Human Pyrin domain-containing protein 1 (PYDC1) ELISA Kit

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AE24919HU
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Product Name Human Pyrin domain-containing protein 1 (PYDC1) ELISA Kit
Description ASC2, a PYD-only protein that functions as a modulator of multidomain PYD-containing proteins involved in NF-kappaB and caspase-1 activation. ASC2 adopts a six-helix bundle structure with a prominent loop, comprising 13 amino acid residues, between helices two and three. This loop represents a divergent feature of PYDs from other domains with the DD fold. Detailed analysis of backbone 15N NMR relaxation data using both the Lipari-Szabo model-free and reduced spectral density function formalisms revealed no evidence of contiguous stretches of polypeptide chain with dramatically increased internal motion, except at the extreme N and C termini. Some mobility in the fast, picosecond to nanosecond timescale, was seen in helix 3 and the preceding alpha2-alpha3 loop, in stark contrast to the complete disorder seen in the corresponding region of the NALP1 PYD. This assay has high sensitivity and excellent specificity for detection of Human PYDC1. No significant cross-reactivity or interference between Human PYDC1 and analogues was observed.
Synonyms ASC2, POP1, PYC1, PAAD-only protein|pyrin domain containing 1|pyrin-domain containing protein 1|pyrin-only protein 1
Method Sandwich ELISA
Detection Range Request Information
Sensitivity Request Information
Reactivity Human
Sample Types Serum, Plasma, Other biological fluids.
Background ASC2, a PYD-only protein that functions as a modulator of multidomain PYD-containing proteins involved in NF-kappaB and caspase-1 activation. ASC2 adopts a six-helix bundle structure with a prominent loop, comprising 13 amino acid residues, between helices two and three. This loop represents a divergent feature of PYDs from other domains with the DD fold. Detailed analysis of backbone 15N NMR relaxation data using both the Lipari-Szabo model-free and reduced spectral density function formalisms revealed no evidence of contiguous stretches of polypeptide chain with dramatically increased internal motion, except at the extreme N and C termini. Some mobility in the fast, picosecond to nanosecond timescale, was seen in helix 3 and the preceding alpha2-alpha3 loop, in stark contrast to the complete disorder seen in the corresponding region of the NALP1 PYD.
Supplier Abebio

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