Anoikis And Caspase-8

Caspase-8 IETD-R110 Fluorometric and Colorimetric Assay Kit (25 assays)

30011-1 1KIT
EUR 244.8
Description: Minimum order quantity: 1 unit of 1KIT

Caspase Assay Laboratories manufactures the anoikis and caspase-8 reagents distributed by Genprice. The Anoikis And Caspase-8 reagent is RUO (Research Use Only) to test human serum or cell culture lab samples. To purchase these products, for the MSDS, Data Sheet, protocol, storage conditions/temperature or for the concentration, please contact caspase assay. Other Anoikis products are available in stock. Specificity: Anoikis Category: And Group: Caspase-8

Caspase-8 Fluorometric Assay Kit

each
EUR 248.4

Caspase-8 Fluorometric Assay Kit

each
EUR 1149.6

Caspase-8 Colorimetric Assay Kit

each
EUR 744

Caspase-8 Colorimetric Assay Kit

each
EUR 248.4

Caspase-8 Colorimetric Assay Kit

each
EUR 1149.6

Caspase-8 Fluorometric Assay Kit

100 assays
EUR 568.8

Caspase-8 Fluorometric Assay Kit

200 assays
EUR 835.2

Caspase-8 information

Caspase-8 Antibody

3158-100 each
EUR 379.2

Caspase-8 Antibody

3158-30T each
EUR 175.2

Caspase-8 Antibody

3020-100 each
EUR 418.8

Caspase-8 Antibody

3020-30T each
EUR 175.2

Caspase-8 Antibody

3473-002mg 0.02 mg
EUR 206.18
Description: Caspase-8 Antibody: Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. The apoptotic subfamily can be further divided into initiator caspases, which are activated in response to death signals, and executioner caspases, which are activated by the initiator caspases and are responsible for cleavage of cellular substrates that ultimately lead to cell death. Caspase-8 is an initiator caspase that was identified as a member of the Fas/APO-1 death-inducing signaling complex. The adaptor molecule FADD couples procaspase-8 to the Fas receptor death domain; subsequent oligomerization promotes procaspase-8 autoactivation. FLIP, a catalytically inactive caspase-8-like molecule inhibits these interactions and thus can inhibit apoptosis.

Caspase-8 Antibody

3473-01mg 0.1 mg
EUR 523.7
Description: Caspase-8 Antibody: Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. The apoptotic subfamily can be further divided into initiator caspases, which are activated in response to death signals, and executioner caspases, which are activated by the initiator caspases and are responsible for cleavage of cellular substrates that ultimately lead to cell death. Caspase-8 is an initiator caspase that was identified as a member of the Fas/APO-1 death-inducing signaling complex. The adaptor molecule FADD couples procaspase-8 to the Fas receptor death domain; subsequent oligomerization promotes procaspase-8 autoactivation. FLIP, a catalytically inactive caspase-8-like molecule inhibits these interactions and thus can inhibit apoptosis.

Caspase-8 Antibody

3475-002mg 0.02 mg
EUR 206.18
Description: Caspase-8 Antibody: Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. The apoptotic subfamily can be further divided into initiator caspases, which are activated in response to death signals, and executioner caspases, which are activated by the initiator caspases and are responsible for cleavage of cellular substrates that ultimately lead to cell death. Caspase-8 is an initiator caspase that was identified as a member of the Fas/APO-1 death-inducing signaling complex. The adaptor molecule FADD couples procaspase-8 to the Fas receptor death domain; subsequent oligomerization promotes procaspase-8 autoactivation. FLIP, a catalytically inactive caspase-8-like molecule inhibits these interactions and thus can inhibit apoptosis. This antibody will only detect isoform E of caspase-8.

Caspase-8 Antibody

3475-01mg 0.1 mg
EUR 523.7
Description: Caspase-8 Antibody: Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. The apoptotic subfamily can be further divided into initiator caspases, which are activated in response to death signals, and executioner caspases, which are activated by the initiator caspases and are responsible for cleavage of cellular substrates that ultimately lead to cell death. Caspase-8 is an initiator caspase that was identified as a member of the Fas/APO-1 death-inducing signaling complex. The adaptor molecule FADD couples procaspase-8 to the Fas receptor death domain; subsequent oligomerization promotes procaspase-8 autoactivation. FLIP, a catalytically inactive caspase-8-like molecule inhibits these interactions and thus can inhibit apoptosis. This antibody will only detect isoform E of caspase-8.

Caspase-8 Antibody

48679-100ul 100ul
EUR 399.6

Caspase-8 Antibody

48679-50ul 50ul
EUR 286.8

Caspase-8 Antibody

49184-100ul 100ul
EUR 399.6

Caspase-8 Antibody

49184-50ul 50ul
EUR 286.8

Caspase-8 Antibody

R30365 100 ug
EUR 356.15
Description: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases including CASP3/4/6/7/9/10. [UniProt]

Caspase-8 Antibody

R30599 100 ug
EUR 356.15
Description: The human CASP8 gene, whose product is also known as Caspase-8 and FLICE, encodes an interleukin-1beta converting enzyme (ICE)-related cysteine protease that is activated by the engagement of several different death receptors. It is immediately recruited to the Fas receptor once it oligomerizes, and its protease activity is crucial for the apoptotic response generated by the resulting death-inducing signaling complex (DISC). This gene contains at least 11 exons spanning approximately 30kb on human chromosome band 2q33-34. This region of chromosome 2 was previously reported as the location of the CASP10 gene, whose product is closely related to CASP8. Caspase-8 deficiency in humans is compatible with normal development and shows that the enzyme has a postnatal role in immune activation of naive lymphocytes.

Caspase-8 Antibody

R30825 100 ug
EUR 356.15
Description: The human CASP8 gene, whose product is also known as Caspase-8 and FLICE, encodes an interleukin-1beta converting enzyme (ICE)-related cysteine protease that is activated by the engagement of several different death receptors. It is immediately recruited to the Fas receptor once it oligomerizes, and its protease activity is crucial for the apoptotic response generated by the resulting death-inducing signaling complex (DISC). This gene contains at least 11 exons spanning approximately 30kb on human chromosome band 2q33-34. This region of human chromosome 2 was previously reported as the location of the CASP10 gene, whose product is closely related to CASP8. Caspase-8 deficiency in humans is compatible with normal development and shows that the enzyme has a postnatal role in immune activation of naive lymphocytes.

Caspase-8 Antibody

R31744 100 ug
EUR 356.15
Description: Caspase-8 is also known as CASP8, CAP4, MACH or MCH5. This gene encodes a member of the cysteine-aspartic acid protease family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined.

Caspase-8 Antibody

RQ6952 100 ug
EUR 356.15
Description: CASP8 is also known as CAP4, MACH or MCH5. 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 composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. In addtion, this protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined.