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Rabbit Polyclonal Phospho-DRP1 (S637) antibody (STJ91001)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, IHC, ELISA
Recommended dilution: WB 1:500-1:2000; IHC 1:100-1:300; ELISA 1:10000;
Recommended protocols: check protocols
Click or hover above images to see image description for DRP1 (phospho Ser637) Polyclonal Antibody.
Check alternative names for the antibodyExpand
DNM1L antibody, DLP1 antibody, DRP1 antibody,|DLP1 antibody|Dynamin-1-like protein antibody|DYNIV 11 antibody|EMPF antibody|EMPF1 antibody|FLJ41912 antibody|HdynIV antibody|VPS1 antibody|Anti-DRP1 antibody (ab56788)
SCBT cat No: sc-101270|sc-271583|sc-21804|sc-32898|
DRP1 (phospho Ser637) Polyclonal Antibody
|Catalogue No.|| |
Human, Mouse, Rat
Phospho-DRP1 (S637) Polyclonal Antibody detects endogenous levels of DRP1 protein only when phosphorylated at S637.
Synthesized phospho-peptide derived from DRP1 (phospho Ser637) at AA range 580-660
WB, IHC, ELISA
|Recommended dilution|| |
WB 1:500-1:2000; IHC 1:100-1:300; ELISA 1:10000;
|Molecular weight|| |
DRP1 (phospho Ser637) Antibody was tube-contained. Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
DRP1 (phospho Ser637) Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Dynamin-1-like protein antibody, Dnm1p/Vps1p-like protein antibody, DVLP antibody, Dynamin family member proline-rich carboxyl-terminal domain less antibody, Dymple antibody, Dynamin-like protein antibody, Dynamin-like protein 4 antibody, Dynamin-like protein IV antibody, HdynIV antibody, Dynamin-related protein 1 antibody
|Protein names|| |
Dynamin-1-like protein , Dnm1p/Vps1p-like protein , DVLP , Dynamin family member proline-rich carboxyl-terminal domain less , Dymple , Dynamin-like protein , Dynamin-like protein 4 , Dynamin-like protein IV , HdynIV , Dynamin-related protein 1
|Protein function|| |
Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage. Required for normal brain development, including that of cerebellum. Facilitates developmentally regulated apoptosis during neural tube formation. Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues. Also required for mitochondrial fission during mitosis. Required for formation of endocytic vesicles. Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles. Required for programmed necrosis execution. / Isoform 1 and isoform 4 inhibit peroxisomal division when overexpressed. / GTP + H2O = GDP + phosphate. / GTPase activity is increased by binding to phospholipid membranes.
|Protein tissue specificity|| |
Ubiquitously expressed with highest levels found in skeletal muscles, heart, kidney and brain. Isoform 1 is brain-specific. Isoform 2 and isoform 3 are predominantly expressed in testis and skeletal muscles respectively. Isoform 4 is weakly expressed in brain, heart and kidney. Isoform 5 is dominantly expressed in liver, heart and kidney. Isoform 6 is expressed in neurons.
|Involvement in disease|| |
Note: May be associated with Alzheimer disease through beta-amyloid-induced increased S-nitrosylation of DNM1L, which triggers, directly or indirectly, excessive mitochondrial fission, synaptic loss and neuronal damage. .; Encephalopathy, lethal, due to defective mitochondrial and peroxisomal fission (EMPF) [MIM:614388]: A rare autosomal dominant systemic disorder resulting in lack of neurologic development and death in infancy. After birth, infants present in the first week of life with poor feeding and neurologic impairment, including hypotonia, little spontaneous movement, no tendon reflexes, no response to light stimulation, and poor visual fixation. Other features include mildly elevated plasma concentration of very-long-chain fatty acids, lactic acidosis, microcephaly, deep-set eyes, optic atrophy and hypoplasia, and an abnormal gyral pattern in both frontal lobes associated with dysmyelination. . Note: The disease is caused by mutations affecting the gene represented in this entry.
|Protein sequence and domain|| |
The GED domain folds back to interact, in cis, with the GTP-binding domain and middle domain, and interacts, in trans, with the GED domains of other DNM1L molecules, and is thus critical for activating GTPase activity and for DNM1L dimerization. / Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. / Contains 1 dynamin-type G (guanine nucleotide-binding) domain. / Contains 1 GED domain.
|Protein post-translational modifications|| |
Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission. Phosphorylation on Ser-637 inhibits mitochondrial fission probably through preventing intramolecular interaction. Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission. Phosphorylation on Ser-616 also promotes mitochondrial fission. / Sumoylated on various lysine residues within the B domain, probably by MUL1. Sumoylation positively regulates mitochondrial fission. Desumoylated by SENP5 during G2/M transition of mitosis. Appears to be linked to its catalytic activity. / S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage. / Ubiquitination by MARCH5 affects mitochondrial morphology. / O-GlcNAcylation augments the level of the GTP-bound active form of DRP1 and induces translocation from the cytoplasm to mitochondria in cardiomyocytes. It also decreases phosphorylation at Ser-637 (By similarity).
|Protein cellular localization|| |
Cytoplasm > cytosol / Golgi apparatus / Endomembrane system; Peripheral membrane protein / Mitochondrion outer membrane; Peripheral membrane protein / Peroxisome / Membrane > clathrin-coated pit / Cytoplasmic vesicle > secretory vesicle > synaptic vesicle membrane
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St John’s Laboratory Ltd.
|Product type|| |
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