Recombinant Bovine Nucleotide-Binding Oligomerization Domain-Containing Protein 2 (NOD2) Protein (His-KSI)

Name: Recombinant Bovine Nucleotide-Binding Oligomerization Domain-Containing Protein 2 (NOD2) Protein (His-KSI)
Brand: Beta LifeScience
SKU: BLC-01567P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Bovine Nucleotide-Binding Oligomerization Domain-Containing Protein 2 (NOD2) Protein (His-KSI) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q6E804
Target Symbol	NOD2
Synonyms	Caspase recruitment domain-containing protein 15
Species	BO-Bos taurus (Bovine)
Expression System	E.coli
Tag	N-6His-KSI
Target Protein Sequence	MCAQDAFQTQRSQLVELLVSGSLEGFESILDRLLSREVLSWEDYEGLSLVGQPISHLARRLLDTIWNKGTWGCEQLTAAVREAQADSQPPELPSSWDPHSPHPARDLQSHRPAIVRRLYGHVEGVLDLTQQRGFISQYETDEIRRPIFTSSQRARRLLDLATVKANGLAAFLLQCIQELPVPLALPFEDAA
Expression Range	1-191aa
Protein Length	Partial
Mol. Weight	36.8 kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Involved in gastrointestinal immunity. Upon stimulation by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, binds the proximal adapter receptor-interacting RIPK2, which recruits ubiquitin ligases as XIAP, BIRC2, BIRC3, INAVA and the LUBAC complex, triggering activation of MAP kinases and activation of NF-kappa-B signaling. This in turn leads to the transcriptional activation of hundreds of genes involved in immune response. Required for MDP-induced NLRP1-dependent CASP1 activation and IL1B release in macrophages. Component of an autophagy-mediated antibacterial pathway together with ATG16L1. Plays also a role in sensing single-stranded RNA (ssRNA) from viruses. Interacts with mitochondrial antiviral signaling/MAVS, leading to activation of interferon regulatory factor-3/IRF3 and expression of type I interferon.
Subcellular Location	Cytoplasm. Membrane. Basolateral cell membrane.
Database References	KEGG: bta:444867 STRING: 9913.ENSBTAP00000027887 UniGene: PMID: 27853874 Data indicate six single-nucleotide polymorphisms (SNPs) in the caspase recruitment domain 15 protein (CARD15) gene associated with susceptibility to bovine tuberculosis (BTB) in Chinese Holstein cows. PMID: 26244859 Data indicate that the Nod2 signaling adaptor protein (NOD2) G-->A at position 1594 bp plays a critical role in increasing 305-day milk yields. PMID: 25966125 Genetic variation and putative regulatory regions in bovine CARD15. PMID: 16897345 This study indicates that SNP c.3020A>T might play a role in the host response against mastitis and further detailed studies are needed to understand its functional mechanisms PMID: 18005441 A significant association was found between two polymorphisms of CARD15 and paratuberculosis status; cows with the heterozygous genotype were 3.35 times more likely to be infected than cows with the reference genotype. PMID: 18926647

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.