Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to induce VEGF secretion by PC‑3 human prostate cancer cells. The ED50 for this effect is 1-5 μg/mL |
Source | E. coli-derived human PBEF/Visfatin protein Asn2-His491, with an N-terminal Met and 6-His tag |
Accession # | |
N-terminal Sequence | Met |
Protein/Peptide Type | Recombinant Proteins |
Gene | NAMPT |
Purity | >90%, by SDS-PAGE with silver staining. |
Purity Statement | Antigen Affinity-purified |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 56 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 55 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in HEPES, NaCl, EDTA, TCEP and Tween. |
Purity | >90%, by SDS-PAGE with silver staining. |
Reconstitution Instructions | Reconstitute at 500 μg/mL in sterile PBS. |
PBEF, also called Visfatin and NAMPT, is a dimeric type II phosphoribosyltransferase (1). It was initially identified as a secreted cytokine that synergized with IL-7 and SCF to stimulate early stage B cells (2). Human PBEF is predominantly expressed in bone marrow, liver, and muscle, with lower levels found in placenta, kidney, heart, and lung (2). Human PBEF shares 96% and 95% amino acid sequence identity with mouse and rat PBEF, respectively. PBEF has been identified both as an intracellular and as an extracellular protein. Within the cell, PBEF converts nicotinamide to nicotinamide mononucleotide (NMN), which is the rate limiting step in the production of nicotinamide adenine dinucleotide (NAD+) (3, 4). In the extracellular environment, PBEF has been reported to increase the production of inflammatory cytokines and have an important role in the development of T and B cells (5-7). Additionally, PBEF may promote angiogenesis in vivo in an ERK1/2-dependent manner (8). PBEF has been implicated in several inflammatory diseases, including rheumatoid arthritis, osteoarthritis, inflammatory bowel disease, and sepsis (9). PBEF over‑expression has been observed in many cancer types (10).
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