Asc (Unphosphorylated Tyr-144) Blocking Peptide
€155.00
In stock
SKU
ECM-AX5645
Background:
Host- and pathogen-associated cytoplasmic double-stranded DNA triggers the activation of a NALP3-independent inflammasome, which activates caspase-1, leading to maturation of pro-interleukin-1beta and inflammation. Several studies have isolated AIM2 (absent in melanoma 2) as a candidate cytoplasmic-DNA-sensing protein that contains an N-terminal pyrin domain and C-terminal oligonucleotide binding domain. A screen for transcripts induced by interferon-beta identified AIM2 gene expression. AIM2 protein bound double-stranded DNA, recruited the inflammasome adaptor ASC, and localized to ASC containing speckles. AIM2 and ASC form a pyroptosome, which induces pyroptotic cell death mediated by caspase-1. Asc can be phosphorylated at Tyr-144 in a Syk and JNK-dependent manner. This phosphorylation is critical for Asc speck formation and Caspas-1 activation.
Background References
:
Bürckstümmer, T. et al. (2009). Nat Immunol. 10(3):266.
Roberts, T.L. et al. (2009). Science. 323(5917):1057.
Hara, H. et al. (2013) Nature Immunol. 14(12):1247.
Sequence: Unphosphorylated Asc (Tyr-144) peptide corresponding to amino acid residues surrounding Tyr-144 in mouse Asc. This peptide sequence is highly conserved in human and rat Asc.
Specificity: The peptide is an unphosphorylated control peptide for AX5635. The peptide is recommended for use in ELISA and for blocking antibody reactivity in western blot and immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
Host- and pathogen-associated cytoplasmic double-stranded DNA triggers the activation of a NALP3-independent inflammasome, which activates caspase-1, leading to maturation of pro-interleukin-1beta and inflammation. Several studies have isolated AIM2 (absent in melanoma 2) as a candidate cytoplasmic-DNA-sensing protein that contains an N-terminal pyrin domain and C-terminal oligonucleotide binding domain. A screen for transcripts induced by interferon-beta identified AIM2 gene expression. AIM2 protein bound double-stranded DNA, recruited the inflammasome adaptor ASC, and localized to ASC containing speckles. AIM2 and ASC form a pyroptosome, which induces pyroptotic cell death mediated by caspase-1. Asc can be phosphorylated at Tyr-144 in a Syk and JNK-dependent manner. This phosphorylation is critical for Asc speck formation and Caspas-1 activation.
Background References
:
Bürckstümmer, T. et al. (2009). Nat Immunol. 10(3):266.
Roberts, T.L. et al. (2009). Science. 323(5917):1057.
Hara, H. et al. (2013) Nature Immunol. 14(12):1247.
Sequence: Unphosphorylated Asc (Tyr-144) peptide corresponding to amino acid residues surrounding Tyr-144 in mouse Asc. This peptide sequence is highly conserved in human and rat Asc.
Specificity: The peptide is an unphosphorylated control peptide for AX5635. The peptide is recommended for use in ELISA and for blocking antibody reactivity in western blot and immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
| Is Featured? | No |
|---|
Write Your Own Review