Description
Recombinant Human Semaphorin 4D/SEMA4D Protein (His Tag)(Active) | PKSH030994 | Gentaur US, UK & Europe Disrtribition
Synonyms: Semaphorin-4D; A8;BB18; GR3; CD100;C9orf164;CD100;coll-4;M-sema-G;SEMAJ
Active Protein: Active protein
Activity: A DNA sequence encoding the human SEMA4D isoform 1 (Q92854-1) extracellular domain (Met 1-Arg 734) was expressed, with a polyhistidine tag at the C-terminus.
Protein Construction: A DNA sequence encoding the human SEMA4D isoform 1 (Q92854-1) extracellular domain (Met 1-Arg 734) was expressed, with a polyhistidine tag at the C-terminus.
Fusion Tag: C-His
Species: Human
Expressed Host: HEK293 Cells
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 92 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg of the protein as determined by the LAL method.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 80.7 kDa
Formulation: Lyophilized from sterile PBS, pH 7.4
Reconstitution: Please refer to the printed manual for detailed information.
Background: SIGLEC5 contains 2 Ig-like C2-type (immunoglobulin-like) domains and 1 Ig-like V-type (immunoglobulin-like) domain. It belongs to the immunoglobulin superfamily and SIGLEC (sialic acid binding Ig-like lectin) family. SIGLEC5 is expressed by monocytic/myeloid lineage cells. It is found at high levels in peripheral blood leukocytes, spleen, bone marrow and at lower levels in lymph node, lung, appendix, placenta, pancreas and thymus. It is also expressed by monocytes and neutrophils but absent from leukemic cell lines representing early stages of myelomonocytic differentiation. SIGLEC5 is a putative adhesion molecule that 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.
Research Area: N/A
