PAM Protein (Transcript Variant 3) (Myc-DYKDDDDK Tag)
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- Target See all PAM Proteins
- PAM (Peptidylglycine alpha-Amidating Monooxygenase (PAM))
- Protein Type
- Recombinant
- Biological Activity
- Active
- Protein Characteristics
- Transcript Variant 3
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Origin
- Human
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Source
- HEK-293 Cells
- Purification tag / Conjugate
- This PAM protein is labelled with Myc-DYKDDDDK Tag.
- Application
- Antibody Production (AbP), Functional Studies (Func), Protein Interaction (PI), Standard (STD)
- Specificity
- Optimal preservation of protein structure, post-translational modifications and functions.
- Characteristics
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- Recombinant human PAM (transcript variant 3) protein expressed in HEK293 cells.
- Produced with end-sequenced ORF clone
- Tested for bioactivity.
- Purity
- > 80 % as determined by SDS-PAGE and Coomassie blue staining
- Biological Activity Comment
- The specific activity of PAM was determined by measuring the product D-Tyr-Val-NH2 formation from a conversion of D-Tyr-Val-Gly. The reaction was carried out at 37C for 60min in the buffer containing 50 mM MES, pH6.0, 1 μM CuCl2, 2000 units/ml of Catalase, 5 mM L-ascorbic acid, and 50 uM of D-Tyr-Val-Gly as the substrate
- Top Product
- Discover our top product PAM Protein
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- Application Notes
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Recombinant human proteins can be used for:
Native antigens for optimized antibody production
Positive controls in ELISA and other antibody assays
Protein-protein interaction
In vitro biochemical assays and cell-based functional assays - Comment
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The tag is located at the C-terminal.
- Restrictions
- For Research Use only
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- Concentration
- > 50 μg/mL
- Buffer
- 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10 % glycerol.
- Storage
- -80 °C
- Storage Comment
- Store at -80°C. Thaw on ice, aliquot to individual single-use tubes, and then re-freeze immediately. Only 2-3 freeze thaw cycles are recommended.
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- Target
- PAM (Peptidylglycine alpha-Amidating Monooxygenase (PAM))
- Alternative Name
- Pam (PAM Products)
- Background
- Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity. [UniProtKB/Swiss-Prot Function]
- Molecular Weight
- 94.2 kDa
- NCBI Accession
- NP_620176
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