Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | Q9Y6Y9 |
express system | E.coli |
product tag | C-His |
purity | > 95% as determined by Tris-Bis PAGE |
background | MD2, a 160-residue accessory glycoprotein, is responsible for the recognition and binding of Gram-negative bacterial membrane component, lipopolysaccharide (LPS).Internalization of pathogen inside the mononuclear phagocytes has also been attributed to MD2 which leads to the clearance of pathogens from the host. |
molecular weight | The protein has a predicted MW of 18.07 kDa same as Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human MD2 Protein 2610
$1,050.00
Summary
- Expression: E.coli
- Pure: Yes (SDS-PAGE)
- Amino Acid Range: Gln19-Asn160
Human MD2 Protein 2610
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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MD2, a 160-residue accessory glycoprotein, is responsible for the recognition and binding of Gram-negative bacterial membrane component, lipopolysaccharide (LPS).Internalization of pathogen inside the mononuclear phagocytes has also been attributed to MD2 which leads to the clearance of pathogens from the host. |
Protein names Lymphocyte antigen 96 (Ly-96) (ESOP-1) (Protein MD-2) |
Gene names LY96,LY96 ESOP1 MD2 |
Mass 9606Da |
Function Binds bacterial lipopolysaccharide (LPS) (PubMed:17569869, PubMed:17803912). 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 (PubMed:11160242, PubMed:11593030). Enhances TLR4-dependent activation of NF-kappa-B (PubMed:10359581). Cells expressing both LY96 and TLR4, but not TLR4 alone, respond to LPS (PubMed:10359581). |
Catalytic activity #N/A |
Subellular location Secreted, extracellular space. Secreted. Note=Retained in the extracellular space at the cell surface by interaction with TLR4 (PubMed:10359581). |
Structure Heterogeneous homomer formed from homodimers; disulfide-linked (PubMed:11593030, PubMed:12642668). Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4 (PubMed:11274165). Binds to the extracellular domains of TLR2 and TLR4 (PubMed:10359581, PubMed:11593030, PubMed:17803912). Ligand binding induces interaction with TLR4 and oligomerization of the complex. |
Post-translational modification N-glycosylated; high-mannose. |
Target Relevance information above includes information from UniProt accession: Q9Y6Y9 |
The UniProt Consortium |
Publications
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