Recombinant Human Toll/Interleukin-1 Receptor Domain-Containing Adapter Protein (TIRAP) Protein (GST)

Name: Recombinant Human Toll/Interleukin-1 Receptor Domain-Containing Adapter Protein (TIRAP) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09212P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Toll/Interleukin-1 Receptor Domain-Containing Adapter Protein (TIRAP) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P58753
Target Symbol	TIRAP
Synonyms	TIRAP; MAL; Toll/interleukin-1 receptor domain-containing adapter protein; TIR domain-containing adapter protein; Adaptor protein Wyatt; MyD88 adapter-like protein; MyD88-2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MASSTSLPAPGSRPKKPLGKMADWFRQTLLKKPKKRPNSPESTSSDASQPTSQDSPLPPSLSSVTSPSLPPTHASDSGSSRWSKDYDVCVCHSEEDLVAAQDLVSYLEGSTASLRCFLQLRDATPGGAIVSELCQALSSSHCRVLLITPGFLQDPWCKYQMLQALTEAPGAEGCTIPLLSGLSRAAYPPELRFMYYVDGRGPDGGFRQVKEAVMRYLQTLS
Expression Range	1-221aa
Protein Length	Full Length
Mol. Weight	50.9kDa
Research Area	Immunology
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	Adapter involved in TLR2 and TLR4 signaling pathways in the innate immune response. Acts via IRAK2 and TRAF-6, leading to the activation of NF-kappa-B, MAPK1, MAPK3 and JNK, and resulting in cytokine secretion and the inflammatory response. Positively regulates the production of TNF-alpha and interleukin-6.
Subcellular Location	Cytoplasm. Cell membrane. Membrane. Note=Colocalizes with DAB2IP at the plasma membrane.
Database References	HGNC: 17192 OMIM: 606252 KEGG: hsa:114609 STRING: 9606.ENSP00000376445 UniGene: PMID: 28225045 MAL is not disulfide-bonded and requires glutathionylation of C91 for signaling. PMID: 28739909 The Mal-Toll/interleukin-1 receptor (TIR) domains AB loop is capable of mediating direct binding to the TIR domains of TLR4 and MyD88 simultaneously. PMID: 22485159 MAL is multifunctional and integral for the molecular control of bacterial infections as well as inflammatory diseases. [Review] PMID: 23983209 Data indicate that TcpB (Q8YF5, BtpA/Btp1) interacts with MAL, MyD88, and TLR4 but interferes only with the MAL-TLR4 interaction. PMID: 24265315 Docking and physicochemical studies indicated that BTK was involved in close contact with Tyr86 and Tyr106 of MAL, whereas PKCdelta may phosphorylate Tyr106 only. PMID: 24840642 Results show that MAL protein binds to and regulates MYD88. PMID: 26876098 Here the authors show that MAL TIR domains spontaneously and reversibly form filaments in vitro. They also form cofilaments with TLR4 TIR domains and induce formation of MyD88 assemblies. PMID: 28759049 The major allele A of rs2511521 located in DRD2 and the minor allele T of rs625413 located in TIRAP are significantly associated with increased risk of food addiction in overweight/obese subjects with low/zero food addiction symptoms. PMID: 28115213 Combined targeting of UBAP1 and toll-like receptor adaptors TIRAP and MyD88 by Pseudomonas aeruginosa PumA impedes both cytokine and toll-like receptor signalling, highlighting a novel strategy for innate immune evasion. PMID: 28483816 Epistatic interaction between MyD88 and TIRAP against Helicobacter pylori. PMID: 27296467 Presence of at least one copy of the TIRAP (2054C > T) variant may be associated with severity of bronchopulmonary dysplasia among preterm neonates. PMID: 27457283 Chances of malaria caused by Plasmodium falciparum were low in CC genotype carriers in comparison to other genotypes PMID: 26614847 TIRAP polymorphisms are associated with progression and survival of patients with symptomatic myeloma. PMID: 26564000 This present meta-analysis suggests TIRAP C539T polymorphism is significantly correlated with reduced risk of TB infection, with stronger effect in European. PMID: 25003251 Evaluated the possible association between TIRAP rs1893352 and rs8177374 (S180L) gene polymorphisms and pulmonary tuberculosis in a sample of Iranian population. PMID: 25066393 CCL2rs2530797A/A and TIRAPrs8177376A/A were associated to an increase susceptibility to Chagas disease cardiomyopathy. PMID: 24330528 TIRAP rs81777374 is associated with resistance to pulmonary tuberculosis. PMID: 24067789 Data indicate that TcpB (NP_540591) may mimic the function of TIRAP through their similar TIR domain structures. PMID: 24275656 PSP has an immunoregulatory effect through regulation of the TLR4-TIRAP/MAL-MyD88 signaling pathway. PMID: 23802631 the results of our study suggest that there is a defect of TIRAP and MyD88 proteins in B-CLL lymphocytes. PMID: 23419703 TIRAP S180L polymorphism is not increased in Behcet's disease patients in Italian or Turkish populations. PMID: 24064014 In our study, a TLR pathway adapter variant (TIRAP (rs8177374)) protected against preterm birht<32 weeks, supporting our hypothesis that genetic variation in the innate immune signaling pathway contributes to altered risk of PTB. PMID: 23047423 MyD88 exerts antiapoptotic functions in colon cancer cells via the Ras/Erk, but not the NF-kappaB, pathway. MyD88 inhibition leads to defective ERCC1-dependent DNA repair and to accumulation of DNA damage, resulting in cancer cell death via p53. PMID: 23766530 Identification of binding sites for myeloid differentiation primary response gene 88 (MyD88) and Toll-like receptor 4 in MyD88 adapter-like (Mal). PMID: 23460645 PIP5Kalpha promotes TLR4-associated microglial inflammation by mediating PIP(2)-dependent recruitment of TIRAP to the plasma membrane PMID: 23297396 Compared to white women, African American women with clinically suspected pelvic inflammatory disease were more likely to carry variants in the TLR1, TLR2, and TIRAP genes. PMID: 23255565 induction of both IL-6 and IL-8 is associated with elevated TIRAP and reduced TRAM mRNA expression PMID: 22970235 Data suggest a protection effect of the Mal/TIRAP S180L SNP against serious infections in HIV-1 infected individuals with low CD4 cell counts. PMID: 22683004 Data indicate that MyD88 works together with the IL-1/IL-18 receptors, can interact with two distinct sorting adaptors, TRAM and Mal, in a conserved manner. PMID: 22685567 Poxviral protein A46 inhibits TLR4 signaling and interacts with Toll-IL-1 receptor (TIR) domain-containing proteins of the receptor complex. PMID: 22593572 TIRAP S180L polymorphism is unlikely to substantially contribute to tuberculosis susceptibility (Meta-analysis) PMID: 21419702 Blocking of the function of TIRAP and MyD88 largely abrogated intracellular signaling from ligand-activated RAGE PMID: 21829704 TIRAP G286A (D96N) polymorphism is associated with susceptibility to tuberculosis. PMID: 21218381 TIRAP 180Leu was significantly associated with Behcet's disease in UK, but not Middle Eastern, patients. PMID: 21705416 a molecular and structural basis for the role of MAL in TLR signaling and disease protection. PMID: 21873236 RA synovium showed abundant expression of TLR. RA synovitis tissue seems to be responsive to TLR ligands. PMID: 21324962 Comparison of the tirap S180L genotypes between patients with mild malaria and those healthy individuals showed that the frequency of heterozygosity was significantly higher in infected than non-infected individuals. PMID: 21457584 Data demonstrate a key role for Mal in mediating TLR2 and TLR4 activation of CREB and induction of CREB-responsive genes including Il-10. PMID: 21398611 Genetic variations in MyD88 adaptor-like are associated with atopic dermatitis PMID: 21399862 TIRAP gene might be associated with susceptibility to sepsis-associated acute lung injury in the Han Chinese population. PMID: 21118491 Patients simultaneously carrying polymorphisms in TIRAP/Mal and TLR4 and patients homozygous for the TIRAP/Mal SNP had a significantly higher risk of severe infections after surgery PMID: 20525286 The recessive homozygous genotype for a single-nucleotide polymorphisms in the TIRAP (also known as MAL) gene (rs1893352) was strongly associated with nonmeningitis cases of haemophilus influenzae serotype b vaccine failure. PMID: 20804371 An Asp96Asn single nucleotide polymorphism prevents Mal from recruiting its signaling partner MyD88 to the plasma membrane and fails to induce NF-kappa B signaling in human tumor line Huh-7 hepatocytes. PMID: 20164415 Data show that AIP1 is a novel GTPase-activating protein for Arf6, a small GTPase regulating cellular PIP(2) production and formation of the TLR4-TIRAP-MyD88 complex. PMID: 19948740 A TIR domain variant of MyD88 adapter-like (Mal)/TIRAP results in loss of MyD88 binding and reduced TLR2/TLR4 signaling. PMID: 19509286 Polymorphisms in TIRAP do not appear to be involved in childhood tuberculosis susceptibility in South Africa, but may play a role in determining occurrence of tubercular meningitis PMID: 19693265 MyD88 and Mal/TIRAP are essential for LPS-induced I kappa B alpha phosphorylation, NF-kappa B activation, and interleukin 6 (IL-6) or IL-8 production in fibroblasts and endothelial cells in a pathway that also requires IKK2. PMID: 14630816 involvement of a previously uncharacterized, evolutionarily conserved TIR domain protein in innate immunity that is functionally distinct from other known TIR domain signaling adapters PMID: 15123841 activation of Rac1 leads to HIV-LTR trans-activation, mediated through TIRAP. Rac1 and TIRAP are important in TLR4 activation of HIV replication PMID: 15187145

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.