ECHS1 (NM_004092) Human Tagged ORF Clone Lentiviral Particle
SKU
RC200369L4V
Lenti ORF particles, ECHS1 (mGFP-tagged) - Human enoyl CoA hydratase, short chain, 1, mitochondrial (ECHS1), nuclear gene encoding mitochondrial protein, 200ul, >10^7 TU/mL
Product Data | |
Type | Human Tagged ORF Clone Lentiviral Particle |
---|---|
Tag | mGFP |
Target Symbol | ECHS1 |
Synonyms | ECHS1D; SCEH |
Vector | pLenti-C-mGFP-P2A-Puro |
Mammalian Cell Selection | Puromycin |
Sequence Data |
ORF Nucleotide Sequence
The ORF insert of this clone is exactly the same as(RC200369).
|
ACCN | NM_004092 |
ORF Size | 870 bp |
OTI Disclaimer | The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info |
OTI Annotation | This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene. |
Shipping | Dry Ice |
Reference Data | |
RefSeq | NM_004092.2 |
RefSeq Size | 1350 bp |
RefSeq ORF | 873 bp |
Locus ID | 1892 |
UniProt ID | P30084 |
Cytogenetics | 10q26.3 |
Domains | ECH |
Protein Pathways | beta-Alanine metabolism, Butanoate metabolism, Fatty acid elongation in mitochondria, Fatty acid metabolism, leucine and isoleucine degradation, Limonene and pinene degradation, Lysine degradation, Metabolic pathways, Propanoate metabolism, Tryptophan metabolism, Valine |
MW | 31.4 kDa |
Summary | The protein encoded by this gene functions in the second step of the mitochondrial fatty acid beta-oxidation pathway. It catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs. The gene product is a member of the hydratase/isomerase superfamily. It localizes to the mitochondrial matrix. Transcript variants utilizing alternative transcription initiation sites have been described in the literature. [provided by RefSeq, Jul 2008] |
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