Recombinant Human CLEC-2/CLEC1B Fc Chimera Protein, CF

When Recombinant Human CLEC-2/CLEC1B Fc Chimera (Catalog # 11211-CL) is immobilized at 1 µg/mL (100 µL/well), Biotinylated Recombinant Human Podoplanin Fc Chimera binds with an ED50 of 6.00-60.0 pg/mL.

2 μg/lane of Recombinant Human CLEC-2/CLEC1B Fc Chimera Protein (Catalog # 11211-CL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 56-65 kDa and 110-130 kDa, respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human CLEC-2/CLEC1B Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human CLEC-2/CLEC1B Fc Chimera (Catalog # 11211-CL) is immobilized at 1 µg/mL (100 µL/well), Biotinylated Recombinant Human Podoplanin Fc Chimera binds with an ED₅₀ of 6.00-60.0 pg/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human CLEC-2/CLEC1B protein
  

  MD	Human IgG1 (Pro100-Lys330)	IEGR	Human CLEC1B (Gln58-Pro229) Accession # Q9P126.2
  N-terminus			C-terminus

• Accession #: Q9P126.2
• N-terminal Sequence: Met1 of Fc Chimera
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 47 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.
• SDS-PAGE: 56-65 kDa, under reducing conditions.

Packaging, Storage & Formulations

• 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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human CLEC-2/CLEC1B Fc Chimera Protein, CF

• 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

Background

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).

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.

Bioinformatics

• Uniprot:
  • Q9P126.2()