Detection of Human CLEC-2/CLEC1B by Western Blot. Western blot shows lysates of human platelets. PVDF Membrane was probed with 2 µg/mL of Mouse Anti-Human CLEC-2/CLEC1B Monoclonal Antibody (Catalog # MAB1718) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for CLEC-2/CLEC1B at approximately 35 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 5.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
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. 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).
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Suzuki-Inoue, K. et al. (2007) J. Biol. Chem. 282:25993.
Chaipan, C. et al. (2006) J. Virol. 80:8951.
C-type Lectin-like Receptor 2
Entrez Gene IDs:
51266 (Human); 56760 (Mouse)
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
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