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Caspase-3 Recombinant Rabbit Monoclonal Antibody [SR03-01] (ET1602-39)

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Catalog# ET1602-39

Rabbit Monoclonal to Caspase-3

Tested for

  • WB

  • IF-Cell

  • IF-Tissue

  • IHC-P

  • IP

  • FC

Reacts with

  • Human

Recombinant production enables lot-to-lot consistency and is animal-cruelty-free
Knock-Out or Knock-Down validated
This product has been cited in peer reviewed publications, see list HERE

Specifications

Product Type

Recombinant Rabbit monoclonal primary

Product Name

Caspase-3 Recombinant Rabbit Monoclonal Antibody [SR03-01] (ET1602-39)

Immunogen

Synthetic peptide within human caspase-3 aa 60-100.

Host

Rabbit

Positive Control

HeLa cell lysate, Jurkat cell lysate, HEK-293 cell lysate, Hela, human tonsil tissue, human spleen tissue.

Conjugation

Unconjugated

Clonality

Monoclonal

Clone Number

SR03-01

RRID

AB_3069652

APPLICATION DILUTION

  • WB

  • 1:2,000-1:5,000

  • IF-Cell

  • 1:50

  • IF-Tissue

  • 1:50

  • IHC-P

  • 1:50

  • FC

  • 1:20-1:50

  • IP

  • Use at an assay dependent concentration.

PROPERTIES

Form

Liquid

Storage Condition

Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.

Storage Buffer

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

Concentration

1ug/ul

Purification

Protein A 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;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;CC3 antibody;CPP-32 antibody;CPP32 antibody;CPP32B antibody;Cysteine protease CPP32 antibody;EC 3.4.22.56 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;SREBP cleavage activity 1 antibody;Yama 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

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

  • Chen, P., Wang, H., Li, M., Yang, L., Mou, F., Singh, B., He, J. Y., & Zhang, W.

    6, 12-Diphenyl-3, 9-diazatetraasterane-1, 5, 7, 11-tetracarboxylate inhibits proliferation, migration and promotes apoptosis in ovarian cancer cells

  • Jian Li; Caiqiao Zhang

    Metformin Prevents Follicular Atresia in Aging Laying Chickens through Activation of PI3K/AKT and Calcium Signaling Pathways

  • Jin Gu,Wei-Guo Zhu

    5-Fluorouracil Targets Histone Acetyltransferases p300/CBP in the Treatment of Colorectal Cancer

  • Cul4 E3 ubiquitin ligase regulates ovarian cancer drug resistance by targeting the antiapoptotic protein BIRC3

  • Zhang, Huihao;Zhou, Chengcong;Zhang, Zhiguo;Yao, Sai;Bian, Yishan;Fu, Fangda;Luo, Huan;Li, Yan;Yan, Shuxin;Ge, Yuying;Chen, Yuying;Zhan, Kunyu;Yue, Ming;Du, Weibin;Tian, Kun;Jin, Hongting;Li, Xiaofeng;Tong, Peijian;Ruan, Hongfeng;Wu, Chengliang

    Integration of Network Pharmacology and Experimental Validation to Explore the Pharmacological Mechanisms of Zhuanggu Busui Formula Against Osteoporosis

  • Jujuboside B Inhibits the Proliferation of Breast Cancer Cell Lines by Inducing Apoptosis and Autophagy

  • TRIM55 inhibits colorectal cancer development via enhancing protein degradation of c-Myc

  • Cinnamon cassia oil chitosan nanoparticles: Physicochemical properties and anti-breast cancer activity

  • Yue Wang,et al

    Carbon dots-cisplatin nano drug delivery system induces the death of oral tongue squamous cell under self-targeting chemical/photodynamic combined therapy

  • Fan Chengcheng,et al

    Natural Product-Inspired Discovery of Naphthoquinone-Furo-Piperidine Derivatives as Novel STAT3 Inhibitors for the Treatment of Triple-Negative Breast Cancer

  • Zhou Heng,et al

    Modulation of epithelial-mesenchymal transition by gemcitabine: Targeting ionizing radiation-induced cellular senescence in lung cancer cell

  • Deng, Y. L., Chen, S., Wang, H. T., Wang, B., & Xiao, K.

    Prescription of Sageretia hamosa Brongn Relieved Goiter through Promoted Apoptosis of Thyroid Cells via miR-511-3p and PTEN/PI3K/Akt Pathway

  • Protective effect of rutin on ferroptosis‐induced oxidative stress in aging laying hens through Nrf2/HO‐1 signaling

  • A programmed cell death-related model based on machine learning for predicting prognosis and immunotherapy responses in patients with lung adenocarcinoma

  • Tang Xiaolin,et al

    GGTLC1 knockdown inhibits the progression of endometrial cancer by regulating the TGF-β/Smad signaling pathway

  • Mice lacking DCAF2 in placenta die at the gastrulation stage

  • Rao Zichen

    HNRNP I promotes IRAK1 degradation to reduce podocyte apoptosis and inflammatory response alleviating renal injury in diabetic nephropathy

  • Network Pharmacology and Experimental Validation to Reveal the Pharmacological Mechanisms of Liuwei Dihuang Decoction Against Intervertebral Disc Degeneration

  • Selenium‐binding protein 1 inhibits malignant progression and induces apoptosis via distinct mechanisms in non‐small‐cell lung cancer

  • Yuling Mi; Caiqiao Zhang

    The Attenuating Effect of the Intraovarian Bone Morphogenetic Protein 4 on Age-Related Endoplasmic Reticulum Stress in Chicken Follicular Cells

  • Dusp1 regulates thermal tolerance limits in zebrafish by maintaining mitochondrial integrity

  • Liu, X., Cui, S., Dan, C., Li, W., Xie, H., Li, C., & Shi, L.

    Phellinus baumii Polyphenol: A Potential Therapeutic Candidate against Lung Cancer Cells

  • Ji Haofei,et al

    Delivery of 5-fluorouracil for cancer therapy using aptamer-based nonlinear hybridization chain reaction

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