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PDF Rabbit pAb (APR18082N)

CAT: 0882-APR18082N-01Size: 50 µLDry Ice: NoHazardous: No
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CAT#:0882-APR18082N-01Size:50 µL
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Background
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.
Overview
We constantly strive to ensure we provide our customers with the best antibodies. As a result of this work we offer this antibody in purified format. We are in the process of updating our datasheets. If you have any questions regarding this update, please feel free to contact our technical support team. This product is a high quality PDF Rabbit pAb (APR18073N8) .
Synonyms
PDF
Gene ID
64146
UniProt
Q9HBH1
Cellular Locus
Mitochondrion
Dilution
WB 1:500 - 1:2000
Form
Liquid
Buffer
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Molecular Weight
Calculated MW: 27kDa Observed MW: 20kDa
Storage Conditions
Store at 4°C short term. For long-term storage, aliquot and store at -20°C or below. Stable for 12 months at -20°C. Avoid repeated freeze-thaw cycles.
Gene ID URL
https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=64146
Uniprot URL
https://www.uniprot.org/uniprot/Q9HBH1
AA Sequence
EGPALRRSYWRHLRRLVLGPPEPPFSHVCQVGDPVLRGVAAPVERAQLGGPELQRLTQRLVQVMRRRRCVGLSAPQLGVPRQVLALELPEALCRECPPRQRALRQMEPFPLRVFVNPSLRVLDSRLVTFPEGCESVAGFLACVPRFQAVQISGLDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMDSRTFTNVYWMKVND

UniProtKB · Q9HBH1

Peptide deformylase, mitochondrial

DEFM_HUMAN · Homo sapiens

View on UniProt ↗
Primary accession
Q9HBH1
Review status
UniProtKB reviewed (Swiss-Prot)
Gene
PDF
Protein existence
1: Evidence at protein level
Organism
Homo sapiens (Human)
Taxonomy ID
9606
Alternative names
—
EC number
3.5.1.88
Processing
Precursor
Secondary accessions
Q8WUN6
Protein keywords

Technical term

3D-structureProteomics identificationReference proteome

Ligand

CobaltMetal-binding

Molecular function

Hydrolase

Cellular component

Mitochondrion

Biological process

Protein biosynthesis

Domain

Transit peptide