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Rabbit Anti-CASP9 Recombinant Antibody (CBAb045) (CBMAB-Ab045-LY)


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Summary

Host Animal
Rabbit
Specificity
Human, Mouse
Clone
CBAb045
Antibody Isotype
IgG
Application
WB, IHC, ICC, IF, IP

Basic Information

Immunogen
Synthetic peptide within Human Caspase-9 aa 20-69.
Host Species
Rabbit
Specificity
Human, Mouse
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:1,000-1:2,000
IHC-P1:50-1:200
FC1:10-1:50

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

Format
Liquid
Buffer
TBS, pH 7.4, 40% Glycerol, 0.05% BSA
Preservative
0.05% sodium azide
Concentration
1 mg/ml
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Caspase 9
Introduction
This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein can undergo autoproteolytic processing and activation by the apoptosome, a protein complex of cytochrome c and the apoptotic peptidase activating factor 1; this step is thought to be one of the earliest in the caspase activation cascade. This protein is thought to play a central role in apoptosis and to be a tumor suppressor. Alternative splicing results in multiple transcript variants.
Entrez Gene ID
Human842
Mouse12371
UniProt ID
HumanP55211
MouseQ8C3Q9
Alternative Names
CASP9; APAF-3; APAF3; ICE-LAP6; MCH6; PPP1R56; caspase-9
Function
Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP).
Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.
Biological Process
Activation of cysteine-type endopeptidase activity involved in apoptotic process Source: GO_Central
Activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Source: Reactome
Apoptotic process Source: UniProtKB
Cellular response to DNA damage stimulus Source: UniProtKB
Cellular response to UV Source: UniProtKB
Extrinsic apoptotic signaling pathway in absence of ligand Source: Reactome
Intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
Platelet formation Source: UniProtKB
Positive regulation of apoptotic process Source: UniProtKB
Regulation of response to DNA damage stimulus Source: UniProtKB
Signal transduction in response to DNA damage Source: UniProtKB
Cellular Location
Apoptosome; Cytosol; Cytoplasm; Protein-containing complex
PTM
Cleavages at Asp-315 by granzyme B and at Asp-330 by caspase-3 generate the two active subunits. Caspase-8 and -10 can also be involved in these processing events.
Phosphorylated at Thr-125 by MAPK1/ERK2. Phosphorylation at Thr-125 is sufficient to block caspase-9 processing and subsequent caspase-3 activation. Phosphorylation on Tyr-153 by ABL1/c-Abl; occurs in the response of cells to DNA damage.
More Infomation

Han, J., Goldstein, L. A., Hou, W., Watkins, S. C., & Rabinowich, H. (2021). Involvement of CASP9 (caspase 9) in IGF2R/CI-MPR endosomal transport. Autophagy, 17(6), 1393-1409.

Doke, T., Huang, S., Qiu, C., Sheng, X., Seasock, M., Liu, H., ... & Susztak, K. (2021). Genome-wide association studies identify the role of caspase-9 in kidney disease. Science advances, 7(45), eabi8051.

Liao, G., Wang, R., & Tang, D. D. (2021). Plk1 Regulates Caspase-9 Phosphorylation at Ser-196 and Apoptosis of Human Airway Smooth Muscle Cells. American journal of respiratory cell and molecular biology, (ja).

Avrutsky, M. I., & Troy, C. M. (2021). Caspase-9: A Multimodal Therapeutic Target With Diverse Cellular Expression in Human Disease. Frontiers in Pharmacology, 12, 1728.

An, H. K., Chung, K. M., Park, H., Hong, J., Gim, J. E., Choi, H., ... & Yu, S. W. (2020). CASP9 (caspase 9) is essential for autophagosome maturation through regulation of mitochondrial homeostasis. Autophagy, 16(9), 1598-1617.

Han, C., Liu, Z., Zhang, Y., Shen, A., Dong, C., Zhang, A., ... & Fu, Y. X. (2020). Tumor cells suppress radiation-induced immunity by hijacking caspase 9 signaling. Nature immunology, 21(5), 546-554.

Zhang, L., Zhang, X., Wang, X., He, M., & Qiao, S. (2019). MicroRNA-224 promotes tumorigenesis through downregulation of caspase-9 in triple-negative breast cancer. Disease markers, 2019.

Ercan, S., Arinc, S., Yilmaz, S. G., Altunok, C., Yaman, F., & Isbir, T. (2019). Investigation of caspase 9 gene polymorphism in patients with non-small cell lung cancer. Anticancer research, 39(5), 2437-2441.

Iwai, N., Yasui, K., Tomie, A., Gen, Y., Terasaki, K., Kitaichi, T., ... & Itoh, Y. (2018). Oncogenic miR-96-5p inhibits apoptosis by targeting the caspase-9 gene in hepatocellular carcinoma. International journal of oncology, 53(1), 237-245.

Lu, J., Peng, J., Xiang, M., He, L., Wang, D., Xiong, G., & Li, S. (2018). Trichosanthes kirilowii lectin alleviates diabetic nephropathy by inhibiting the LOX1/NF-κB/caspase-9 signaling pathway. Bioscience reports, 38(5), BSR20180071.

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

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