Name :
Recombinant Human methionyl aminopeptidase 2/METAP2 Protein (His Tag)
Biological Activity :
Background :
METAP2 (Methionine aminopeptidase 2), also known as MAP2 is a protein that belongs to the peptidase M24A family. MAP2 binds 2 cobalt or manganese ions and contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. It is found in all organisms and is especially important because of its critical role in tissue repair and protein degradation. The catalytic activity of human MAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo. This protein functions both by protecting the alpha subunit of eukaryotic initiation factor 2 from inhibitory phosphorylation and by removing the amino-terminal methionine residue from nascent protein. MAP2 protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. It also plays a critical role in the regulation of protein synthesis.
Biological Activity :
Measure by its ability to remove methionine from a fluorogenic peptide substrate H-Met-Gly-Pro-AMC (Catalog # ES017). The resulting GP-AMC is cleaved by Recombinant Human DPPIV/CD26 (Catalog # 1180-SE). The specific activity is >15 pmol/min/µg.
Expression Host :
Human
Source :
Baculovirus-Insect Cells
Tag :
Protein Accession No. :
NP_006829.1
NCBI Gene ID :
Synonyms :
Synonyms :
methionyl aminopeptidase 2
Amino Acid Sequence :
Molecular Weight :
The recombinant human METAP2 consists 489 amino acids and predicts a molecular mass of 54.3 kDa.
Purity :
> 85 % as determined by SDS-PAGE.
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg protein as determined by the LAL method.
Protein Construction :
A DNA sequence encoding the human METAP2 (NP_006829.1) (Met1-Tyr478) was expressed with a polyhistidine tag at the C-terminus.
Buffer Solution :
Supplied as sterile 20 mM Tris, 500 mM NaCl, 10 % glycerol, pH 7.4.Please contact us for any concerns or special requirements.Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
Liquid. It is shipped out with blue ice.
Redissolution :
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Synonyms :
MAP2 Protein, Human; MNPEP Protein, Human; p67 Protein, Human; p67eIF2 Protein, Human methionyl aminopeptidase 2/METAP2 背景信息 METAP2 (Methionine aminopeptidase 2), also known as MAP2 is a protein that belongs to the peptidase M24A family. MAP2 binds 2 cobalt or manganese ions and contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. It is found in all organisms and is especially important because of its critical role in tissue repair and protein degradation. The catalytic activity of human MAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo. This protein functions both by protecting the alpha subunit of eukaryotic initiation factor 2 from inhibitory phosphorylation and by removing the amino-terminal methionine residue from nascent protein. MAP2 protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. It also plays a critical role in the regulation of protein synthesis.
References & Citations :
Bennett, et al. (1997) EPR Studies on the Mono- and Dicobalt (II)-Substituted Forms of the Aminopeptidase from Aeromonas proteolytica. Insight into the Catalytic Mechanism of Dinuclear Hydrolases. J Am Chem Soc. 119:1923-33.Johansson, et al. (2008) Dicobalt II-II, II-III, and III-III Complexes as Spectroscopic Models for Dicobalt Enzyme Active Sites. Inorg Chem. 47:5079-92.Bradshaw, et al. (2002) Aminopeptidases and angiogenesis. Essays Biochem. 38: 5-78.
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