• Purity

  >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its binding ability in a functional ELISA. Immobilized Recombinant Human Podoplanin Fc Chimera (Catalog # ) can bind Recombinant Human CLEC-2/CLEC1B with an estimated K    _d <4 nM.  

• Source

  Mouse myeloma cell line, NS0-derived Gln58-Pro229, with an N-terminal 10-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  His

• Predicted Molecular Mass

  21.8 kDa

• SDS-PAGE

  29-36 kDa, under reducing conditions

Background: CLEC-2/CLEC1B

C-type lectin-like receptor 2 (CLEC-2) is a 32 kDa, type II transmembrane glycoprotein and member of the C-type lectin-like family of receptors (1-4). CLEC-2 consists of a 33 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane region, and a 175 aa extracellular domain (SwissProt # Q9P126). The cytoplasmic domain contains multiple threonine and serine residues which are sites of potential phosphorylation, and a YXXL (Tyr-Xaa-Xaa-Leu) motif through which CLEC-2 does its signaling (2, 4-5). Ligand binding and cross-linking of CLEC-2 induces Src kinase-dependent tyrosine phosphorylation of the YXXL sequence, inducing activation of the tyrosine kinase Syk and initiation of a signaling pathway that culminates in activation of phospholipase C gamma 2 (2, 5). The extracellular domain contains three potential sites of N-linked glycosylation, and a single carbohydrate recognition domain (CRD) which shows conservation of six cysteine residues (1, 6). Unlike most other members of the C-type lectin-like family of receptors, CLEC-2's CRD lacks the amino acid residues that are crucial for Ca2  ⁺-dependent carbohydrate binding, making it a non-classical C-type lectin receptor (1, 6). A splicing variant at aa 22-55 produces two isoforms for CLEC-2. Isoform 1 is the longer protein, and in isoform 2, an alanine residue is substituted for aa 22-55. Human CLEC-2 shares 63% aa sequence identity with mouse CLEC-2. CLEC-2 is expressed preferentially in liver, and is also detected in myeloid cells (monocytes, dendritic cells, and granulocytes) (1), platelets, and megakaryocytes (4). CLEC-2 is the receptor for the platelet-aggregating snake venom protein rhodocytin (3 - 4) and the molecule podoplanin, a transmembrane sialoglycoprotein that, when bound to CLEC-2, is involved in platelet aggregation, tumor metastasis, and lymphatic vessel formation (2, 7). CLEC-2 has also been shown to enhance infectivity of HIV-1 by mediating HIV-1 attachment and transfer by CLEC-2 transfected cells and platelets (8).

• References:

1. Colonna, M. et al. (2000) Eur. J. Immunol. 30:697.

2. Christou, C.M. et al. (2008) Biochem. J. 411:133.

3. Watson, A.A. et al. (2007) J. Biol. Chem. 282:3165.

4. Suzuki-Inoue, K. et al. (2006) Blood 107:542.

5. Fuller, G.L. et al. (2007) J. Biol. Chem. 282:12397.

6. Weis, W.I. et al. (1998) Immunol. Rev. 163:19.

7. Suzuki-Inoue, K. et al. (2007) J. Biol. Chem. 282:25993.

8. Chaipan, C. et al. (2006) J. Virol. 80:8951.

• Long Name:

  C-type Lectin-like Receptor 2

• Entrez Gene IDs:

  51266 (Human); 56760 (Mouse)

• Alternate Names:

  1810061I13Rik; CLEC1B; CLEC2; CLEC-2; CLEC2B; CLEC2PRO1384; C-type lectin domain family 1 member B; C-type lectin domain family 1, member B; C-type lectin-like receptor 2; C-type lectin-like receptor-2; QDED721