Recombinant Human Myeloid Differentiation Primary Response Protein Myd88 (MYD88) Protein (His)

Name: Recombinant Human Myeloid Differentiation Primary Response Protein Myd88 (MYD88) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03725P
Availability: InStock

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MYD88.

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Product Overview

Description	Recombinant Human Myeloid Differentiation Primary Response Protein Myd88 (MYD88) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q99836
Target Symbol	MYD88
Synonyms	Mutant myeloid differentiation primary response 88; MYD 88; Myd88; MYD88_HUMAN; MYD88D; Myeloid differentiation marker 88; Myeloid differentiation primary response 88; Myeloid differentiation primary response gene (88); Myeloid differentiation primary response gene 88; Myeloid differentiation primary response gene; Myeloid differentiation primary response protein MyD88; OTTHUMP00000161718; OTTHUMP00000208595; OTTHUMP00000209058; OTTHUMP00000209059; OTTHUMP00000209060
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MAAGGPGAGSAAPVSSTSSLPLAALNMRVRRRLSLFLNVRTQVAADWTALAEEMDFEYLEIRQLETQADPTGRLLDAWQGRPGASVGRLLELLTKLGRDDVLLELGPSIEEDCQKYILKQQQEEAEKPLQVAAVDSSVPRTAELAGITTLDDPLGHMPERFDAFICYCPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELIEKRCRRMVVVVSDDYLQSKECDFQTKFALSLSPGAHQKRLIPIKYKAMKKEFPSILRFITVCDYTNPCTKSWFWTRLAKALSLP
Expression Range	1-296aa
Protein Length	Full Length
Mol. Weight	37.2 kDa
Research Area	Cardiovascular
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 protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Increases IL-8 transcription. Involved in IL-18-mediated signaling pathway. Activates IRF1 resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. Upon TLR8 activation by GU-rich single-stranded RNA (GU-rich RNA) derived from viruses such as SARS-CoV-2, SARS-CoV and HIV-1, induces IL1B release through NLRP3 inflammasome activation. MyD88-mediated signaling in intestinal epithelial cells is crucial for maintenance of gut homeostasis and controls the expression of the antimicrobial lectin REG3G in the small intestine.
Subcellular Location	Cytoplasm. Nucleus.
Database References	HGNC: 7562 OMIM: 602170 KEGG: hsa:4615 STRING: 9606.ENSP00000401399 UniGene: PMID: 29080258 A summary of recent progress on elucidating the molecular and cellular processes affected by the oncogenic L265P mutation of MYD88 (review) . PMID: 30203262 the results of the present study showed significantly higher mRNA expression levels for MYD88 180days post-transplantation in the graft dysfunction group compared to well functioning graft group PMID: 29452169 the expression levels of TLR4/MyD88 were positively correlated with the metastatic potential of breast cancer cells and tumors. The expression levels of TLR4/MyD88 may be used as a biomarker to evaluate the prognosis and guide the treatment of patients with breast cancer. PMID: 30066873 AGAP2-AS1 was upregulated and transcriptionally induced by SP1 in breast cancer..ChIP assays showed that AGAP2-AS1-bound CBP increased the enrichment of H3K27ac at the promoter region of MyD88, thus resulting in the upregulation of MyD88. Gain- and loss-of-function assays confirmed that the NF-kappaB pathway was activated by MyD88 and AGAP2-AS1 PMID: 30157918 Activates the NFkappaB pathway through the Tolllike receptor 4 (TLR4)/myeloid differentiation factor 88 (MyD88)/IkappaBalpha axis. PMID: 29916535 explored the detection method and clinical relevance of MYD88 mutations in Chinese patients with Chronic Lymphocytic Leukemia PMID: 29242635 The combination of Ligusticum chuanxiong and Radix Paeoniae protects against focal cerebral ischaemia via TLR4/MyD88/MAPK/NF-kappaB signalling pathway in rat model of middle cerebral artery stroke. PMID: 29193143 MYD88 Gene Polymorphism is not associated with Chronic Lymphocytic Leukemia. PMID: 29286214 17.6% of cases with primary CNS diffuse large B-cell lymphoma had homozygous/hemizygous MYD88 mutations, which has not been previously reported PMID: 28856744 MyD88 mutation status did not correlate with overall survival (OS), post-ASCT OS, or progression-free survival (PFS) for Diffuse Large B Cell Lymphoma Patients undergoing Autologous Stem Cell Transplantation. PMID: 28847710 Inducible activation of MyD88 and CD40 in CAR T cells with a small-molecule drug not only enhances their effector function, resulting in potent antitumor activity in preclinical solid tumors, but also enables their remote control post infusion. PMID: 28801306 loss of MyD88 is essential for retinoic acid-facilitated differentiation of human embryonal carcinoma cells. PMID: 28885616 Study supports that MYD88 status is a necessary biomarker in patients with primary cutaneous large B-cell lymphomas for diagnosis, prognosis, and management. PMID: 27189828 Among age >65 patients, the MyD88 L265P mutation portended a worse overall survival compared with the MyD88 wild type PMID: 29258950 Results show that MyD88 protein is necessary to activate autophagy in HSV-1-infected THP-1 cells. PMID: 27509841 confirmed the high prevalence of MYD88 L265P mutation in Waldenstrom macroglobulinaemia patients, as well as in smouldering Waldenstrom macroglobulinaemia; patients with asymptomatic IgM gammopathies carrying the MYD88 L265P mutation showed a trend towards a shorter time to Waldenstrom macroglobulinaemia progression PMID: 27605200 interleukin-1 receptor 1/MyD88 signalling has roles in the development and progression of pulmonary hypertension PMID: 27418552 Results from whole exome sequencing has led to the identification of the MYD88L265P somatic variants in Waldenstrom's Macroglobulinemia, occurring in about 90% of the patients. [review] PMID: 28423722 Among genotyped patients, nonresponders associated with wild-type MYD88 and mutated CXCR4 status. Median time to response was 4 weeks PMID: 27836860 The authors demonstrated that EV71 infection upregulates miR-21, which in turn suppresses EV71-triggered type I IFN production, thus promoting EV71 replication. Furthermore, they demonstrated that miR-21 targets the myeloid differentiation factor 88(MyD88) and interleukin-1 receptor-associated kinase 1(IRAK1), which are involved in EV71-induced type I IFN production. PMID: 28506791 The findings show that among suspected MYD88(WT) WM cases, an alternative clinicopathological diagnosis is common and can impact clinical care. WM patients with MYD88(WT) disease have a high incidence of associated DLBCL events and significantly shorter survival versus those with MYD88(MUT) disease. PMID: 29181840 our study shows that MYD88 L265P mutation is associated with poor prognosis and high risk of progression in PCNSL patients. PMID: 27161435 This study highlights the relative heterogeneity of MYD88-mutant diffuse large B-cell lymphoma (DLBCL), adding to the field's knowledge of the theranostic importance of MYD88 mutations, but also of associated alterations, emphasizing the usefulness of genomic profiling to best stratify patients for targeted therapy PMID: 27923841 mutated MYD88 can be used to identify malignant pleural effusions in WM patients. WM patients with a suspected malignant pleural effusion should be considered for MYD88 mutation testing as part of their workup to establish the aetiology of their pleural effusion. PMID: 27748515 MYD88 L265P mutations, but no other variants, identify a subgroup of diffuse large B-cell lymphoma mainly of activated B-cell like origin, with extranodal involvement and poor outcome. PMID: 26792260 DNA was extracted from CD138+ or CD19+CD138+ sorted cells isolated from the bone marrows of IgM amyloidosis patients. The study reports of MYD88 L265P somatic mutation in IgM-associated light-chain amyloidosis patients. PMID: 27034430 BTK-inhibitor ibrutinib and FK866 resulted in a significant and synergistic anti-Waldenstrom macroglobulinemia cell death, regardless of MYD88 and CXCR4 mutational status. PMID: 27287071 Study found evidence of alterations in the expression of the initial elements of the TLR4 signalling pathway (TLR4, MyD88 and NF-kappaB) in the PFC of patients with schizophrenia. These alterations seem to depend on the presence/absence of antipsychotic treatment at death. Moreover, a polymorphism within the MyD88 gene was significantly associated with schizophrenia risk. PMID: 27070349 The present study demonstrates that MYD-88 L265P mutation may represent the only sensitive marker for the differentiation of CBL-MZ from probable WM. PMID: 27734522 Aqueous fluid from the second patient with intraocular B-cell lymphoma demonstrated a less common mutation in the MYD88 gene associated with B-cell lymphoma. PMID: 29122821 Studies indicate that ibrutinib is active in patients with Waldenstrom macroglobulinemia (WM) and is affected by MYD88 and CXCR4 mutation status. PMID: 28294689 Moreover, anchoring of MyD88 to the cell membrane augments signaling supporting the importance of membrane localization in MyD88-mediated signaling. PMID: 29155181 MyD88 cysteine residues functionally modulate MyD88-dependent NF-kappaB activation, suggesting a link between MyD88 thiol oxidation state and immune signaling. PMID: 27720842 the expression of certain TAM components was reduced as a result of prolonged degradation of MYD88 by Porphyromonas gingivalis infection. PMID: 28076786 MYD88 expression in subcutaneous adipose tissue of obese subjects could be associated with the development of components of Metabolic syndrome. PMID: 28075222 Patients with primary breast and primary female genital tract diffuse large B cell lymphoma have a high frequency of MYD88 mutations. PMID: 28803429 Mutation in the MYD88 gene is associated with lymphoplasmacytic lymphoma and chronic lymphocytic leukemia. PMID: 27840426 the polymorphisms in TLR-MyD88-NF-kappaB signaling pathway confer genetic susceptibility to Type 2 diabetes mellitus and diabetic nephropathy. PMID: 27062898 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 data show that in pericytes, MyD88 and IRAK4 are key regulators of 2 major injury responses: inflammatory and fibrogenic. PMID: 27869651 Data indicate that 64 patients (57.1%) carried the myeloid differentiation factor 88 protein (MYD88) L265P mutation and 14 patients (12.5%) carried the chemokine (C-X-C motif) receptor 4 (CXCR4) WHIM-like mutation. PMID: 28280994 HCK represents a novel target for therapeutic development in MYD88-mutated Waldenstrom macroglobulinemia and activated-B cell diffuse large B-cell lymphoma, and possibly other diseases driven by mutated MYD88. PMID: 27143257 We found an that enhanced expression of the TLR4-MyD88-NF-kB pathway occurs in GDM placentae, which positively correlates with heightened local IR in placentae and higher maternal hyperglycemia. The TLR4/MyD88/NF-kB pathway may play a potential role in the development of IR in placentae of GDM. PMID: 27340831 We found that over-expression of CRNDE in astrocytes increased the expression of key factors in the toll-like receptor signaling pathway, especially toll-like receptor-3-mediated MyD88-independent pathway.We speculated that CRNDE might trigger inflammation to regulate tumorigenesis and tumor development through the toll-like receptor pathway PMID: 28621230 Data suggest that, in monocytes and macrophages, the interleukin-1B- (IL1B)-stimulated trans-autophosphorylation of IRAK4 (interleukin-1 receptor-associated kinase 4) is initiated by MYD88-induced dimerization of IRAK4. In contrast, IRAK1 (interleukin-1 receptor-associated kinase 1) is inactive in unstimulated monocytes/macrophages and is converted to an active protein kinase in response to IL1B. PMID: 28512203 our data suggest a new role of MyD88 in the development of glucose intolerance and hepatic steatosis. PMID: 27196572 In patient population from Southeast Serbia Myd 88 L265 mutation was not responsible for the development of diffuse large B-cell non Hodgkin lymphoma. PMID: 27837631 FSTL1 displays anti-inflammatory effects against oxidized low-density lipoprotein-induced pro-inflammatory cytokine production via a mechanism that involves the TLR4/MyD88/NF-kappaB and MAPK signaling pathways. PMID: 27569284 The incidence of MYD88 and CD79B mutations in patients with CD5(+) DLBCL is lower than that in patients with DLBCL-SS, suggesting that CD5(+) DLBCL is not the same disease as DLBCL-SS in terms of gene mutation status. PMID: 27915469

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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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