Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
SGPP1 (F2B6W) Rabbit mAb #96703
Filter:
- WB
- IP
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 35 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Description
| MW (kDa) | 35 |
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Flow Cytometry (Fixed/Permeabilized) | 1:50 - 1:200 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
SGPP1 (F2B6W) Rabbit mAb recognizes endogenous levels of total SGPP1 protein.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala78 of human SGPP1 protein.
Background
Sphingosine kinases (SPHKs) catalyze the phosphorylation of sphingosine to form sphingosine-1-phosphate (S1P), a lipid mediator that affects various cellular functions, including immune response, neurogenesis, and angiogenesis (1). Sphingosine-1-phosphate phosphatase 1 (SGPP1) dephosphorylates S1P back to sphingosine, which is then readily converted to ceramide in the endoplasmic reticulum (ER) (2). The activity balance between SPHKs and SGPP1 is crucial for regulating sphingolipid metabolites and their downstream effects (3). SGPP1 overexpression results in elevated ceramide levels, which ultimately promotes apoptosis (4). Conversely, SGPP1 depletion increases S1P levels and induces autophagy and ER stress (5). Elevated S1P due to SGPP1 loss may also provide cellular resistance to cytotoxic agents, and SGPP1 has been found to be downregulated in gastric cancer and multiple myeloma (MM) (6-8).
- Bravo, G.Á. et al. (2022) Cells 11, 2058. doi: 10.3390/cells11132058.
- Giussani, P. et al. (2006) Mol Cell Biol 26, 5055-69.
- Le Stunff, H. et al. (2007) J Biol Chem 282, 34372-80.
- Le Stunff, H. et al. (2002) J Cell Biol 158, 1039-49.
- Lépine, S. et al. (2011) Cell Death Differ 18, 350-61.
- Johnson, K.R. et al. (2003) J Biol Chem 278, 34541-7.
- Gao, X.Y. et al. (2015) Oncol Rep 34, 1977-87.
- Petrusca, D.N. et al. (2022) Cancers (Basel) 14, 772. doi: 10.3390/cancers14030772.
限制使用
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