Recombinant Pig Sialoadhesin(SIGLEC1),partial CSB-EP021293PI
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
pSn;Sialic acid-binding Ig-like lectin 1;Siglec-1;p210
Species: (Organism)
Sus scrofa (Pig)
Gene Names:
SIGLEC1
Tag info:
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Target Protein AA Sequence:
SWTVSRPETVQGIKGSCLIIPCTFGFPANVEVPHGITAIWYYDYSGKRLVVSHSRNPKVVENHFQGRALLLGQAEQRTCSLLLKDLQPQDSGSYNFRFEISEGNRWSDVKGTVVTVTEVPSVPTIALPAKLHEG
Expression Region:
20-153aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Partial
Pathway:
Mol. Weight:
22.3 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Immunology
Function:
Involvement in disease:
Relevance:
Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells. Preferentially binds to alpha-2,3-linked sialic acid. Binds to SPN/CD43 on T-cells. May play a role in hemopoiesis (By similarity). Acts as an endocytic receptor mediating clathrin dependent endocytosis. In case of porcine reproductive and respiratory syndrome virus (PRRSV), mediates virion attachment and internalization into alveolar macrophages through a clathrin-coated dependent process.
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Reference:
"Porcine arterivirus attachment to the macrophage-specific receptor sialoadhesin is dependent on the sialic acid-binding activity of the N-terminal immunoglobulin domain of sialoadhesin." Delputte P.L., Van Breedam W., Delrue I., Oetke C., Crocker P.R., Nauwynck H.J. J. Virol. 81:9546-9550(2007)
