Recombinant Mouse Interferon-Induced Helicase C Domain-Containing Protein 1 (IFIH1) Protein (His)

Name: Recombinant Mouse Interferon-Induced Helicase C Domain-Containing Protein 1 (IFIH1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01657P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Interferon-Induced Helicase C Domain-Containing Protein 1 (IFIH1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q8R5F7
Target Symbol	IFIH1
Synonyms	Helicase with 2 CARD domains;Helicard;Interferon induced with helicase C domain protein 1;Melanoma differentiation-associated protein 5;MDA-5;RIG-I-like receptor 2;RLR-2
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	KLIKLRNTILEQFTRSEESSRGIIFTKTRQSTYALSQWIMENAKFAEVGVKAHHLIGAGHSSEVKPMTQTEQKEVISKFRTGEINLLIATTVAEEGLDIKECNIVIRYGLVTNEIAMVQARGRARADESTYVLVTSSGSGVTEREIVNDFREKMMYKAINRVQNMKPEEYAHKILELQVQSILEKKMKVKRSIAKQYNDNPSLITLLCKNCSMLVCSGENIHVIEKMHHVNMTPEFKGLYIVRENKALQKKFADYQTNGEIICKCGQAWGTMMVHKGLDLPCLKIRNFVVNFKNNSPKKQYKKWVELPIRFPDLDYSEYCLYSDED
Expression Range	700-1025aa
Protein Length	Partial
Mol. Weight	41.5 kDa
Research Area	Epigenetics And Nuclear Signaling
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	Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include mRNA lacking 2'-O-methylation at their 5' cap and long-dsRNA (>1 kb in length). Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Responsible for detecting the Picornaviridae family members such as encephalomyocarditis virus (EMCV), mengo encephalomyocarditis virus (ENMG), and theiler's murine encephalomyelitis virus (TMEV). Can also detect other viruses such as dengue virus (DENV), west Nile virus (WNV), and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome, such as vaccinia virus. Plays an important role in amplifying innate immune signaling through recognition of RNA metabolites that are produced during virus infection by ribonuclease L (RNase L). May play an important role in enhancing natural killer cell function and may be involved in growth inhibition and apoptosis in several tumor cell lines.
Subcellular Location	Cytoplasm. Nucleus. Mitochondrion.
Protein Families	Helicase family, RLR subfamily
Database References	KEGG: mmu:71586 STRING: 10090.ENSMUSP00000028259 UniGene: PMID: 29032202 These findings imply that MDA5-induced cell death and inflammation in the pancreas facilitate progression to autoimmune destruction of pancreatic beta-cells. PMID: 28851763 Mice with a knock-in mutation encoding IFIH1(T946) displayed enhanced basal expression of type I interferons, survived a lethal viral challenge and exhibited increased penetrance in autoimmune models, including a combinatorial effect with other risk variants. Furthermore, IFIH1(T946) mice manifested an embryonic survival defect consistent with enhanced responsiveness to RNA self ligands. PMID: 28553952 TRIM65 as an essential component for the MDA5 signaling pathway and provide physiological evidence showing that ubiquitination is important for MDA5 oligomerization and activation. PMID: 28031478 MDA-5 stimulation leads to endothelial dysfunction. PMID: 27130701 The p150 isoform of ADAR1 uniquely regulated the MDA5 pathway. PMID: 26588779 MDA5, detects viral RNA and triggers induction of type I interferons, chemical messengers that induce inflammation and help regulate the immune responses. PMID: 26423942 Duox2-derived reactive oxygen species are necessary for the innate immune response and trigger the induction of RIG-I and MDA5 to resist influenza A infection in human nasal epithelium and mouse nasal mucosa. PMID: 25751630 L region antisense RNA of EMCV is a key determinant of innate immunity to the virus and represents an RNA that activates LGP2 associated MDA5 in virally-infected cells. PMID: 24550253 embryonic death and phenotypes of Adar1(E861A/E861A) were rescued by concurrent deletion of the cytosolic sensor of dsRNA, MDA5. PMID: 26275108 IFIH1 heterozygous mice have a regulatory rather than effector T-cell response at the site of autoimmunity, supporting IFIH1 expression as an essential regulator of the diabetogenic T-cell response. PMID: 25591872 Our results, therefore, suggest that Arl5B is a negative regulator for MDA5. PMID: 25451939 TRIM13 interacts with MDA5 and negatively regulates MDA5-mediated type I IFN production PMID: 25008915 RIG-I and MDA-5 detection of viral RNA-dependent RNA polymerase activity restricts positive-strand RNA virus replication. PMID: 24039580 MDA5 modulates the development of chronic lung inflammation by regulating the early inflammatory response in the lung. PMID: 24417465 These results strongly suggest that RIG-I and MDA5 participate in innate antiviral responses in cochlear tissue. PMID: 23644230 These studies suggest that MDA5 in the immune priming environment shapes optimal CD8(+) T cell activation and subsequent clearance of West Nile virus from the central nervous system. PMID: 23966390 Thus, RIG-I and MDA5 are essential pattern recognition receptors that recognize distinct pathogen-associated molecular patterns that accumulate during West Nile virus replication. PMID: 23966395 Collectively, our in vitro and in vivo studies both support a critical role for MDA5 in the innate immune response against hepatitis B virus infection. PMID: 23926323 these findings suggest that mast cells produce cytokines and chemokines in the early infection stage after recognizing viruses via RIG-I and MDA5, and may contribute to antiviral responses PMID: 23171655 MDA5 localization to stress granules is not required for the induction of interferon alpha and beta during mengovirus infection PMID: 23536668 Myocardial MDA5 may be a key molecule in protecting the heart from direct viral injury and myocardial dysfunction. PMID: 23271791 MDA5 is a polymerization-dependent signaling platform that uses the amyloid-like self-propagating properties of mitochondrial antiviral-signaling protein to amplify signaling. PMID: 23090998 Pretreatment of mice with melanoma differentiation-associated gene 5 (MDA5) and IFN-beta promoter stimulator-1 ASOs. PMID: 22505629 MDA5 overexpression led to a chronic IFN-I state characterized by resistance to a lethal viral infection through rapid clearance of virus in the absence of a CD8(+) or Ab response PMID: 22205024 It was shown that MDA5 cooperatively binds short RNA ligands as a dimer with a 16-18-basepair footprint. A crystal structure of the MDA5 helicase-insert domain demonstrates an evolutionary relationship with the archaeal Hef helicases. PMID: 22314235 However, only MDA5 interacted with the V protein dependently on the C-terminal V unique (Vu) region, inhibiting IRF3 reporter activation. PMID: 21851384 MDA5 and TLR3 initiate pro-inflammatory signaling pathways leading to rhinovirus-induced airways inflammation and hyperresponsiveness. PMID: 21637773 Signaling through melanoma differentiation-associated (MDA)5 and RIG-I controls rotavirus production in intestinal epithelial cells. PMID: 21187438 These results demonstrate that mouse hepatitis virus is recognized by both RIG-I and MDA5 and induces IFN-alpha/beta through the activation of the IRF-3 signaling pathway. PMID: 20427526 MDA-5 plays an important role in the host immune response to CVB3 by preventing early virus replication and limiting tissue pathology. PMID: 20206372 MDA5 and Toll-like receptor 3 mediate substantially distinct yet complementary functions during polyinosinic:polycytidylic acid (poly I-C)-mediated activation of antigen-specific CD8 T cell responses. PMID: 20164430 These findings indicate that changes in MDA5 and PTPN2 expression modify beta-cell responses to dsRNA. PMID: 19825843 data suggest that LGP2 facilitates viral RNA recognition by RIG-I and MDA5 through its ATPase domain. PMID: 20080593 MDA5 is indispensable for sustained expression of IFN in response to paramyxovirus infection PMID: 20107606 Two RNA-sensing proteins, RIG-I and MDA5, participate in the IFN response to Legionella pneumophila. PMID: 19936053 stimulation with RNA viruses encephalomyocarditis virus and Sendai virus specifically activates MDA5 and RIG-I, blocking Treg cell function PMID: 19966212 MDA5 and its adaptor molecule MAVS are critical for type I interferon responses to CVB; the absence of either MAVS or MDA5 leads to deficient type I interferon production and early mortality PMID: 19846534 Data show that viral RNA stimulates glomerular mesangial cells to produce large amounts of type I IFN, especially when being delivered into the intracellular cytosol where it can interact with Mda5. PMID: 19850889 Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity. PMID: 16116171 RIG-I is essential for the production of interferons in response to RNA viruses including paramyxoviruses, influenza virus and Japanese encephalitis virus, whereas MDA5 is critical for picornavirus detection PMID: 16625202 mda-5-/- mice exhibited a selectively impaired antiviral response to encephalomyocarditis picornavirus, indicating functional specialization of mda-5 in vivo PMID: 16714379 These observations demonstrate differential and redundant roles for RIG-I and MDA5 in pathogen recognition and innate immune signaling. PMID: 17942531 RIG-I and MDA5 are responsible for triggering downstream gene expression in response to West Nile Virus infection by signaling through IPS-1. PMID: 17977974 offer biological relevance to the previously reported inhibition of MDA5 by different paramyxovirus V proteins PMID: 18354215 Collectively, RIG-I detects dsRNAs without a 5'-triphosphate end, and RIG-I and MDA5 selectively recognize short and long dsRNAs, respectively. PMID: 18591409 Data suggest that mouse hepatitis virus induces type I interferon in macrophages and microglia in the brain and is recognized by an MDA5-dependent pathway in macrophages. PMID: 18667505 Astrocytes recognize intracellular poly I-C via MDA-5. PMID: 19036857 activation of the virus-sensing MDA-5 receptor leads to a rapid and reversible involution of the thymus PMID: 19414755 two RIG-I-like receptors (RLRs), RIG-I and MDA5, known as cytosolic RNA receptors, nonredundantly function as cytosolic DNA receptors that lead to the selective activation of type I IFN genes PMID: 19805092

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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.

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