Lectin / Lectins

Sino biological offers a comprehensive set of tools for lectin related research, including recombinant proteins, antibodies, ELISA kits, and ORF cDNA clones. Lectins are a group of proteins that are capable of specific recognition of and reversible binding to carbohydrate moieties. A lectin molecule contains at least two sugar-binding sites. They may be soluble or membrane-bound proteins or glycoproteins, and are expressed in many types of organism. Lectins can be divided into several subgroups, including C-type lectin family, galectins, sialic acid binding Ig-like lectins (SIGLECs). Selectins are single-chain transmembrane glycoproteins that share similar properties to C-type lectins due to a related amino terminus and calcium-dependent binding. They bind to sugar moieties and so are considered to be a type of lectin.

Product / Species	Human	Mouse	Rat	Cynomolgus
Recombinant Proteins	22	13	1	1
Antibodies	20	13	-	-
ELISA Kit	1	-	-	-
ORF cDNA Clones	29	31	2	1

Lectin Products

C-type Lectin Family

• ASGPR1
• CLEC4N / Nkcl
• MBL-2 / MBL
• CD23 / FCER2
• CLEC10A / CD301
• CLEC12A
• CD69 / CLCE2C
• CLEC13A / CD302
• NKG2D / CD314
• CD72
• CLEC14A
• NKp80 / KLRF1
• CD93 / C1qR
• DC-SIGN / CD209
• OCIL / CLEC2d
• CHODL / Chondrolectin
• DC-SIGNR / CD299
• REG1A
• CLL1 / COLEC10
• DCIR / CLEC4A
• REG1B
• CL-K1 / COLEC11
• Dectin-1 / CLEC7A
• REG3A
• CL-P1 / COLEC12
• Dectin-2 / CLEC6A
• REG3D
• CLEC1A
• FCN1 / Ficolin 1
• REG3G
• CLEC1B
• Ficolin 3
• REG4 / RELP
• CLEC3B / Tetranectin
• Langerin / CD207
• SCGF / CLEC11a
• CLEC4D / CLECSF8
• Layilin
• SIGNR1 / CD209b
• CLEC4E
• LOX-1 / OLR1
• SIGNR7
• CLEC4F / CLECSF13
• LSECtin / CLEC4G
• SFTPD / SP-D / SFTP4
• CLEC4G
• MBL-1
• OLR1
• CLEC10A/MGL1

Galectin

• Galectin-1
• Galectin-3BP
• Galectin-8
• Galectin-3
• Galectin-4

Selectin

• E-Selectin / CD62E
• CD62L / L-Selectin

Sialic Acid Binding Ig-like Lectin (SIGLEC)

• Siglec-3 / CD33
• Siglec 5

Lectin Background

Lectins are a group of proteins that are capable of specific recognition of and reversible binding to carbohydrate moieties. A lectin molecule contains at least two sugar-binding sites. Lectins may be soluble or membrane-bound proteins or glycoproteins, and are expressed in many types of organism. Lectins were first described in 1888 by Stillmark working with castor bean extracts. Although lectins were first discovered more than 100 years ago in plants, they are now known to be present ubiquitously in nature. Lectins typically agglutinate red blood cells and precipitate glycoconjugates. They have also been demonstrated to be antigenic. In animals, lectins function in many different biological processes, including cell adhesion, glycoprotein synthesis, endocytosis, and the control of protein levels in the blood. Lectins are also known to play important roles in the immune system by recognizing carbohydrates that are found exclusively on pathogens, or that are inaccessible on host cells. Examples are the lectin complement activation pathway and mannose binding lectin.

Lectins can be divided into several subgroups, including C-type lectin family, galectins, sialic acid binding Ig-like lectins (SIGLECs). Selectins are single-chain transmembrane glycoproteins that share similar properties to C-type lectins due to a related amino terminus and calcium-dependent binding. They bind to sugar moieties and so are considered to be a type of lectin.

Lectin Related Studies

1. Pyz E, et al. (2006) C-type lectin-like receptors on myeloid cells. Ann Med. 38(4):242-51.
2. van Vliet SJ (2008) Dendritic cells and C-type lectin receptors: coupling innate to adaptive immune responses. Immunol Cell Biol. 86(7):580-7.
3. Rhodes JM, et al. (2008) Lectin-epithelial interactions in the human colon. Biochem Soc Trans. 36(Pt 6):1482-6.
4. Ip WK, et al. (2009) Mannose-binding lectin and innate immunity. Immunol Rev. 230(1):9-21.