Mouse Anti-METAP2 (AA 2-212) Recombinant Antibody (CBFYM-2112) (CBMAB-M2294-FY)

Name: Mouse Anti-METAP2 (AA 2-212) Recombinant Antibody (CBFYM-2112)
SKU: CBMAB-M2294-FY
Rating: 5 (1 reviews)

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Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

CBFYM-2112

Application

FC, IF, IHC-P, WB

Immunogen

Human recombinant protein fragment corresponding to amino acids 2-212 of human METAP2 (NP_006829) produced in E. coli

Specificity

Human

Antibody Isotype

IgG1

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

Concentration

1 mg/mL

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Epitope

AA 2-212

More Infomation

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

10988

UniProt ID

P50579

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.

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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

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