Recombinant Mouse MD2 Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-3319

Recombinant Mouse MD2 Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-3319
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Product Overview

Tag Fc
Host Species Mouse
Accession Q9JHF9
Synonym ESOP-1, MD-2, MD2
Background LY-96, also known as ESOP-1, is a protein which associates with toll-like receptor 4 on the cell surface and confers responsiveness to lipopolysaccyaride (LPS). LY-96 also cooperates with TLR2 in the response to cell wall components from Gram-positive and Gram-negative bacteria. It enhances TLR4-dependent activation of NF-kappa-B. ESOP-1 has 16 amino acids, the sequence of which shows 64% identity with human ESOP-1/MD-2. ESOP-1 mRNA is highly expressed in the mouse embryos at 7.5 days after coitus.
Description A DNA sequence encoding the mouse LY96 (Q9JHF9) (Met1-Asn160) was expressed with the Fc region of human IgG1 at the C-terminus.
Source HEK293
Predicted N Terminal Glu 19
AA Sequence Met1-Asn160
Molecular Weight The recombinant mouse LY96/Fc is a disulfide-linked homodimer. The reduced monomer comprises 383 a.a. and has a predicted molecular mass of 43.4 kDa. The apparent molecular mass of the protein is approximately 47 kDa in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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
Tissue Specificity Highly expressed in spleen, bone marrow, thymus, liver, kidney, ovary and decidua. Detected at lower levels in testis, small intestine and skin.

Gene Functions References

  1. We conclude that MD2 is a significant contributor in the Ang II-induced kidney inflammatory injury in chronic renal diseases. PMID: 28322341
  2. Blockade of MD2 prevents obesity-induced inflammation and nephropathy. PMID: 28767204
  3. MD2 is essential to obesity-related cardiac hypertrophy through activating JNK/ERK and NF-kappaB-dependent cardiac inflammatory pathways. Targeting MD2 would be a therapeutic approach to prevent obesity-induced cardiac injury and remodeling. PMID: 28965884
  4. RTFs contribute to the regulation of LPS-induced inflammatory response in RAW264.7 cells through TLR4/MD-2 mediated NF-kappaB and JNK pathway. It PMID: 27235587
  5. This study provides evidence that MD2 plays a key role in the pathogenesis of retinal I/R damage. PMID: 29111459
  6. Data suggest that C4bp prevents interaction between Tlr4/MD-2 and its ligand; C4bp does not appear to interact with Tlr3; C4bp binds to macrophage surface Tlr4 and inhibits Tlr/Tlr ligand interaction, thereby inhibiting Tlr4 activation. (C4bp = complement component 4 binding protein; Tlr = toll-like receptor; MD-2 = myeloid differentiation protein-2) PMID: 28542817
  7. MD2 plays an important role in induction of allergic sensitization to cat dander and common pollens relevant to human allergic diseases. PMID: 26586036
  8. Oxidative stress in retinal ischemia-reperfusion injury activates TLR4 signaling via MD2. PMID: 28063877
  9. Neoseptin-3 and lipid A form dissimilar molecular contacts to achieve receptor activation; hence strong TLR4/MD-2 agonists need not mimic LPS PMID: 26831104
  10. Here we demonstrate that cholesterol binds to myeloid differentiation-2 (MD-2), a TLR4 ancillary molecule. PMID: 26806306
  11. MD-2 is a critical regulator of the establishment of allergic airway sensitization to HDM in mice. Serum MD-2 may represent a potential biomarker for the amplification of allergic sensitization and allergic inflammation. PMID: 26344079
  12. Data show that myeloid differentiation factor 2 (MD-2) binds specifically to disulfide isoform of box protein 1, high mobility group (HMGB1) to facilitate toll-like receptor 4 (TLR4)-dependent signaling. PMID: 25559892
  13. Carbon monoxide treatment reduces the expression of the TLR4/MD2 complex on the surface of myeloid cells, which renders them resistant to lipopolysaccharide priming in vitro, as well as in vivo in a model of endotoxic shock. PMID: 25179131
  14. 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
  15. SAA3 directly binds MD-2 and activates the MyD88-dependent TLR4/MD-2 pathway. PMID: 23858030
  16. Monophosphoryl lipid A is unable to efficiently form TLR4/MD-2 heterotetramers, but it still needs heterotetramer formation for the full extent of signaling it is able to achieve. PMID: 23638128
  17. Data show that rifampin binds to myeloid differentiation protein 2 (MD-2), the key coreceptor for innate immune TLR4. PMID: 23568774
  18. Gb4 is an endogenous ligand for TLR4-MD-2 and is capable of attenuating LPS toxicity, indicating the possibility for its therapeutic application in endotoxin shock. PMID: 23471986
  19. Data provide structural evidence of the agonistic property of lipid IVa on TLR4/MD-2 and deepen understanding of the ligand binding and dimerization mechanism by the structurally diverse Lipopolysaccharide (LPS) variants. PMID: 22532668
  20. GL and ILG modulate the TLR4/MD-2 complex at the receptor level, leading to suppress LPS-induced activation of signaling cascades and cytokine production PMID: 22422925
  21. Data show that morphine binds to an accessory protein of Toll-like receptor 4 (TLR4), myeloid differentiation protein 2 (MD-2), thereby inducing TLR4 oligomerization and triggering proinflammation. PMID: 22474354
  22. Data show that LPS priming of tolerant FLDCs inhibited the up-regulation of TLR4/MD-2 expression. PMID: 21802073
  23. According to our murine TLR4/MD-2-activation model, the two phosphates on lipid A were predicted to interact extensively with the two positively charged patches on mouse TLR4activation PMID: 21865549
  24. Demonstrate a novel, critical role for MD-2 and TLR4 through NADPH activation in liver steatosis, and fibrosis in a NASH model in mice. PMID: 21233280
  25. species-specific activation of lipid IV(A) PMID: 20592019
  26. Neutralizing toll-like receptor 4/myeloid differentiation protein-2 is highly efficacious in protecting against bacterial infection-induced toxemia. PMID: 17947685
  27. MD-2-mediated ionic interactions between lipid A and TLR4 are essential for receptor activation PMID: 20018893
  28. MD-2 in complex with toll-like receptor 4 mediates signal transduction induced by the amino acid-containing bacterial lipid, flavolipin. PMID: 11884465
  29. MD-2 is essential for correct intracellular distribution and LPS-recognition of TLR4. PMID: 12055629
  30. By alanine-scanning mutagenesis of MD-2, important amino acid residues have been identified that confer lipopolysaccharide and taxol responsiveness on TLR4 and enable formation of cell surface TLR4-MD-2 complex recognized by specific monoclonal antibody. PMID: 12496426
  31. TLR4 and its partner molecule MD-2 may play an important role in Kupffer cell activation and ischemia-reperfusion injury. PMID: 15334694
  32. Results show that the N-terminal region of toll-like receptor 4 is essential for association with MD-2, which is required for the cell surface expression and hence the responsiveness to lipopolysaccharide. PMID: 15337750
  33. Collectively, MD-2 is essential for the recognition of LPS by TLR4 but not for that of PGN by TLR2 of mast cells. PMID: 15369778
  34. Results indicate that amino acid residues 57, 61, and 122 of mouse MD-2 are critical to determine the agonist-antagonist activity of lipid IVa and suggest that these amino acid residues may be involved in the discrimination of lipid A structure. PMID: 16407172
  35. agonistic mAb to Toll-Like Receptor 4 (TLR4)/MD-2 protected mice from lipopolysaccharide/d-galactosamine-induced acute lethal hepatitis by delivering a protective signal activating NF-kappaB through TLR4/MD-2 PMID: 16547261
  36. This study shows regulatory roles for MD-2 in initiating and terminating ligand-induced TLR4 oligomerization. PMID: 16670331
  37. a unique complex of TLR4, MD-2, and CD44 recognizes hyaluronan in signaling tissue injury PMID: 17400552
  38. Data show that lipopolysaccharides act through both MyD88-dependent and -independent TLR4/MD2 signaling pathways to directly inhibit GHR gene expression. PMID: 17601656
  39. Based on structural analysis and mutagenesis experiments on MD-2 and TLR4, we propose a model of TLR4-MD-2 dimerization induced by LPS. PMID: 17803912
  40. The lower expression of the CD14 and TLR-4/MD-2 receptors may be partly responsible for the immunodeficiency observed in the malnourished mice. PMID: 17950615
  41. MD-2 is a newly recognized type II acute-phase reactant, an opsonin for Gram-negative bacteria, and a cofactor essential for the activation of TLR4-expressing cells. PMID: 18056837
  42. role of the TLR4/MD-2 signaling axis in bacterial recognition by phagocytes PMID: 18203953
  43. Data compare the inflammatory potency of two types of Neisseria meningitidis endotoxins in lungs: wild type (hexaacylated, LOS(wt)) and mutant type (pentaacylated, LOS(msbB)), and describe the importance of MD-2 in endotoxin responses in lungs in vivo. PMID: 18203970
  44. The species-specific difference between human and murine MD-2 activation of TLR4 by PTX can be explained by alterations of surface charge distribution (i.e. electrostatic potential), binding pocket size, and the locus of PTX binding within the MD-2 pocket PMID: 18650420
  45. Myeloid differentiation protein-2 has an important role in the CD14-independent LPS-mediated cascade of neutrophil influx PMID: 18988922
  46. the leucine at position 815 is required for the normal maturation of TLR4 and for formation of the TLR4.MD-2 complex. PMID: 19064998
  47. These findings reveal novel roles of lysines 122, 125, and 58 in human MD-2 that contribute to the functional differences between human and murine MD-2 and, potentially, to differences in the sensitivity of humans and mice to endotoxin. PMID: 19783674


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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.

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