Myeloperoxidase (MPO) (NM_000250) Human 3' UTR Clone

Specifications

Product Data
Product Name	Myeloperoxidase (MPO) (NM_000250) Human 3' UTR Clone
Vector	pMirTarget
ACCN	NM_000250
Insert Size	831 bp
Sequence Data	Insert Sequence (showhide) >SC210009 3’UTR clone of NM_000250 The sequence shown below is from the reference sequence of NM_000250. The complete sequence of this clone may contain minor differences, such as SNPs. Blue=Stop Codon Red=Cloning site GGCAAGTTGGACGCCCGCAAGATCCGCGAGATTCTCATTAAGGCCAAGAAGGGCGGAAAGATCGCCGTG TAACAATTGGCAGAGCTCAGAATTCAAGCGATCGCC AACCTGGCTTCCTGGAGGGAAGCCTCCTAGAGGCCAGGTAAGGGGGTGCAGCAGTGAGGGGTATATCTG GGCTGGCCAGTTGGAACCACGGAGATCTCCTTGCCCTAGATGAGCCCAGCCCTGTTCTGGGTGCAGCTG AGAAAATGAGTGACTAGACGTTCATTTGTGTGCTCATGTATGTGCGAAGTATATAAATTGGCTTTTCAT GCGTGTGTGTTGTCTGAACATGGGGAGTGTTTCATGGGTTATGTGTATGTGCCATTTATGTGAGTGTGT GTTTGTGCTGATGAGAATACTGAGTATGTGGAAGGCAGCAGAGCGGACTGGTGAGGAGCACAGCTCAGG AACTAGACTGCCTGGGTTCCAATCCTGGCTCTGTGGCTTGCTAGCTATGTGACCTTGAGCAAATTACCC TCCTTAAACAAGAGTTTTCTTCCTTGTAAATTACATCTGTCATGGTTTCTTGGAGGGCCCACTTGTATC CTCTGGTTCTTCATTTATTGAGCACCTACTACATGCAAGGCACTGTACTAGGCGTGAGAAGCATATAGA GGCAAGAAAGAGATACCAAGATGCCATCTGTGTCCTGGTTAGCAGAGCTGGACCAGTGGTGCCTTGGAG GGATAAGCCAGCTGCAGCTGGGCTGTGTGGTTGACTTATGGGCCCAGCCAGCCAGGCTCAGGCCATGGC TCCCCTTTTTCTTCCTCACCCTGATTTCTTGCTTATTCACTGAAGTTCTCCTGAAGAGGAACTGGGCCT GTTGCCCTTTCTGTACCATTTATTTGCTCCCAATGTTTATGATAATAAAGGCACCGCTGATGGGGACCT CCA 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_000250.2
Summary	Myeloperoxidase (MPO) is a heme protein synthesized during myeloid differentiation that constitutes the major component of neutrophil azurophilic granules. Produced as a single chain precursor, myeloperoxidase is subsequently cleaved into a light and heavy chain. The mature myeloperoxidase is a tetramer composed of 2 light chains and 2 heavy chains. This enzyme produces hypohalous acids central to the microbicidal activity of neutrophils. [provided by RefSeq, Nov 2014]
Locus ID	4353
MW	30.9

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