SIGLEC5 Protein

07.09.2012

Produkt-Information von SIGLEC5 Protein

Synonym	SIGLEC5, CD33L2, OBBP
Protein Construction	A DNA sequence encoding the human SIGLEC5 (O15389) (Met1-Thr 434) was expressed, fused with the Fc region of human IgG1 at the C-terminus.
Source	Human
Expression Host	Human Cells

QC Testing von SIGLEC5 Protein

Purity	>90 % as determined by SDS-PAGE	SDS-PAGE: SIGLEC5 protein
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Stability	Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal	Glu 17
Molecular Mass	The recombinant human SIGLEC5 /Fc is a disulfide-linked homodimer. The reduced monomer comprises 659 amino acids and has a predicted molecular mass of 73.4 kDa. The apparent molecular mass of the protein is approximately 74-93 kDa in SDS-PAGE under reducing conditions.
Formulation	Lyophilized from a 0.2μm filtered solution of PBS, pH7.4. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.

Usage Guide von SIGLEC5 Protein

Storage	Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution	A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

Beschreibung von SIGLEC5 Protein

SIGLEC5 is a member of the immunoglobulin superfamily and SIGLEC (sialic acid binding Ig-like lectin) family. It contains 2 Ig-like C2-type (immunoglobulin-like) domains and 1 Ig-like V-type (immunoglobulin-like) domain. SIGLEC5 also contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. It is highly expressed in peripheral blood leukocytes, spleen, bone marrow and at lower levels in lymph node, lung, appendix, placenta, pancreas and thymus. As a putative adhesion molecule, SIGLEC5 mediates sialic-acid dependent binding to cells. It binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.

References

Angata T. et al., 2006, FASEB J. 20 (12): 1964-73.
Avril T. et al., 2005, J Biol Chem. 280 (20): 19843-51.
Erickson-Miller CL. et al., 2003, Exp Hematol. 31 (5): 382-8.

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