Recombinant Human CLEC-2/CLEC1B Protein, CF Summary
Gln58-Pro229, with an N-terminal 10-His tag
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 250 μg/mL in sterile PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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).
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- Christou, C.M. et al. (2008) Biochem. J. 411:133.
- Watson, A.A. et al. (2007) J. Biol. Chem. 282:3165.
- Suzuki-Inoue, K. et al. (2006) Blood 107:542.
- Fuller, G.L. et al. (2007) J. Biol. Chem. 282:12397.
- Weis, W.I. et al. (1998) Immunol. Rev. 163:19.
- Suzuki-Inoue, K. et al. (2007) J. Biol. Chem. 282:25993.
- Chaipan, C. et al. (2006) J. Virol. 80:8951.
Citations for Recombinant Human CLEC-2/CLEC1B Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 3
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Podoplanin regulates the migration of mesenchymal stromal cells and their interaction with platelets
Authors: LSC Ward, L Sheriff, JL Marshall, JE Manning, A Brill, GB Nash, HM McGettrick
J. Cell. Sci., 2019;0(0):.
Sample Types: Whole Cells
Origin-Specific Adhesive Interactions of Mesenchymal Stem Cells with Platelets Influence Their Behavior After Infusion
Authors: L Sheriff, A Alanazi, LSC Ward, C Ward, H Munir, J Rayes, M Alassiri, SP Watson, PN Newsome, GE Rainger, N Kalia, J Frampton, HM McGettrick, GB Nash
Stem Cells, 2018;0(0):.
Sample Types: Whole Cells
Inhibitory effects of polypeptides derived from a snake venom C-type lectin, aggretin, on tumor cell-induced platelet aggregation.
Authors: Chang C, Chung C, Hsu C, Peng H, Huang T
J Thromb Haemost, 2014;12(4):540-9.
Sample Types: Protein
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