<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
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.
SDS-PAGE
55 kDa, reducing conditions
Publications
Read Publications using 8424-VF in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
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.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human PBEF/Visfatin Protein, CF
EC 2.4.2.12
MGC117256
NAmPRTase
NAMPT
nicotinamide phosphoribosyltransferase
NMPRTase
PBEF
PBEF1
PBEF1110035O14Rik
PBEF1DKFZp666B131
Pre-B cell-enhancing factor
pre-B-cell colony enhancing factor 1
Pre-B-cell colony-enhancing factor 1
VF
Visfatin
Background
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).
Wang, T. et al. (2006) Nat. Struct. Mol. Biol. 13:661.
Samal, B. et al. (1994) Mol. Cell. Biol. 14:1431.
Rongvaux, A. et al. (2002) Eur. J. Immunol. 32:3225.
Revollo, J.R. et al. (2007) Cell Metab. 6:363.
Ognjanovic, S. and G.D. Bryant-Greenwood (2002) Am. J. Obstet. Gynecol. 187:1051.
Tanaka, M. et al. (2007) Biochem. Biophys. Res. Commun. 359:194.
Rongvaux, A. et al. (2008) J. Immunol. 181:4685.
Kim, S.R. et al. (2007) Biochem. Biophys. Res. Commun. 357:150.
Sun, Z. et al. (2013) Cytokine Growth Factor Rev. 24:433.
Shackelford, R.E. et al. (2013) Genes Cancer 4:447.
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