Recombinant Human Lymphocyte Antigen 96 (LY96) Protein (His-GST&Myc)

Name: Recombinant Human Lymphocyte Antigen 96 (LY96) Protein (His-GST&Myc)
Brand: Beta LifeScience
SKU: BLC-03804P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Lymphocyte Antigen 96 (LY96) Protein (His-GST&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9Y6Y9
Target Symbol	LY96
Synonyms	ESOP 1; ESOP-1; ESOP1 ; LY 96; Ly-96; LY96; LY96_HUMAN; Lymphocyte antigen 96; md 2; MD 2 protein; MD2 protein; Myeloid differentiation protein 2 ; Protein MD 2; Protein MD-2; Protein MD2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His-GST&C-Myc
Target Protein Sequence	EAQKQYWVCNSSDASISYTYCDKMQYPISINVNPCIELKRSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGSDDDYSFCRALKGETVNTTISFSFKGIKFSKGKYKCVVEAISGSPEEMLFCLEFVILHQPNSN
Expression Range	17-160aa
Protein Length	Partial
Mol. Weight	46.7kDa
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	Binds bacterial lipopolysaccharide (LPS). Cooperates with TLR4 in the innate immune response to bacterial lipopolysaccharide (LPS), and with TLR2 in the response to cell wall components from Gram-positive and Gram-negative bacteria. Enhances TLR4-dependent activation of NF-kappa-B. Cells expressing both LY96 and TLR4, but not TLR4 alone, respond to LPS.
Subcellular Location	Secreted, extracellular space. Secreted.
Database References	HGNC: 17156 OMIM: 605243 KEGG: hsa:23643 STRING: 9606.ENSP00000284818 UniGene: PMID: 29036538 MD-2 siRNA or plasmid further confirmed the efficacy of Iturin A by suppressing MD-2/TLR4 signaling pathway. The in silico docking study showed that the Iturin A interacted well with the MD-2 in MD-2/TLR4 receptor complex. Conclusively, inhibition of MD-2/TLR4 complex with Iturin A offered strategic advancement in cancer therapy. PMID: 28347875 data confirm that engineered human cells expressing TLR4, MD2 and CD14 can respond to CMP with NF-kappaB activation and the response can be influenced by variations in CMP-mannosylation PMID: 29281684 The observations suggest that MD-2 helps to regulate lipopolysaccharide-induced NLRP3 inflammasome activation and the inflammatory response in NR8383 cells, and likely does so by affecting MyD88/NF-kappaB signaling. PMID: 28654770 MD2 plays an important role in induction of allergic sensitization to cat dander and common pollens relevant to human allergic diseases. PMID: 26586036 we report that exogenous CnB is taken up by cells in a time- and concentration-dependent manner via clathrin-dependent receptor-mediated internalization. Our findings further confirm that uptake is mediated by the TLR4/MD2 complex together with the co-receptor CD14 PMID: 27090571 In this study, a novel naturally occurring spliceosome of human MD2, termed as MD2-T3, has been identified. PMID: 27317890 Results show that cigarette smoke may alter innate immune responses reducing the expression of the MD2, a molecule with an important role in TLR4 signaling. PMID: 26068048 Predominantly hydrophobic interactions between MD-2 and TLR4 contribute to the stabilization of the TLR4/MD-2/metal ion complex in a conformation that enables activation. PMID: 25803856 The intensity of the intra-amniotic inflammatory response to bacteria or perhaps to other TLR4 ligands may be facilitated through synthesis and release of sMD2 by the amniochorion. PMID: 25605324 Three genes (LY96, IL8 DPR) were significantly downregulated over time. This finding was confirmed in a validation cohort of stroke patients (n=8). PMID: 25124890 The study revealed the impact of specific residues and regions of MD-2 on the binding of lipolysaccharides and TLR4. PMID: 26320630 Gene polymorphisms of MD2 and GM2A were associated with the occurrence or severity of neonatal necrotizing enterocolitis. PMID: 25816011 In patients undergoing CABG surgery, we found genetic polymorphisms in LY96 associated with decreased risk of postoperative AF. PMID: 26385043 Aminoarabinose residues in lipid A contribute to Burkholderia lipid A binding to the TLR4.Myeloid Differentiation Factor 2 complex. PMID: 26160169 TLR4 along with its accessory protein MD-2 builds a heterodimeric complex that specifically recognizes lipopolysaccharides, which are present on the cell wall of gram-negative bacteria, activating the immune response. (Review) PMID: 25515751 genetic polymorphism is associated with asthma exacerbations in children PMID: 24902762 In monocytes of sepsis, MD-2 expression was found to be regulated by STAT1. PMID: 24858600 Substitution of hMD-2 residue V82 with an amino acid residue with a bulkier hydrophobic side chain enables activation of TLR4/MD-2. PMID: 25203747 This study suggests that genetic variants of LY96 may modulate the effect of smoking on carotid plaque burden. PMID: 24954085 overexpression of MD-2s led to marked reduction in markers of tissue injury and inflammation in models of lung inflammation PMID: 25576596 Purified monomeric ligand.MD-2 complexes reveal molecular and structural requirements for activation and antagonism of TLR4 by Gram-negative bacterial endotoxins. PMID: 24895101 Studies suggest that myeloid differentiation 2 (MD-2) as a therapeutic target for sepsis. PMID: 24896325 Mechanistically, engagement of MD-2 by PTX3-opsonized Aspergillus conidia activated the TLR4/Toll/IL-1R domain-containing adapter inducing IFN-beta-dependent signaling pathway converging on IL-10. PMID: 25049357 Collectively, these data showed for the first time that, HIV-1 Tat interacts physically with high affinity with TLR4-MD2 to promote proinflammatory cytokines (TNF-alpha) and the immunosuppressive cytokine IL-10 both. PMID: 24165011 Data suggest that zhankuic acid A (ZAA), which competes with LPS for binding to MD-2 as a TLR4/MD-2 antagonist, may be a potential therapeutic agent for gram-negative bacterial infections. PMID: 24532584 these findings indicate that MD-2 is involved in IFN-gamma signalling and IFN-gamma-augmented MMP-1 up-regulation by LPS. PMID: 23800176 Extracellular complex formation of TLR4 with secreted MD-2 was detectable using monoclonal antibodies. PMID: 24021278 both oral and enteric C. concisus strains upregulated expression of TLR4 and MD-2 in HT-29 cells. PMID: 23437263 Consistently, soluble TLR4 expressed without MD2 inhibited metal- but not LPS-induced responses, opening new therapeutic perspe PMID: 23059983 Respiratory syncytial virus F protein requires MD-2 for the induction of the TLR4-mediated inflammatory response. PMID: 22872782 In LOS.MD-2 complexes, one of the six fatty acyl chains of LOS is more susceptible to paramagnetic attenuation, suggesting protrusion of that fatty acyl chain from the hydrophobic pocket of MD-2, independent of association with TLR4. PMID: 22433852 Lipopolysaccharide cytokine response was efficiently and equally abolished by MD-2 and CD14 neutralization; the response induced by whole E. coli bacteria was only modestly reduced by MD-2 neutralization, whereas CD14 neutralization was more efficient. PMID: 21948372 have identified specific structural and dynamic features of the MD-2-endotoxin complexes that may control dimerization of TLR4 molecules. PMID: 21924775 The association between occupational endotoxin exposure and wheeze in agricultural workers was significantly modified by genetic variants in CD14 and MD2 PMID: 21389010 Data demonstrate that during bacterial infection, newborns amplify the TLR2-MyD88 pathway in G+ bacterial infection and the TLR4/MD2/MyD88 pathway in G- bacterial infection, implicating the innate immune pathway in response to bacterial infection. PMID: 20805788 higher expression levels in tissue from patients with colorectal cancer PMID: 20699280 Computational study of the interactions of the unmodified dendrimer, glucosamine, and of the partially glycosylated dendrimer with TLR4 and MD-2 using molecular docking and molecular dynamics techniques. PMID: 21738462 tyrosine phosphorylation of MD-2 is important for signaling following exposure to lipopolysaccharide PMID: 21918188 Cytokines can enhance TLR4 and MD-2 expressions and promote the reaction with LPS in intestinal epithelial cells. PMID: 20848773 Interferon-gamma-induced MD-2 protein expression and lipopolysaccharide (LPS) responsiveness in corneal epithelial cells is mediated by Janus tyrosine kinase-2 activation and direct binding of STAT1 protein to the MD-2 promoter. PMID: 21572044 In this study, we produced variants of MD-1 and MD-2 in Pichia pastoris. PMID: 21130168 Innate immune recognition of meningococcal capsular polysaccharides by macrophages can occur via TLR2- and TLR4-MD-2 pathways. PMID: 21191086 Neisserial lipooligosaccharides from different meningococcal and gonococcal strains have different potencies to activate NF-kappaappaB through the Toll-like receptor 4-MD-2 pathway in monocytes. PMID: 21037101 Data conclude that these gene variants in the MD-2 gene promoter region are not associated with tuberculosis, and apparently do not play a role in susceptibility to tuberculosis in the Chinese population. PMID: 20730709 species-specific activation of lipid IV(A) PMID: 20592019 increased expression in intestinal epithelial cells in patients with inflammatory bowel disease PMID: 19710105 In this study, we have identified a novel alternatively spliced isoform of human MD-2, termed MD-2 short (MD-2s), which lacks the region encoded by exon 2 of the MD-2 gene. PMID: 20435923 Polymorphisms of the promoter region of MD-2 gene at position - 1625 C/G is correlated with MODS and sepsis after severe trauma in Chinese Han population. PMID: 19209789 sMD-2 and sCD14 inhibit the growth of both Gram-positive and Gram-negative bacteria. PMID: 20377740

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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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