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Rabbit Anti-METAP2 Recombinant Antibody (CBFYM-2113) (CBMAB-M2295-FY)


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Summary

Host Animal
Rabbit
Specificity
Human, Monkey, Mouse, Rat
Clone
CBFYM-2113
Antibody Isotype
IgG
Application
WB

Basic Information

Immunogen
Synthetic peptide corresponding to residues surrounding Gly390 of human MetAP2
Specificity
Human, Monkey, Mouse, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
HEPES, pH 7.5, 0.15 M NaCl, 0.01% BSA, 50% glycerol
Preservative
0.02% Sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Methionyl Aminopeptidase 2
Introduction
The protein encoded by this gene is a member of the methionyl aminopeptidase family. The encoded 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 proteins. Increased expression of this gene is associated with various forms of cancer, and the anti-cancer drugs fumagillin and ovalicin inhibit the protein by irreversibly binding to its active site. Inhibitors of this gene have also been shown to be effective for the treatment of obesity. A pseudogene of this gene is located on chromosome 2. Several transcript variants encoding different isoforms have been found for this gene.
Entrez Gene ID
Human10988
Mouse56307
Rat64370
Monkey712400
UniProt ID
HumanP50579
MouseO08663
RatP38062
MonkeyH9Z4P2
Alternative Names
Methionyl Aminopeptidase 2; Initiation Factor 2-Associated 67 KDa Glycoprotein; Peptidase M; P67eIF2; MNPEP; Testicular Tissue Protein Li 17; EIF-2-Associated P67 Homolog; Methionine Aminopeptidase 2
Function
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human METAP2 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.

Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.
Biological Process
N-terminal protein amino acid modification Source: HGNC-UCL
Peptidyl-methionine modification Source: HGNC-UCL
Protein initiator methionine removal Source: UniProtKB-UniRule
Protein processing Source: HGNC-UCL
Cellular Location
Cytoplasm
Note: About 30% of expressed METAP2 associates with polysomes.
PTM
Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding.
More Infomation

Zhang, K., Hu, J., & Zhao, Z. (2023). Fumagillin regulates stemness and malignancies in cancer stem-like cells derived from liver cancer via targeting to MetAP-2. Plos one, 18(7), e0289024.

Birgül, K., Uba, A. I., Çuhadar, O., Sevinç, S. K., Tiryaki, S., Tiber, P. M., ... & Küçükgüzel, Ş. G. (2022). Synthesis and molecular modeling of MetAP2 of thiosemicarbazides, 1, 2, 4-triazoles, thioethers derived from (S)-Naproxen as possible breast cancer agents. Journal of Molecular Structure, 1259, 132739.

Demers, M., Sturtevant, S., Guertin, K. R., Gupta, D., Desai, K., Vieira, B. F., ... & Light, D. R. (2021). MetAP2 inhibition modifies hemoglobin S to delay polymerization and improves blood flow in sickle cell disease. Blood Advances, 5(5), 1388-1402.

Shaikh, S. K. J., Kamble, R. R., Bayannavar, P. K., Somagond, S. M., & Joshi, S. D. (2020). Triazolothiadizepinylquinolines as potential MetAP-2 and NMT inhibitors: Microwave-assisted synthesis, pharmacological evaluation and molecular docking studies. Journal of Molecular Structure, 1203, 127445.

He, W. P., Guo, Y. Y., Yang, G. P., Lai, H. L., Sun, T. T., Zhang, Z. W., ... & Yang, G. F. (2020). CHD1L promotes EOC cell invasiveness and metastasis via the regulation of METAP2. International Journal of Medical Sciences, 17(15), 2387.

Siddik, M. A. B., Das, B. C., Weiss, L., Dhurandhar, N. V., & Hegde, V. (2019). A MetAP2 inhibitor blocks adipogenesis, yet improves glucose uptake in cells. Adipocyte, 8(1), 240-253.

Heinrich, T., Seenisamy, J., Becker, F., Blume, B., Bomke, J., Dietz, M., ... & Zenke, F. T. (2019). Identification of methionine aminopeptidase-2 (MetAP-2) inhibitor M8891: A clinical compound for the treatment of cancer. Journal of Medicinal Chemistry, 62(24), 11119-11134.

Heinrich, T., Seenisamy, J., Blume, B., Bomke, J., Calderini, M., Eckert, U., ... & Zenke, F. T. (2019). Discovery and structure-based optimization of next-generation reversible methionine aminopeptidase-2 (MetAP-2) inhibitors. Journal of medicinal chemistry, 62(10), 5025-5039.

Farrell, P. J., Zopf, C. J., Huang, H. J., Balakrishna, D., Holub, C., Bilakovics, J., ... & Larson, C. J. (2019). Using target engagement biomarkers to predict clinical efficacy of MetAP2 inhibitors. Journal of Pharmacology and Experimental Therapeutics, 371(2), 299-308.

Huang, H. J., Holub, C., Rolzin, P., Bilakovics, J., Fanjul, A., Satomi, Y., ... & Farrell, P. J. (2019). MetAP2 inhibition increases energy expenditure through direct action on brown adipocytes. Journal of Biological Chemistry, 294(24), 9567-9575.

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For research use only. Not intended for any clinical use.

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