Recombinant human Caspase-8 protein is a Human Fragment protein, in the 200 to 496 aa range, expressed in Escherichia coli, with >=99% purity and suitable for SDS-PAGE, FuncS.
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Publications
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- Acta pharmacologica Sinica :2020Gasdermin E-derived caspase-3 inhibitors effectively protect mice from acute hepatic failure.Applications:Unspecified applicationReactive species:Unspecified reactive speciesWan-Feng Xu et. al.PubMed 32457417
Key facts
- Purity
- >=99% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag C-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
Amino acid sequence
M N K S L L K I I N D Y E E F S K G E E L C G V M T I S D S P R E Q D S E S Q T L D K V Y Q M K S K P R G Y C L I I N N H N F A K A R E K V P K L H S I R D R N G T H L D A G A L T T T F E E L H F E I K P H D D C T V E Q I Y E I L K I Y Q L M D H S N M D C F I C C I L S H G D K G I I Y G T D G Q E A P I Y E L T S Q F T G L K C P S L A G K P K V F F I Q A C Q G D N Y Q K G I P V E T D S E E Q P Y L E M D L S S P Q T R Y I P D E A D F L L G M A T V N N C V S Y R N P A E G T W Y I Q S L C Q S L R E R C P R G D D I L T I L T E V N Y E V S N K D D K K N M G K Q M P Q P T F T L R K K L V F P S D H H H H H H
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Target data
Function
Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224). Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for FAS/CD95-mediated and TNFRSF1A-induced cell death (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224). Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (PubMed:16916640, PubMed:8962078, PubMed:9006941). Binding to the adapter molecule FADD recruits it to either receptor FAS/TNFRSF6 or TNFRSF1A (PubMed:8681376, PubMed:8681377). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed:9184224). The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (PubMed:9184224). Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (PubMed:9184224). In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-324', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (PubMed:31827280, PubMed:31827281). Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-C and -D (GSDMC and GSDMD, respectively): gasdermin cleavage promotes release of the N-terminal moiety that binds to membranes and forms pores, triggering pyroptosis (PubMed:32929201, PubMed:34012073). Initiates pyroptosis following inactivation of MAP3K7/TAK1 (By similarity). Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production (By similarity). May participate in the Granzyme B (GZMB) cell death pathways (PubMed:8755496). Cleaves PARP1 and PARP2 (PubMed:8681376). Independent of its protease activity, promotes cell migration following phosphorylation at Tyr-380 (PubMed:18216014, PubMed:27109099). Isoform 5. Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex. Isoform 6. Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex. Isoform 7. Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex (Probable). Acts as an inhibitor of the caspase cascade (PubMed:12010809). Isoform 8. Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex.
Alternative names
MCH5, CASP8, Caspase-8, CASP-8, Apoptotic cysteine protease, Apoptotic protease Mch-5, CAP4, FADD-homologous ICE/ced-3-like protease, FADD-like ICE, ICE-like apoptotic protease 5, MORT1-associated ced-3 homolog, FLICE, MACH
Recommended products
Recombinant human Caspase-8 protein is a Human Fragment protein, in the 200 to 496 aa range, expressed in Escherichia coli, with >=99% purity and suitable for SDS-PAGE, FuncS.
Key facts
- Purity
- >=99% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag C-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
- Biological activity
- Specific Activity: ≥ 1145 pmol/min/μg
- Accession
- Q14790-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Preservative: 1.36% Imidazole
Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.02% Potassium chloride
Sequence info
Amino acid sequence
- M N K S L L K I I N D Y E E F S K G E E L C G V M T I S D S P R E Q D S E S Q T L D K V Y Q M K S K P R G Y C L I I N N H N F A K A R E K V P K L H S I R D R N G T H L D A G A L T T T F E E L H F E I K P H D D C T V E Q I Y E I L K I Y Q L M D H S N M D C F I C C I L S H G D K G I I Y G T D G Q E A P I Y E L T S Q F T G L K C P S L A G K P K V F F I Q A C Q G D N Y Q K G I P V E T D S E E Q P Y L E M D L S S P Q T R Y I P D E A D F L L G M A T V N N C V S Y R N P A E G T W Y I Q S L C Q S L R E R C P R G D D I L T I L T E V N Y E V S N K D D K K N M G K Q M P Q P T F T L R K K L V F P S D H H H H H H
- Accession
- Q14790
- Protein length
- Fragment
- Predicted molecular weight
- 34.5 kDa
- Amino acids
- 200 to 496
- Nature
- Recombinant
- Tags
- His tag C-Terminus
Specifications
- Form
- Liquid
General info
- Function
Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224). Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for FAS/CD95-mediated and TNFRSF1A-induced cell death (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224). Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (PubMed:16916640, PubMed:8962078, PubMed:9006941). Binding to the adapter molecule FADD recruits it to either receptor FAS/TNFRSF6 or TNFRSF1A (PubMed:8681376, PubMed:8681377). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed:9184224). The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (PubMed:9184224). Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (PubMed:9184224). In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-324', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (PubMed:31827280, PubMed:31827281). Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-C and -D (GSDMC and GSDMD, respectively): gasdermin cleavage promotes release of the N-terminal moiety that binds to membranes and forms pores, triggering pyroptosis (PubMed:32929201, PubMed:34012073). Initiates pyroptosis following inactivation of MAP3K7/TAK1 (By similarity). Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production (By similarity). May participate in the Granzyme B (GZMB) cell death pathways (PubMed:8755496). Cleaves PARP1 and PARP2 (PubMed:8681376). Independent of its protease activity, promotes cell migration following phosphorylation at Tyr-380 (PubMed:18216014, PubMed:27109099).
- Sequence similarities
Belongs to the peptidase C14A family.
- Post-translational modifications
Generation of the p10 and p18 subunits requires association with the death-inducing signaling complex (DISC), whereas additional processing is likely due to the autocatalytic activity of the activated protease. GZMB and CASP10 can be involved in these processing events.
- Subcellular localisation
- Nucleus
Storage
- Shipped at conditions
- Dry Ice
- Appropriate short-term storage conditions
- -80°C
- Appropriate long-term storage conditions
- -80°C
- Storage information
- Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Notes
Peptide notes: Autocleaved between the prodomain and large protease subunit (p18). The cleavage product, p30, contains both the large (p18) and small (p10 [His-tag]) protease subunits. p30 is further processed to the p18 and p10 subunits, which dimerize to form active enzyme.
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2 product images
SDS-PAGE - Recombinant human Caspase-8 protein (ab198070)
4-20% SDS-PAGE analysis of ab198070 (7 μg) with Coomassie staining.
Functional Studies - Recombinant human Caspase-8 protein (ab198070)
Example of specific activity of ab198070.
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