Rabbit Anti-NAIP Recombinant Antibody (
13E6) (V2LY-0725-LY1269)

Name: Rabbit Anti-NAIP Recombinant Antibody (13E6)
SKU: V2LY-0725-LY1269
Rating: 5 (1 reviews)

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Tested Data

Rabbit Anti-NAIP Recombinant Antibody (13E6) (V2LY-0725-LY1269) in IHC

IHC image of V2LY-0725-LY1269 diluted at 1:80 and staining in paraffin-embedded human placenta tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.48% DAB.

Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Rabbit

Clone

13E6

Application

ELISA, IHC

Immunogen

A synthesized peptide derived from Human NAIP.

Host Species

Rabbit

Specificity

Human

Antibody Isotype

IgG

Clonality

Monoclonal Antibody

Application Notes

Application	Note
IHC	1:50-1:200

Formulations & Storage [For reference only, actual COA shall prevail!]

Format

Liquid

Buffer

PBS, glycerol

Preservative

Sodium azide

Concentration

Batch dependent

Purity

> 95% Purity determined by SDS-PAGE.

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

More Infomation

Target

Full Name

NLR Family Apoptosis Inhibitory Protein

Entrez Gene ID

4671

UniProt ID

Q13075

Function

Anti-apoptotic protein which acts by inhibiting the activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in pathological conditions. Prevents motor-neuron apoptosis induced by a variety of signals. Possible role in the prevention of spinal muscular atrophy that seems to be caused by inappropriate persistence of motor-neuron apoptosis: mutated or deleted forms of NAIP have been found in individuals with severe spinal muscular atrophy.

Acts as a sensor component of the NLRC4 inflammasome that specifically recognizes and binds needle protein CprI from pathogenic bacteria C.violaceum. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria such as C.violaceum and L.pneumophila.

Biological Process

Defense response to bacterium Source: GO_Central
Detection of bacterium Source: GO_Central
Icosanoid biosynthetic process Source: ComplexPortal
Inflammatory response Source: GO_Central
Innate immune response Source: UniProtKB-KW
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Negative regulation of neuron apoptotic process Source: UniProtKB
Negative regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
Nervous system development Source: ProtInc
Pattern recognition receptor signaling pathway Source: ComplexPortal
Positive regulation of inflammatory response Source: ComplexPortal
Positive regulation of interleukin-1 beta production Source: ComplexPortal
Positive regulation of JNK cascade Source: UniProtKB
Pyroptosis Source: GO_Central
Regulation of apoptotic process Source: UniProtKB

Cellular Location

Cytosol
inflammasome complex
IPAF inflammasome complex
Plasma Membrane
basolateral plasma membrane
Other locations
cytoplasm

Matico, R. E., Yu, X., Miller, R., Somani, S., Ricketts, M. D., Kumar, N., ... & Sharma, S. (2024). Structural basis of the human NAIP/NLRC4 inflammasome assembly and pathogen sensing. Nature Structural & Molecular Biology, 1-10.

Amaral, M. P., Cardoso, F. D., de Farias, I. S., de Souza, R. Q., Matteucci, K. C., Torrecilhas, A. C., & Bortoluci, K. R. (2023). NAIP/NLRC4 inflammasome participates in macrophage responses to Trypanosoma cruzi by a mechanism that relies on cathepsin-dependent caspase-1 cleavage. Frontiers in Immunology, 14.

Paidimuddala, B., Cao, J., Nash, G., Xie, Q., Wu, H., & Zhang, L. (2023). Mechanism of NAIP—NLRC4 inflammasome activation revealed by cryo-EM structure of unliganded NAIP5. Nature Structural & Molecular Biology, 30(2), 159-166.

Triantafilou, K., Ward, C. J., Czubala, M., Ferris, R. G., Koppe, E., Haffner, C., ... & Triantafilou, M. (2021). Differential recognition of HIV-stimulated IL-1β and IL-18 secretion through NLR and NAIP signalling in monocyte-derived macrophages. PLoS Pathogens, 17(4), e1009417.

Kay, C., Wang, R., Kirkby, M., & Man, S. M. (2020). Molecular mechanisms activating the NAIP‐NLRC4 inflammasome: implications in infectious disease, autoinflammation, and cancer. Immunological reviews, 297(1), 67-82.

Bauer, R., & Rauch, I. (2020). The NAIP/NLRC4 inflammasome in infection and pathology. Molecular Aspects of Medicine, 76, 100863.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

For research use only. Not intended for any clinical use.

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