Product Pathways - Apoptosis
HtrA2 Antibody #2176
PhosphoSitePlus® protein, site, and accession data: HTRA2
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W | H M R Mk (Dg) | Endogenous | 36 | Rabbit |
Applications Key:
W=Western Blotting
Reactivity Key:
H=Human
M=Mouse
R=Rat
Mk=Monkey
Dg=Dog
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Protocols
- 2176:
- Western Blotting
Specificity / Sensitivity
HtrA2 Antibody detects endogenous levels of the mature form of HtrA2. This antibody is expected to also recognize the unprocessed form of HtrA2. The unprocessed form is detected in cells overexpressing HtrA2.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser335 of HtrA2. Antibodies are purified by protein A and peptide affinity chromatography.
Background
High temperature requirement protein A2 (HtrA2)/Omi is a serine protease with homology to the E. coli HtrA protein (DegP) and is thought to be involved in apoptosis and stress-induced degradation of misfolded proteins (1). While HtrA2 was orignally identified to be present in either the nucleus (1) or endoplasmic reticulum (2), subsequent studies have shown that it localizes in mitochondria and is released during apoptosis (3-8). HtrA2 is produced as a 50 kDa zymogen that is cleaved to generate a 36 kDa mature protein that exposes an amino terminal motif (AVPS) resembling that of the IAP inhibitor Smac/Diablo (3-8). Like Smac, interaction between HtrA2 and IAP family members, such as XIAP, antagonizes their inhibition of caspase activity and protection from apoptosis (3-8). Interestingly, HtrA2 knock-out mice did not show signs of reduced apoptosis, but rather had a loss of neurons in the striatum and a Parkinson's-like phenotype, suggesting that HtrA2 might have a neuroprotective function (9-11). This activity is associated with the protease activity of HtrA2 (9). Furthermore, research studies have shown that loss of function mutations in the HtrA2 gene are associated with Parkinson's disease (12).
- Gray, C.W. et al. (2000) Eur. J. Biochem. 267, 5699-5710.
- Faccio, L. et al. (2000) J. Biol. Chem. 275, 2581-2588.
- Suzuki, Y. et al. (2001) Mol. Cell 8, 613-621.
- Hegde, R. et al. (2002) J. Biol. Chem. 277, 432-438.
- Martins, L.M. et al. (2002) J. Biol. Chem. 277, 439-444.
- van Loo, G. et al. (2002) Cell Death Differ. 9, 20-26.
- Verhagen, A.M. et al. (2002) J. Biol. Chem. 277, 445-454.
- Martins, L.M. et al. (2002) J. Biol. Chem. 277, 439-444.
- Jones, J.M. et al. (2003) Nature 425, 721-727.
- Vaux, D.L. and Silke, J. (2003) Cell 115, 251-253.
- Martins, L.M. et al. (2004) Mol. Cell Biol. 24, 9848-9862.
- Strauss, K.M. et al. (2005) Hum. Mol. Genet. 14, 2099-2111.
Application References
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For Research Use Only. Not For Use In Diagnostic Procedures.