutic strategies for metabolic diseases linked to ECHDC1 deficiencies. Moreover, understanding how ECHDC1 functions at the molecular level can provide insights into the broader landscape of fatty acid metabolism, paving the way for innovative treatments for related pathologies. As the demand for recombinant proteins in both basic and applied research continues to grow, ECHDC1 represents a compelling target for biochemical studies that aim to clarify the complexities of energy metabolism in human health and disease.











