Recombinant Human MD-1 Protein


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Product Details

Reactivity HuSpecies Glossary
Applications Binding Activity

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Recombinant Human MD-1 Protein Summary

Details of Functionality
Measured by its ability to bind rmRP105/Fc Chimera in a functional ELISA.
Mouse myeloma cell line, NS0-derived human MD-1 protein
Human MD-1
(Gly21 - Ser162)
Accession # O95711
N-terminus C-terminus
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.


Theoretical MW
18.2 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
28 kDa, reducing conditions

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 10 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human MD-1 Protein

  • LY86
  • Ly-86
  • lymphocyte antigen 86
  • MD1
  • MD-1
  • MMD-1
  • Protein MD-1
  • RP105-associated


MD-1 is a secreted glycoprotein that was originally identified as a v-myb-regulated gene from avian myeloleukemia virus-transformed chicken myeloblasts. MD-1 homologues were subsequently cloned from human and mouse. MD-1 was found to be a molecule that is associated with RP105, a type I transmembrane glycoprotein with extracellular leucine-rich repeats (LRR) typically found in Toll-like receptor (TLR) family members. However, RP105 has a short cytoplasmic tail and lacks the Toll-IL-1 R (TIR) domain that defines the IL-1 R/TLR superfamily (1 - 3). RP105 plays an important role in B-cell activation by bacterial lipopolysaccharide (LPS). It is expressed primarily on mature B cells, dendritic cells and macrophages (3).

Human MD-1 cDNA encodes a 162 amino acid (aa) residue precursor protein with a putative 19 aa signal peptide and two potential N-linked glycosylation sites. It shares 38% and 66% amino acid sequence identity with chicken and mouse MD-1 respectively (1, 2). MD-1 is mainly expressed in spleen, and also detectable in liver, brain, thymus, and kidney. MD-1 is required for efficient RP105 cell surface expression and function (1 - 4). Cell surface RP105/MD-1 complex, in conjunction with TLR4, mediates the innate immune response to LPS in B cells. Activation of the RP105 complex has been shown to protect against apoptosis, induce B-cell proliferation and upregulate B7.2, a co-stimulatory molecule (4, 5). Since MD-1 is also expressed in liver and brain where RP105 is absent, it has been speculated that MD-1 can also be associated with other LRR-containing molecules, or have additional functions outside the immune system (5).

  1. Miyake, K. et al. (1998) J. Immun. 161:1348.
  2. Miura, Y. et al. (1998) Blood 92:2815.
  3. Miyake, K. et al. (1995) J. Immunol. 154:3333.
  4. Nagai, Y. et al. (2002) Blood 99:1699.
  5. Ogata, H. et al. (2000) J. Exp. Med. 192:23.

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Gene Symbol LY86