GDPD5 Antibody
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Application
| WB, IF, E, IHC-P |
|---|---|
| Primary Accession | Q8WTR4 |
| Other Accession | NP_110419, 189571657 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | 68586 Da |
| Concentration (mg/ml) | 1 mg/mL |
| Conjugate | Unconjugated |
| Application Notes | GDPD5 antibody can be used for detection of GDPD5 by Western blot at 1 - 2 µg/ml. Antibody can also be used for Immunohistochemistry at 5 µg/mL. For Immunoflorescence start at 20 µg/mL. |
| Gene ID | 81544 |
|---|---|
| Other Names | Glycerophosphodiester phosphodiesterase domain-containing protein 5, 3.1.-.-, Glycerophosphodiester phosphodiesterase 2, GDPD5, GDE2 |
| Target/Specificity | GDPD5; GDPD5 antibody is human, mouse and rat reactive. At least three isoforms of GDPD5 are known to exist. |
| Reconstitution & Storage | GDPD5 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. |
| Precautions | GDPD5 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | GDPD5 (HGNC:28804) |
|---|---|
| Function | Ecto-phospholipase that cleaves the phosphodiester bond in the glycosylphosphatidylinositol (GPI) anchor of various proteins, releasing them from the plasma membrane into the extracellular space (PubMed:27693046, PubMed:31932507, PubMed:33731436). Cleaves the GPI- anchor of glypican-6/GPC6, thereby positively regulating neuron differentiation in a cell-autonomous manner (PubMed:27693046, PubMed:31932507). May also hydrolyze the GPI-anchor of glypican-3/GPC3 (PubMed:27693046). Cleaves the GPI-anchor of the serine protease inhibitor RECK, leading to its inactivation (PubMed:33731436). RECK inactivation inhibits NOTCH signaling in neighboring cells and induces differentiation of spinal motor neurons (By similarity). RECK inactivation can also regulate amyloid-beta precursor protein (APP) processing by ADAM10 (PubMed:33731436). May additionally catalyze the hydrolysis of the phosphodiester bond in sn-glycerol 3-phosphocholine, potentially contributing to osmotic regulation of cellular glycerophosphocholine levels (By similarity). |
| Cellular Location | Cell membrane; Multi-pass membrane protein. Membrane raft; Multi-pass membrane protein. Cell projection, growth cone {ECO:0000250|UniProtKB:Q640M6}. Note=Colocalizes with recycling endosome as it undergoes constitutive clathrin- and dynamin-mediated internalization and recycling. |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
The glycerophosphodiester phosphodiesterase domain containing 5 (GDPD5) protein, also known as GDE2, is a seven transmembrane, widely expressed protein (1) that is necessary for spinal motor neuron differentiation and retinoid-induced neuronal outgrowth (2,3). Altered choline phospholipid metabolism is a hallmark of cancer, and the elevated expression of GDPD5 correlates with malignant choline phospholipid metabolite profiles in human breast cancer (4).
REFERENCES
Nogusa Y, Fujioka Y, Komatsu R, et al. Isolation and characterization of two serpentine membrane proteins containing glycerophosphodiester phosphodiesterase, GDE2 and GDE6. Gene 2004; 337:173-9.
Rao M and Sockanathan S. Transmembrane protein GDE2 induces motor neuron differentiation in vivo. Science 2005; 309:2212-5.
Yanaka N, Nogusa Y, Fujioka Y, et al. Involvement of membrane protein GDE2 in retinoic acid-induced neurite formation in Neuro2A cells. FEBS Lett. 2007; 581:712-8.
Cao MD, Dopkens M, Krishnamachary B, et al. Glycerophosphodiester phosphodiesterase domain containing 5 (GDPD5) expression correlates with malignant choline phospholipid metabolite profiles in human breast cancer. NMR Biomed. 2012; 25:1033-42.
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