Analytical Data
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Gene name
NLRP11
- Application
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Alternative Names
CLR19.6; FLJ26273; NACHT leucine rich repeat and PYD containing 11; NACHT LRR and PYD domains containing protein 11; NACHT. LRR and PYD domains-containing protein 11; NAL11_HUMAN; NALP11; NLR family pyrin domain containing 11; NLRP11; NOD17; Nucleotide binding oligomerization domain protein 17; Nucleotide-binding oligomerization domain protein 17; Nucleotide-binding oligomerization domain. leucine rich repeat and pyrin domain containing 11; PAAD and NACHT containing protein 10B; PAAD and NACHT domain containing protein 10; PAAD-and NACHT domain-containing protein 10; PAN10; PYPAF6; PYPAF7; PYRIN containing APAF1 like protein 6; PYRIN-containing APAF1-like protein 6
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P59045
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Expression Region
1-1033 aa
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AA Sequence
MAESDSTDFDLLWYLENLSDKEFQSFKKYLARKILDFKLPQFPLIQMTKEELANVLPISYEGQYIWNMLFSIFSMMRKEDLCRKIIGRRNRNQEACKAVMRRKFMLQWESHTFGKFHYKFFRDVSSDVFYILQLAYDSTSYYSANNLNVFLMGERASGKTIVINLAVLRWIKGEMWQNMISYVVHLTSHEINQMTNSSLAELIAKDWPDGQAPIADILSDPKKLLFILEDLDNIRFELNVNESALCSNSTQKVPIPVLLVSLLKRKMAPGCWFLISSRPTRGNNVKTFLKEVDCCTTLQLSNGKREIYFNSFFKDRQRASAALQLVHEDEILVGLCRVAILCWITCTVLKRQMDKGRDFQLCCQTPTDLHAHFLADALTSEAGLTANQYHLGLLKRLCLLAAGGLFLSTLNFSGEDLRCVGFTEADVSVLQAANILLPSNTHKDRYKFIHLNVQEFCTAIAFLMAVPNYLIPSGSREYKEKREQYSDFNQVFTFIFGLLNANRRKILETSFGYQLPMVDSFKWYSVGYMKHLDRDPEKLTHHMPLFYCLYENREEEFVKTIVDALMEVTVYLQSDKDMMVSLYCLDYCCHLRTLKLSVQRIFQNKEPLIRPTASQMKSLVYWREICSLFYTMESLRELHIFDNDLNGISERILSKALEHSSCKLRTLKLSYVSTASGFEDLLKALARNRSLTYLSINCTSISLNMFSLLHDILHEPTCQISHLSLMKCDLRASECEEIASLLISGGSLRKLTLSSNPLRSDGMNILCDALLHPNCTLISLVLVFCCLTENCCSALGRVLLFSPTLRQLDLCVNRLKNYGVLHVTFPLLFPTCQLEELHLSGCFFSSDICQYIAIVIATNEKLRSLEIGSNKIEDAGMQLLCGGLRHPNCMLVNIGLEECMLTSACCRSLASVLTTNKTLERLNLLQNHLGNDGVAKLLESLISPDCVLKVVGLPLTGLNTQTQQLLMTVKERKPSLIFLSETWSLKEGREIGVTPASQPGSIIPNSNLDYMFFKFPRMSAAMRTSNTASRQPL
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Molecular Weight
144.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
NLRP11 is a member of the NLR (NOD-like receptor) family, which plays a crucial role in the innate immune system by detecting intracellular pathogens and initiating inflammatory responses. Recent studies have highlighted the importance of NLRP11 in modulating immune responses, particularly its potential involvement in the regulation of autophagy and the activation of pro-inflammatory cytokines. Research has shown that NLRP11 may influence various diseases, including infections and autoimmune disorders, making it a significant target for therapeutic interventions. Recombinant proteins of NLRP11 are being developed to explore its functional properties in detail and to understand its role in signaling pathways that govern immune responses. The production of NLRP11 recombinant protein allows for biochemical assays and structural analysis, which can facilitate the identification of its ligand interactions and downstream signaling mechanisms. Furthermore, studying NLRP11 in a controlled experimental setting promotes insights into its potential as a biomarker for disease diagnosis and prognosis, revealing its implications in both fundamental immunology and clinical applications. Overall, the investigation of NLRP11 recombinant proteins is essential for unraveling the complexities of immune regulation and developing novel strategies for managing immune-related diseases.
