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Key Specifications Table
| Species Reactivity | Key Applications | Host | Format | Antibody Type |
|---|---|---|---|---|
| H, M, R | WB, IHC | Rb | Purified | Polyclonal Antibody |
| Description | |
|---|---|
| Catalogue Number | 06-735 |
| Replaces | 04-1090; 04-439 |
| Brand Family | Upstate |
| Trade Name |
|
| Description | Anti-Caspase 3 Antibody |
| Background Information | Caspase-3 (UniProt: P42574; also known as EC:3.4.22.56, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 1, SCA-1) is encoded by the CASP3 (also known as CPP32) gene (Gene ID: 836) in human. Cysteine-aspartic proteases or Caspases play essential roles in apoptosis, necrosis, and inflammation. Historically, caspases were numbered in the order in which they were identified. Caspase-3 is a heterotetrameric enzyme that consists of two anti-parallel arranged heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit. Caspase-3 is initially produced with a propeptide sequence (aa 1-9), the removal of which yields the 268 aa. caspase-3 proenzyme. Upon activation, the proenzyme is proteolytically cleaved first between Asp175-Ser176 to generate a p20 (aa 10-175) fragment and the p12 (aa 176-277) subunit. Further cleavage of the p20 fragment between Asp28-Ser29 produces the p17 (aa 29-175) subunit. The p17 and p12 subunits dimerize and forms the active caspase-3 enzyme. Caspase-3 has a strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position. Caspase-3 is involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a Asp216-|-Gly217 bond. Caspase-3 mediates the proteolytic activation of caspases-6 and -7, while caspase-3 itself is processed and activated by caspase-8, -9, or -10. |
| Product Information | |
|---|---|
| Format | Purified |
| Control |
|
| Presentation | Protein A purified IgG in of 0.1M Tris-glycine, pH 7.4, 0.15M NaCl,and 0.05% sodium azide. |
| Quality Level | MQ100 |
| Applications | |
|---|---|
| Application | This Anti-Caspase 3 Antibody is validated for use in Immunohistochemistry and Western Blotting for the detection of Caspase 3. |
| Key Applications |
|
| Application Notes | Western Blotting Analysis: 1mg/mL of this antibody detects Caspase-3 in A431 cell lysate. Immunohistochemistry (Paraffin) Analysis: A 1:250 dilution of this antibody detected Caspase-3 in Human tonsil tissue sections. |
| Biological Information | |
|---|---|
| Immunogen | Human full-length Caspase 3 fusion protein containing a histidine-6 tag |
| Host | Rabbit |
| Specificity | Recognizes full-length Caspase 3 (Yama/Apopain) and proteolytic fragments. |
| Isotype | IgG |
| Species Reactivity |
|
| Antibody Type | Polyclonal Antibody |
| Entrez Gene Number |
|
| Entrez Gene Summary | This gene encodes a protein which is 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 cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimers disease. Alternative splicing of this gene results in two transcript variants that encode the same protein. |
| Gene Symbol |
|
| Purification Method | Protein A Purfied |
| UniProt Number |
|
| UniProt Summary | FUNCTION: SwissProt: P42574 # Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a 216-Asp- -Gly-217 bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. SIZE: 277 amino acids; 31608 Da SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit. SUBCELLULAR LOCATION: Cytoplasm. 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. PTM: 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. SIMILARITY: SwissProt: P42574 ## Belongs to the peptidase C14 family. |
| Molecular Weight | 32 kDa |
| Product Usage Statements | |
|---|---|
| Quality Assurance | routinely evaluated by immunoblot on RIPA lysates from non-stimulated human A431 cells, mouse 3T3/A31 or rat PC12 cells |
| Usage Statement |
|
| Storage and Shipping Information | |
|---|---|
| Storage Conditions | Stable for 2 years at 2-8°C from date of shipment. For maximum recovery of product, centrifuge the original vial prior to removing the cap. |
| Packaging Information | |
|---|---|
| Material Size | 200 µg |