Item no. |
SI0-H5255-1mg |
Manufacturer |
ACROBiosystems
|
Amount |
1 mg |
Category |
|
Type |
Proteins |
Format |
Powder |
Specific against |
Human |
Host |
HEK293 |
Conjugate/Tag |
Unconjugated, Fc |
Purity |
85% |
ECLASS 10.1 |
32160409 |
ECLASS 11.0 |
32160409 |
UNSPSC |
12352202 |
Alias |
SIGLEC10,MGC126774,PRO940,Siglec10,SLG2 |
Available |
|
Manufacturers Category |
Protein / Bio-Markers & CD Antigens |
Description |
Human Siglec-10, Fc (L118A, G120A, E201A) Tag (SI0-H5255) is expressed from human 293 cells (HEK293). It contains AA Met 17 - Thr 546 (Accession # Q96LC7-1). |
Molecule |
Siglec-10 |
Exp Region |
Met 17 - Thr 546 |
Storage |
-20℃ |
Shipping |
RT |
Stability |
-20°C to -70°C for 12 months in lyophilized state; -70°C for 3 months under sterile conditions after reconstitution.
For long term storage, the product should be stored at lyophilized state at -20°C or lower. |
Molecular Weight |
84.6 kDa |
Characteristics |
This protein carries a human IgG1 Fc (L118A, G120A, E201A) tag at the C-terminus. The protein has a calculated MW of 84.6 kDa. As the result of the mutations for Fc-Tag, the protein migrates as 90-110 kDa (Siglect-10 with Fc-Tag), 60-67 kDa (Siglect-10) and 30-32 kDa (Fc fragment) under reducing (R) condition (SDS-PAGE) due to glycosylation. Mutations (L118A, G120A, E201A /EU number: L235A/G237A/E318A) in human immunoglobulin G1 (hIgG1) Fc strongly reduce binding of the Fc mutant to cell expressed FcγRs, resulting in an almost 4-fold reduction in ADCC compared to that of wild type human IgG1. |
Endotoxin |
1.0 EU per μg |
Buffer |
PBS, pH7.4 |
Background |
The siglecs (sialic acid-binding Ig-like lectins) are a distinct subset of the Ig superfamily with adhesion-molecule-like structure. We describe here a novel member of the siglec protein family that shares a similar structure including five Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing two ITIM-signaling motifs. Siglec-10 was identified through database mining of an asthmatic eosinophil EST library. The Siglec-10-VAP-1 interaction seems to mediate lymphocyte adhesion to endothelium and has the potential to modify the inflammatory microenvironment via the enzymatic end products. |
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