Pycard (NM_023258) Mouse Tagged ORF Clone Lentiviral Particle

CAT#: MR201872L3V

  • LentiORF®

Lenti ORF particles, Pycard (Myc-DDK-tagged) - Mouse PYD and CARD domain containing (Pycard), 200ul, >10^7 TU/mL

ORF Plasmid: DDK tGFP

Lentiviral Particles: DDK w/ Puro mGFP w/ Puro

AAV Particle: DDK



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Buy this product and get 50% off on the Lenti RapidTiter kit. Use Code: Rapid50

USD 850.00

7 Weeks*

Size
    • 200 ul

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Specifications

Product Data
Type Mouse Tagged ORF Clone
Tag Myc-DDK
Symbol Pycard
Synonyms 9130417A21Rik; Asc; CARD5; masc; TMS-1; TNS1
Mammalian Cell Selection Puromycin
Vector pLenti-C-Myc-DDK-P2A-Puro
ACCN NM_023258
ORF Size 579 bp
Sequence Data
The ORF insert of this clone is exactly the same as(MR201872).
OTI Disclaimer The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info
OTI Annotation This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene.
Reference Data
RefSeq NM_023258.3
RefSeq Size 1286 bp
RefSeq ORF 582 bp
Locus ID 66824
UniProt ID Q9EPB4
Cytogenetics 7 F3
Gene Summary Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA (PubMed:28314590).[UniProtKB/Swiss-Prot Function]

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