Mouse Anti-CASP7 Recombinant Antibody (CBFYC-0481) (CBMAB-C0529-FY)

Name: Mouse Anti-CASP7 Recombinant Antibody (CBFYC-0481)
SKU: CBMAB-C0529-FY
Rating: 5 (1 reviews)

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Published Data

Mouse Anti-CASP7 Recombinant Antibody (CBFYC-0481) (CBMAB-C0529-FY) in WB

Western-blot analyses of control and 24 h MortaparibPlus-treated colorectal cancer cells showed different changes in the levels of key proteins favouring the initiation of apoptosis as a tumour suppression fate. ...View More

Sari, A. N., Elwakeel, A., Dhanjal, J. K., Kumar, V., Sundar, D., Kaul, S. C., & Wadhwa, R. (2021). Identification and characterization of mortaparibPlus-A novel triazole derivative that targets mortalin-p53 interaction and inhibits cancer-cell proliferation by wild-type p53-dependent and-independent mechanisms. Cancers, 13(4), 835.

Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

CBFYC-0481

Application

ELISA, IHC-P, IF, IP, WB

Immunogen

Amino acids 76-140 mapping within an internal region of caspase-7 p20 of human origin.

Host Species

Mouse

Specificity

Human, Mouse, Rat

Antibody Isotype

IgG2a, κ

Clonality

Monoclonal

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Application	Note
WB	1:100-1:1,000
IP	1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
ELISA	1:100-1:1,000
IF(ICC)	1:50-1:500
IHC-P	1:50-1:500

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

Format

Liquid

Buffer

PBS, 0.1% gelatin

Preservative

< 0.1% sodium azide

Concentration

0.2 mg/ml

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

More Infomation

Target

Full Name

Caspase 7

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. The precursor of the encoded protein is cleaved by caspase 3 and 10, is activated upon cell death stimuli and induces apoptosis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.

Entrez Gene ID

840

UniProt ID

P55210

Alternative Names

Caspase 7; Caspase 7, Apoptosis-Related Cysteine Peptidase; Caspase 7, Apoptosis-Related Cysteine Protease; ICE-Like Apoptotic Protease 3; ICE-LAP3; CASP-7; CMH-1; MCH3

Function

Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death.

Biological Process

Apoptotic process Source: UniProtKB
Cellular response to staurosporine Source: CAFA
Execution phase of apoptosis Source: GO_Central
Proteolysis Source: UniProtKB

Cellular Location

Cytoplasm

PTM

Cleavages by granzyme B or caspase-10 generate the two active subunits. Propeptide domains can also be cleaved efficiently by caspase-3. Active heterodimers between the small subunit of caspase-7 and the large subunit of caspase-3, and vice versa, also occur.

Mahib, M. R., Hosojima, S., Kushiyama, H., Kinoshita, T., Shiroishi, T., Suda, T., & Tsuchiya, K. (2020). Caspase‐7 mediates caspase‐1‐induced apoptosis independently of Bid. Microbiology and immunology, 64(2), 143-152.

Safdar, M., Zaheer, S., Khailany, R. A., Parvez, S., Naveed, M., Bhuiyan, P., ... & Junejo, Y. (2020). The Relevance of SNPs at 3′ UTR Region of CASP7 and miR-371b-5p Associated Diseases: A Computational Analysis. Cell Biochemistry and Biophysics, 78(4), 541-557.

Gonçalves, A. V., Margolis, S. R., Quirino, G. F., Mascarenhas, D. P., Rauch, I., Nichols, R. D., ... & Zamboni, D. S. (2019). Gasdermin-D and Caspase-7 are the key Caspase-1/8 substrates downstream of the NAIP5/NLRC4 inflammasome required for restriction of Legionella pneumophila. PLoS pathogens, 15(6), e1007886.

Pham, B., Eron, S. J., Hill, M. E., Li, X., Fahie, M. A., Hardy, J. A., & Chen, M. (2019). A nanopore approach for analysis of caspase-7 activity in cell lysates. Biophysical journal, 117(5), 844-855.

Shigemura, M., Lecuona, E., Angulo, M., Homma, T., Rodríguez, D. A., Gonzalez-Gonzalez, F. J., ... & Sznajder, J. I. (2018). Hypercapnia increases airway smooth muscle contractility via caspase-7–mediated miR-133a–RhoA signaling. Science translational medicine, 10(457).

Venkatesh, A., Cheng, S. Y., & Punzo, C. (2017). Loss of the cone-enriched caspase-7 does not affect secondary cone death in retinitis pigmentosa. Molecular vision, 23, 944.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

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

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