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Pro Caspase-3 Rabbit Polyclonal Antibody (ER30804)

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Catalog# ER30804

Rabbit Polyclonal to Caspase-3

Tested for

  • WB

  • IF-Cell

  • IHC-P

  • FC

  • IHC-Fr

Reacts with

  • Human

  • Mouse

This product has been cited in peer reviewed publications, see list HERE

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COA DOWNLOAD

Specifications

Product Type

Rabbit polyclonal primary

Product Name

Pro Caspase-3 Rabbit Polyclonal Antibody (ER30804)

Immunogen

Synthetic peptide within n-terminal human caspase-3.

Host

Rabbit

Positive Control

Jurkat cell lysate, Ramos cell lysate, human brain tissue lysate, HepG2, A549, human liver carcinoma tissue, human tonsil tissue.

Conjugation

Unconjugated

Clonality

Polyclonal

RRID

AB_3069554

APPLICATION DILUTION

  • WB

  • 1:5,000

  • IF-Cell

  • 1:200

  • IHC-P

  • 1:200

  • FC

  • 1:100-1:200

  • IHC-Fr:1:100

PROPERTIES

Form

Liquid

Storage Condition

Shipped at 4℃. Store at +4℃ short term (1-2 weeks). It is recommended to aliquot into single-use upon delivery. Store at -20℃ long term.

Storage Buffer

1*PBS (pH7.4), 0.2% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.

Concentration

1ug/ul

Purification

Immunogen affinity purified.

Molecular Weight

Predicted band size: 32 kDa

Isotype

IgG

TARGET

UNIPROT #

P42574

PROTEIN NAME

Caspase-3

SYNONYMS

Caspase3;A830040C14Rik antibody;Apopain antibody;CASP 3 antibody;CASP-3 antibody;CASP3 antibody;CASP3_HUMAN antibody;Casp3a antibody;Caspase 3 antibody;Caspase 3, apoptosis-related cysteine peptidase antibody;Caspase 3, apoptosis-related cysteine protease antibody;Caspase 3, apoptosis-related cysteine protease a antibody;Caspase-3 subunit p12 antibody;Caspase3 antibody;CC3 antibody;CPP 32 antibody;CPP-32 antibody;CPP32 antibody;CPP32B antibody;Cysteine protease CPP32 antibody;EC 3.4.22.56 antibody;ICE3 antibody;LICE antibody;mldy antibody;OTTHUMP00000165052 antibody;OTTHUMP00000165053 antibody;OTTHUMP00000165054 antibody;PARP cleavage protease antibody;Procaspase3 antibody;Protein Yama antibody;SCA 1 antibody;SCA-1 antibody;SCA1 antibody;SREBP cleavage activity 1 antibody;Yama antibody;Yama protein antibody

SEQUENCE SIMILARITIES

Belongs to the peptidase C14A family.

TISSUE SPECIFICITY

Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.

POST-TRANSLATIONAL MODIFICATION

Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa.; S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol.

SUBCELLULAR LOCATION

Nucleus, cytoplasm,

FUNCTION

Caspase-3 is a caspase protein that interacts with caspase-8 and caspase-9. It is encoded by the CASP3 gene. CASP3 orthologs have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts. Caspase-3 shares many of the typical characteristics common to all currently-known caspases. For example, its active site contains a cysteine residue (Cys-163) and histidine residue (His-121) that stabilize the peptide bond cleavage of a protein sequence to the carboxy-terminal side of an aspartic acid when it is part of a particular 4-amino acid sequence. This specificity allows caspases to be incredibly selective, with a 20,000-fold preference for aspartic acid over glutamic acid. A key feature of caspases in the cell is that they are present as zymogens, termed procaspases, which are inactive until a biochemical change causes their activation. Each procaspase has an N-terminal large subunit of about 20 kDa followed by a smaller subunit of about 10 kDa, called p20 and p10, respectively.

CITATIONS

  • Pin Fang,et al

    Pharmacodynamic Insights into Maresin 1: Enhancing Flap Viability via the Keap1/Nrf2 Axis to Control ROS-Driven Apoptosis and Ferroptosis

  • Jian-Hong Luo;Tian-Le Xu;Xiang-Yao Li

    Restoration of Cingulate Long-Term Depression by Enhancing Non-apoptotic Caspase 3 Alleviates Peripheral Pain Hypersensitivity

  • Yao Wenjian,et al

    Recombinant human protein TCFL5-activated NRSN2-AS1 promotes esophageal cancer progression via the microRNA-874-5p/RELT regulatory axis

  • Photodynamic therapy of lung cancer with photosensitizers based on polycationic derivatives of synthetic bacteriochlorin (experimental study)

  • Proteomics and Metabolomics Unveil Codonopsis pilosula (Franch.) Nannf. Ameliorates Gastric Precancerous Lesions via Regulating Energy Metabolism

  • Fan, H., Ren, Z., Xu, C., Wang, H., Wu, Z., Rehman, Z. U., Wu, S., Sun, M. A., & Bao, W.

    Chromatin Accessibility and Transcriptomic Alterations in Murine Ovarian Granulosa Cells upon Deoxynivalenol Exposure

  • Hu, J., Cao, J., Jin, R., Zhang, B., Topatana, W., Juengpanich, S., Li, S., Chen, T., Lu, Z., Cai, X., & Chen, M.

    Inhibition of AMPK/PFKFB3 mediated glycolysis synergizes with penfluridol to suppress gallbladder cancer growth

  • Shusen Zheng

    Combination of HSP90 and autophagy inhibitors promotes hepatocellular carcinoma apoptosis following incomplete thermal ablation

  • Fengjie Huang

    Sini decoction alleviates E. coli induced acute lung injury in mice via equilibrating ACE-AngII-AT1R and ACE2-Ang-(1-7)-Mas axis

  • Fan, H., Wang, S., Wang, H., Sun, M., Wu, S., & Bao, W.

    Melatonin Ameliorates the Toxicity Induced by Deoxynivalenol in Murine Ovary Granulosa Cells by Antioxidative and Anti-Inflammatory Effects. Antioxidants (Basel, Switzerland), 10(7), 1045.

  • Dr Xia Liu,Professor Jianchao Wang

    Silencing RRM2 inhibits multiple myeloma by targeting the Wnt/β-catenin signaling pathway

  • Shi, D., Shan, Y., Zhu, X., Wang, H., Wu, S., Wu, Z., & Bao, W.

    Histone Methyltransferase MLL1 Mediates Oxidative Stress and Apoptosis upon Deoxynivalenol Exposure in the Intestinal Porcine Epithelial Cells

  • Tao Guoa,Fengjie Huang

    Sini decoction ameliorates sepsis-induced acute lung injury via regulating ACE2-Ang (1-7)-Mas axis and inhibiting the MAPK signaling pathway

  • Xiaoyang Zhu,et al

    DNA ligase III mediates deoxynivalenol exposure-induced DNA damage in intestinal epithelial cells by regulating oxidative stress and interaction with PCNA

  • Wu, H., Guo, H., Liu, H., Cui, H., Fang, J., Zuo, Z., Deng, J., Li, Y., Wang, X., & Zhao, L.

    Copper sulfate-induced endoplasmic reticulum stress promotes hepatic apoptosis by activating CHOP, JNK and caspase-12 signaling pathways

  • Xiao, Y., Wang, J., Wang, J., Wang, H., Wu, S., & Bao, W.

    Analysis of the roles of the Notch1 signalling pathway in modulating deoxynivalenol cytotoxicity

  • Gao, Z., Xu, C., Fan, H., Wang, H., Wu, Z., Wu, S., & Bao, W.

    Analysis of RIOK2 Functions in Mediating the Toxic Effects of Deoxynivalenol in Porcine Intestinal Epithelial Cells

  • Gui Jianxiong,et al

    Autophagy alleviates hippocampal neuroinflammation by inhibiting the NLRP3 inflammasome in a juvenile rat model exposed particulate matter

  • Toxoplasma gondii induces MLTC-1 apoptosis via ERS pathway

  • Chen, Y., Lu, Z., Qi, C., Yu, C., Li, Y., Huan, W., Wang, R., Luo, W., Shen, D., Ding, L., Ren, L., Xie, H., Xue, D., Wang, M., Ni, K., Xia, L., Qian, J., & Li, G.

    N6-methyladenosine-modified TRAF1 promotes sunitinib resistance by regulating apoptosis and angiogenesis in a METTL14-dependent manner in renal cell carcinoma

  • Lai Yingying,et al

    Dihydrocapsaicin suppresses the STING-mediated accumulation of ROS and NLRP3 inflammasome and alleviates apoptosis after ischemia-reperfusion injury of perforator skin flap

  • Wang, L., Meng, Q., Yang, L., Yang, D., Guo, W., Lin, P., Chen, H., Tang, K., Wang, A., & Jin, Y.

    Luman/CREB3 knock-down inhibit hCG induced MLTC-1 apoptosis

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