MTHFD1 (NM_005956) Human 3' UTR Clone
CAT#: SC203448
3' UTR clone of methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1 methenyltetrahydrofolate cyclohydrolase formyltetrahydrofolate synthetase (MTHFD1) for miRNA target validation
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CNY 4,845.00
货期*
3周
规格
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经常一起买 (2)
Specifications
Product Data | |
Product Name | MTHFD1 (NM_005956) Human 3' UTR Clone |
Vector | pMirTarget |
Synonyms | CIMAH; MTHFC; MTHFD |
ACCN | NM_005956 |
Insert Size | 301 bp |
Sequence Data |
>SC203448 3’UTR clone of NM_005956
The sequence shown below is from the reference sequence of NM_005956. The complete sequence of this clone may contain minor differences, such as SNPs. Blue=Stop Codon Red=Cloning site GGCAAGTTGGACGCCCGCAAGATCCGCGAGATTCTCATTAAGGCCAAGAAGGGCGGAAAGATCGCCGTG TAACAATTGGCAGAGCTCAGAATTCAAGCGATCGCC GAAACAGAACAGGTGAATGGATTATTCTAAACAGATCACCATCCATCTTCAAGAAGCTACTTTGAAAGT CTGGCCAGTGTCTATTCAGGCCCACTGGGAGTTAGGAAGTATAAGTAAGCCAAGAGAAGTCAGCCCCTG CCCAGAAGATCTGAAACTAATAGTAGGAGTTTCCCCAGAAGTCATTTTCAGCCTTAATTCTCATCATGT ATAAATTAACATAAATCATGCATGTCTGTTTACTTTAGTGACGTTCCACAGAATAAAAGGAAACAAGTT TGCCATCTTGGTGTTGCAATATGAA ACGCGTAAGCGGCCGCGGCATCTAGATTCGAAGAAAATGACCGACCAAGCGACGCCCAACCTGCCATCA CGAGATTTCGATTCCACCGCCGCCTTCTATGAAAGG |
Restriction Sites | SgfI-MluI |
OTI Disclaimer | Our molecular clone sequence data has been matched to the sequence identifier above as a point of reference. Note that the complete sequence of this clone is largely the same as the reference sequence but may contain minor differences , e.g., single nucleotide polymorphisms (SNPs). |
Reference Data | |
RefSeq | NM_005956.4 |
Synonyms | CIMAH; MTHFC; MTHFD |
Summary | This gene encodes a protein that possesses three distinct enzymatic activities, 5,10-methylenetetrahydrofolate dehydrogenase, 5,10-methenyltetrahydrofolate cyclohydrolase and 10-formyltetrahydrofolate synthetase. Each of these activities catalyzes one of three sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses. The trifunctional enzymatic activities are conferred by two major domains, an aminoterminal portion containing the dehydrogenase and cyclohydrolase activities and a larger synthetase domain. [provided by RefSeq, Jul 2008] |
Locus ID | 4522 |
MW | 11.3 |
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