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MTIF2 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P46199 |
|---|---|
| Clone Names | 100405120 |
| Gene ID | 4528 |
|---|---|
| Other Names | Translation initiation factor IF-2, mitochondrial, IF-2(Mt), IF-2Mt, IF2(mt), MTIF2 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | MTIF2 |
|---|---|
| Function | One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. |
| Cellular Location | Mitochondrion. |
| Tissue Location | Expressed in all tissues examined. Highest level in skeletal muscle |
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Provided below are standard protocols that you may find useful for product applications.
Background
During the initiation of protein biosynthesis, initiationfactor-2 (IF-2) promotes the binding of the initiator tRNA to thesmall subunit of the ribosome in a GTP-dependent manner.Prokaryotic IF-2 is a single polypeptide, while eukaryoticcytoplasmic IF-2 (eIF-2) is a trimeric protein. Bovine livermitochondria contain IF-2(mt), an 85-kD monomeric protein that isequivalent to prokaryotic IF-2. The predicted 727-amino acid humanprotein contains a 29-amino acid presequence. Human IF-2(mt) shares32 to 38% amino acid sequence identity with yeast IF-2(mt) andseveral prokaryotic IF-2s, with the greatest degree of conservationin the G domains of the proteins. Two transcript variants encodingthe same protein have been found for this gene. [provided byRefSeq].
References
Dick, D.M., et al. Am. J. Med. Genet. B Neuropsychiatr. Genet. (2010) In press :Reiling, E., et al. Eur. J. Hum. Genet. 17(8):1056-1062(2009)Miura, E., et al. Plant Cell 19(4):1313-1328(2007)Bouwmeester, T., et al. Nat. Cell Biol. 6(2):97-105(2004)Overman, R.G. Jr., et al. Biochim. Biophys. Acta 1628(3):195-205(2003)
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