Recombinant Human MetAP2 Protein (N-6His)

Beta LifeScience SKU/CAT #: BL-1645NP
BL-1645NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
BL-1645NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human MetAP2 Protein (N-6His)

Beta LifeScience SKU/CAT #: BL-1645NP
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Product Overview

Description Recombinant Human Methionine Aminopeptidase 2 is produced by our Baculovirus expression system and the target gene encoding Ala2-Tyr478 is expressed with a 6His tag at the N-terminus.
Accession P50579
Synonym Methionine aminopeptidase 2; MAP 2; MetAP 2; p67; p67eIF2; Peptidase M; METAP2; MAP2
Gene Background Human Methionine Aminopeptidase 2 (METAP2, MAP2) is a member of the M24 family of metalloproteases. METAPs catalyze the removal of the initiator methionine residue from nascent peptides and are essential for cell growth. 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. METAP2 plays an important role in the development of different types of cancer and has been a novel target for developing anti-cancer drugs. This protein functions both by protecting the alpha subunit of eukaryotic initiation factor 2 from inhibitory phosphorylation and by removing the amno-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.
Molecular Mass 53.6 KDa
Apmol Mass 66-80 KDa, reducing conditions
Formulation Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 500mM NaCl, 10% Glycerol, pH 8.0.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution
Storage Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target 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.
Subcellular Location Cytoplasm. Note=About 30% of expressed METAP2 associates with polysomes.
Protein Families Peptidase M24A family, Methionine aminopeptidase eukaryotic type 2 subfamily
Database References

Gene Functions References

  1. MetAP1 and MetAP2 have roles in driving cell selectivity for a potent anti-cancer agent in synergy, by controlling glutathione redox state PMID: 27542228
  2. Suggest MetAP2 as important regulator of proliferation/apoptosis in non-small cell lung cancers. PMID: 26935506
  3. Nt-acetylation prevents the excision of the initiator methionine by MetAP2. PMID: 25886145
  4. Data indicate that methionine aminopeptidase 2 (MetAP2) contains a single disulfide bond that exists in oxidized and reduced states and influences enzyme function. PMID: 24700462
  5. The activity of unmodified, nitrated and oxidised METAP2 was assessed and it was found that nitration significantly reduced its ability to cleave a chromogenic substrate. Mass spectrometry analysis identified Tyr336 as a nitrated residue in METAP2. PMID: 24041691
  6. Increased expression of METAP2 is associated with pilocytic astrocytoma. PMID: 23161775
  7. This study demonstrated a hitherto-undescribed role of MetAP2 in definitive hematopoiesis and a possible link to noncanonical Wnt and ERK signaling. PMID: 21937698
  8. the substrate specificities of Escherichia coli MetAP1, human MetAP1, and human MetAP2 were systematically profiled PMID: 20521764
  9. Data indicate that MetAP2 expression and pp60c-src phosphorylation were decreased in NC2213 treated cells. PMID: 19703310
  10. the functional role of S100A4 in regulating endothelial cell growth and tumor metastasis involves interaction with the N-terminal half of Methionine Aminopeptidase 2. PMID: 11994292
  11. High expression in germinal center B cells and their neoplastic counterparts. PMID: 12118091
  12. Divalent metal cofactors are physiologically relevant for activity of this enzyme. PMID: 12718546
  13. MetAP protein has a role in colorectal adenocarcinoma progression PMID: 15102683
  14. Expressed in colon cancer cells PMID: 15336565
  15. MetAP-1 and MetAP-2 have essential functions in the control of mammalian cell proliferation PMID: 15962312
  16. A comparison of the structual differences between Type I and Type II methionine aminopeptidases. PMID: 16274222
  17. Data suggest that methionine aminopeptidase 2 plays a role in the proliferation of fibroblasts and myofibroblasts in fibrotic lung diseases and may serve as a novel pharmacologic target in idiopathic pulmonary fibrosis. PMID: 17446530
  18. MetAP2 plays an important role in tumor cell growth and may contribute to tumorigenesis PMID: 18264137
  19. Discovery, identification, and characterization of candidate pharmacodynamic markers of METAP2 inhibition are reported. PMID: 18828628
  20. Using bovine cell extract, fumagillin was found to be bound by methionine aminopeptidase (MetAP-2). PMID: 9177176

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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