Product Name	PDF1A
Chinese Name	肽脱甲酰基酶PDF抗体
Alias	PDF; CG6496; DEFM_HUMAN; mitochondrial; Pdf; PDF1A; Peptide deformylase; Peptide deformylase like protein; Peptide deformylase, mitochondrial; Polypeptide deformylase.
Research Area	Tumour  Cell biology  Cell differentiation  Epigenetics
Immunogen Species	Rabbit
Clonality	Polyclonal
React Species	(predicted: Human, Mouse, Rat, Pig, Cow, Sheep, )
Applications	ELISA=1:5000-10000 IHC-P=1:100-500 IHC-F=1:100-500 ICC=1:100-500 IF=1:100-500 （Paraffin sections need antigen repair） not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user.
Theoretical molecular weight	23kDa
Cellular localization	cytoplasmic
Form	Liquid
Concentration	1mg/ml
immunogen	KLH conjugated synthetic peptide derived from human PDF1A: 121-220/243
Lsotype	IgG
Purification	affinity purified by Protein A
Buffer Solution	0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
Storage	Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.
Attention	This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
PubMed	PubMed
Product Detail	Protein synthesis proceeds after formylation of methionine by methionyl-tRNA formyl transferase (FMT) and transfer of the charged initiator f-met tRNA to the ribosome. In eubacteria and eukaryotic organelles the product of this gene, peptide deformylase (PDF), removes the formyl group from the initiating methionine of nascent peptides. In eubacteria, deformylation of nascent peptides is required for subsequent cleavage of initiating methionines by methionine aminopeptidase. The discovery that a natural inhibitor of PDF, actinonin, acts as an antimicrobial agent in some bacteria has spurred intensive research into the design of bacterial-specific PDF inhibitors. In human cells, only mitochondrial proteins have N-formylation of initiating methionines. Protein inhibitors of PDF or siRNAs of PDF block the growth of cancer cell lines but have no effect on normal cell growth. In humans, PDF function may therefore be restricted to rapidly growing cells. [provided by RefSeq, Nov 2008] Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Subcellular Location: Mitochondrion. Tissue Specificity: Ubiquitous. Similarity: Belongs to the polypeptide deformylase family. SWISS: Q9HBH1 Gene ID: 64146 Database links: Entrez Gene: 64146 Human SwissProt: Q9HBH1 Human Unigene: 130849 Human

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