Recombinant Human Methionine Aminopeptidase 2 (METAP2) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-10797P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) METAP2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) METAP2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) METAP2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) METAP2.

Recombinant Human Methionine Aminopeptidase 2 (METAP2) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-10797P
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Product Overview

Description Recombinant Human Methionine Aminopeptidase 2 (METAP2) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P50579
Target Symbol METAP2
Synonyms A930035J23Rik; AI047573; AL024412; Amp2; AU014659,; EIF 2 associated p67 homolog; EIF-2-associated p67; Initiation factor 2 associated 67 kDa glycoprotein; Initiation factor 2-associated 67 kDa glycoprotein; MAP 2; MAP2; MAP2_HUMAN; MetAP 2; Metap2; Methionine aminopeptidase 2; Methionyl aminopeptidase 2; MGC102452; MGC127390; MGC53792; MNPEP; p67; p67eIF2; Peptidase M; Peptidase M2
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence AGVEEVAASGSHLNGDLDPDDREEGAASTAEEAAKKKRRKKKKSKGPSAAGEQEPDKESGASVDEVARQLERSALEDKERDEDDEDGDGDGDGATGKKKKKKKKKRGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY
Expression Range 2-478aa
Protein Length Full Length of Mature Protein
Mol. Weight 59.8 kDa
Research Area Metabolism
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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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