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Mouse Anti-HTRA2 Monoclonal Antibody (CBFYH-3267) (CBMAB-H3522-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-3267
Antibody Isotype
IgG1
Application
WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4, 50% glycerol
Preservative
0.03% Proclin 300
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
HtrA Serine Peptidase 2
Introduction
This gene encodes a serine protease. The protein has been localized in the endoplasmic reticulum and interacts with an alternatively spliced form of mitogen-activated protein kinase 14. The protein has also been localized to the mitochondria with release to the cytosol following apoptotic stimulus. The protein is thought to induce apoptosis by binding the apoptosis inhibitory protein baculoviral IAP repeat-containing 4. Nuclear localization of this protein has also been observed. Alternate splicing of this gene results in multiple transcript variants encoding different isoforms.
Entrez Gene ID
27429
UniProt ID
O43464
Alternative Names
HtrA Serine Peptidase 2; High Temperature Requirement Protein A2; Omi Stress-Regulated Endoprotease; Serine Proteinase OMI; Protease, Serine, 25; Serine Protease 25; EC 3.4.21.108; PRSS25
Function
Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 seems to be proteolytically inactive.
Biological Process
Adult walking behavior Source: Ensembl
Aging Source: Ensembl
Cellular protein catabolic process Source: ParkinsonsUK-UCL
Cellular response to growth factor stimulus Source: UniProtKB
Cellular response to heat Source: UniProtKB
Cellular response to interferon-beta Source: ParkinsonsUK-UCL
Cellular response to oxidative stress Source: ParkinsonsUK-UCL
Cellular response to retinoic acid Source: ParkinsonsUK-UCL
Ceramide metabolic process Source: Ensembl
Execution phase of apoptosis Source: UniProtKB
Forebrain development Source: Ensembl
Intrinsic apoptotic signaling pathway in response to DNA damage Source: ParkinsonsUK-UCL
Mitochondrion organization Source: Ensembl
Negative regulation of cell cycle Source: UniProtKB
Negative regulation of mitophagy in response to mitochondrial depolarization Source: Ensembl
Negative regulation of neuron death Source: ParkinsonsUK-UCL
Negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
Neuron development Source: Ensembl
Pentacyclic triterpenoid metabolic process Source: Ensembl
Positive regulation of apoptotic process Source: UniProtKB
Positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: ParkinsonsUK-UCL
Positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: UniProtKB
Positive regulation of mitochondrion organization Source: ParkinsonsUK-UCL
Positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
Programmed cell death Source: UniProtKB
Protein autoprocessing Source: ParkinsonsUK-UCL
Proteolysis Source: ParkinsonsUK-UCL
Regulation of autophagy of mitochondrion Source: ParkinsonsUK-UCL
Regulation of multicellular organism growth Source: Ensembl
Response to herbicide Source: Ensembl
Cellular Location
Mitochondrion intermembrane space; Mitochondrion membrane. Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment, and stimulation of mitochondria with caspase-8 truncated BID/tBID.
Isoform 1: Endoplasmic reticulum
Involvement in disease
3-methylglutaconic aciduria 8 (MGCA8):
An autosomal recessive inborn error of metabolism resulting in early death. Clinical features include extreme hypertonia observed at birth, alternating with hypotonia, subsequent appearance of extrapyramidal symptoms, lack of psychomotor development, microcephaly, and intractable seizures. Patients show lactic acidemia, 3-methylglutaconic aciduria, intermittent neutropenia, and progressive brain atrophy.
Parkinson disease 13 (PARK13):
A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.
Topology
Helical: 105-125
PTM
Autoproteolytically activated.
More Infomation

Chakraborty, A., Bose, R., & Bose, K. (2022). Unraveling the Dichotomy of Enigmatic Serine Protease HtrA2. Frontiers in Molecular Biosciences, 9, 824846.

Guo, Y., Han, L., Han, S., Tang, H., Wang, S., Cui, C., ... & Shu, Y. (2022). Specific knockdown of Htra2 by CRISPR-CasRx prevents acquired sensorineural hearing loss in mice. Molecular Therapy-Nucleic Acids, 28, 643-655.

Toyama, Y., Harkness, R. W., Lee, T. Y., Maynes, J. T., & Kay, L. E. (2021). Oligomeric assembly regulating mitochondrial HtrA2 function as examined by methyl-TROSY NMR. Proceedings of the National Academy of Sciences, 118(11), e2025022118.

Gu, X., Wang, D., Xu, Z., Wang, J., Guo, L., Chai, R., ... & Li, H. (2021). Prevention of acquired sensorineural hearing loss in mice by in vivo Htra2 gene editing. Genome Biology, 22(1), 1-23.

Saini, P., Rudakou, U., Yu, E., Ruskey, J. A., Asayesh, F., Laurent, S. B., ... & Gan-Or, Z. (2021). Association study of DNAJC13, UCHL1, HTRA2, GIGYF2, and EIF4G1 with Parkinson's disease. Neurobiology of aging, 100, 119-e7.

Schmelter, C., Fomo, K. N., Perumal, N., Pfeiffer, N., & Grus, F. H. (2021). Regulation of the HTRA2 protease activity by an inhibitory antibody-derived peptide ligand and the influence on HTRA2-specific protein interaction networks in retinal tissues. Biomedicines, 9(8), 1013.

Su, X. J., Huang, L., Qu, Y., & Mu, D. (2019). Progress in research on the role of Omi/HtrA2 in neurological diseases. Reviews in the Neurosciences, 30(3), 279-287.

Botham, A., Coyaud, E., Nirmalanandhan, V. S., Gronda, M., Hurren, R., Maclean, N., ... & Schimmer, A. (2019). Global interactome mapping of mitochondrial intermembrane space proteases identifies a novel function for HTRA2. Proteomics, 19(24), 1900139.

Zhang, C., He, A., Liu, S., He, Q., Luo, Y., He, Z., ... & Yan, J. (2019). Inhibition of HtrA2 alleviated dextran sulfate sodium (DSS)-induced colitis by preventing necroptosis of intestinal epithelial cells. Cell Death & Disease, 10(5), 344.

Wang, P., Hu, Y., Yao, D., & Li, Y. (2018). Omi/HtrA2 regulates a mitochondria-dependent apoptotic pathway in a murine model of septic encephalopathy. Cellular Physiology and Biochemistry, 49(6), 2163-2173.

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For research use only. Not intended for any clinical use.

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