NLR Family, Pyrin Domain Containing 1 (NLRP1) (C-Term) antibody

Details for Product No. ABIN500310
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

 
Antigen
Synonyms CARD7, CIDED, CLR17.1, DEFCAP, DEFCAP-L/S, NAC, NALP1, PP1044, SLEV1, VAMAS1, Gm14, Gm15, Nalp1, Nalp1a, Nlrp1
Epitope
C-Term
(13), (3), (2), (2), (1), (1), (1), (1), (1)
Reactivity
Human
(53), (12), (11), (1)
Host
Rabbit
(48), (6), (1)
Clonality
Polyclonal
Conjugate
Un-conjugated
(1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
ELISA, Immunocytochemistry (ICC), Immunofluorescence (IF), Western Blotting (WB)
(38), (18), (14), (12), (11), (9), (6), (5), (5), (1), (1)
Pubmed 4 references available
Catalog no. ABIN500310
Quantity 0.1 mg
Price
401.50 $   Plus shipping costs $45.00
Shipping to United States (Change)
Availability Will be delivered in 6 to 8 Business Days

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Immunogen NALP1 antibody was raised against a peptide corresponding to 13 amino acids near the carboxy-terminus of human NALP1.
Isotype IgG
Specificity This antibody detects CARD7 / NLRP1. Species Reactivity: Tested: Human
Purification Peptide affinity chromatography
Alternative Name CARD7 / NLRP1
Background NALP1 belongs to a family of cytoplasmic proteins that have been implicated in cell responses to apoptotic and inflammatory stimuli (1). It contains a caspase recruitment domain (CARD) in addition to a NACHT domain and leucine rich repeat (LRR). This protein interacts strongly with caspase 2 and weakly with caspase 9, as well as with Apaf-1 (2). Transient overexpression of this gene in cultured cells was sufficient to induce apoptosis (3). NALP1 mRNA and protein expression levels in myeloid leukemia cells are increased following CREB (cAMP-response element binding protein) activation, suggesting that NALP1 may contribute to modulate the response of these cells to pro-inflammatory stimuli (4). Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for NALP1 (3).
Alternate names: Caspase recruitment domain-containing protein 7, DEFCAP, Death effector filament-forming ced-4-like apoptosis protein, KIAA0926, LRR and PYD domains-containing protein 1, NAC, NACHT, NALP1, Nucleotide-binding domain and caspase recruitment domain
Gene ID 22861
NCBI Accession AAG30288
UniProt Q9C000
Application Notes ELISA. Western blot. Immunocytochemistry. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Format Liquid
Buffer PBS containing 0.02% sodium azide
Preservative Sodium azide
Handling Advice Avoid repeated freezing and thawing.
Storage 4 °C/-20 °C
Storage Comment Store at 2 - 8 °C for up to one month or (in aliquots) at -20 °C for longer.
Expiry Date 12 months
Background publications Hlaing, Guo, Dilley et al.: "Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins." in: The Journal of biological chemistry, Vol. 276, Issue 12, pp. 9230-8, 2001 (PubMed).

Chu, Pio, Xie et al.: "A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis." in: The Journal of biological chemistry, Vol. 276, Issue 12, pp. 9239-45, 2001 (PubMed).

Tschopp, Martinon, Burns: "NALPs: a novel protein family involved in inflammation." in: Nature reviews. Molecular cell biology, Vol. 4, Issue 2, pp. 95-104, 2003 (PubMed).

Sanz, Calasanz, Andreu et al.: "NALP1 is a transcriptional target for cAMP-response-element-binding protein (CREB) in myeloid leukaemia cells." in: The Biochemical journal, Vol. 384, Issue Pt 2, pp. 281-6, 2004 (PubMed).

Hosts (48), (6), (1)
Reactivities (53), (12), (11), (1)
Applications (38), (18), (14), (12), (11), (9), (6), (5), (5), (1), (1)
Conjugates (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Epitopes (13), (3), (2), (2), (1), (1), (1), (1), (1)
back to top