SIGLEC11 Antibody (N-term) Blocking Peptide
€363.00
In stock
SKU
AC-BP1629a
Background:
SIGLECs are members of the immunoglobulin superfamily that are expressed on the cell surface. Most SIGLECs have one or more cytoplasmic immune receptor tyrosine-based inhibitory motifs (ITIM). SIGLECs are typically expressed on cells of the innate immune system, with the exception of the B-cell expressed SIGLEC6. Sequence analysis predicted that the 697-amino acid SIGLEC10 protein contains a signal peptide, an N-terminal V-set Ig-like domain and four C2-set Ig-like domains, five potential N-linked glycosylation sites, a transmembrane region, and a 126-residue cytoplasmic tail with 3 putative ITIMs. Northern blot analysis detected a major 3.0-kb SIGLEC10 transcript, with highest levels in spleen, lymph node, blood leukocytes, and appendix. Little or no expression was observed in pancreas, thyroid, and testis. Flow cytometric analysis demonstrated eosinophil-specific expression of SIGLEC10, but at a lower level than that of SIGLEC8. Expression was also detected on monocytes and a CD16-positive/CD56-negative natural killer-like lymphocyte population. After sialidase treatment, which is necessary for unmasking the sialic acid-binding site on SIGLECs interacting with cell surface sialic acids, cells expressing SIGLEC10 bound to red blood cells. Immunoprecipitation analysis indicated expression of a 100- to 120-kD monomeric protein, higher than the predicted molecular mass, suggesting that SIGLEC10 is glycosylated.
Other Names:
Sialic acid-binding Ig-like lectin 11, Sialic acid-binding lectin 11, Siglec-11, SIGLEC11
Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP1629a was selected from the N-term region of human SIGLEC11 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Gene Name: SIGLEC11
Gene ID: 114132
Primary Accession: Q96RL6
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
SIGLECs are members of the immunoglobulin superfamily that are expressed on the cell surface. Most SIGLECs have one or more cytoplasmic immune receptor tyrosine-based inhibitory motifs (ITIM). SIGLECs are typically expressed on cells of the innate immune system, with the exception of the B-cell expressed SIGLEC6. Sequence analysis predicted that the 697-amino acid SIGLEC10 protein contains a signal peptide, an N-terminal V-set Ig-like domain and four C2-set Ig-like domains, five potential N-linked glycosylation sites, a transmembrane region, and a 126-residue cytoplasmic tail with 3 putative ITIMs. Northern blot analysis detected a major 3.0-kb SIGLEC10 transcript, with highest levels in spleen, lymph node, blood leukocytes, and appendix. Little or no expression was observed in pancreas, thyroid, and testis. Flow cytometric analysis demonstrated eosinophil-specific expression of SIGLEC10, but at a lower level than that of SIGLEC8. Expression was also detected on monocytes and a CD16-positive/CD56-negative natural killer-like lymphocyte population. After sialidase treatment, which is necessary for unmasking the sialic acid-binding site on SIGLECs interacting with cell surface sialic acids, cells expressing SIGLEC10 bound to red blood cells. Immunoprecipitation analysis indicated expression of a 100- to 120-kD monomeric protein, higher than the predicted molecular mass, suggesting that SIGLEC10 is glycosylated.
Other Names:
Sialic acid-binding Ig-like lectin 11, Sialic acid-binding lectin 11, Siglec-11, SIGLEC11
Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP1629a was selected from the N-term region of human SIGLEC11 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Gene Name: SIGLEC11
Gene ID: 114132
Primary Accession: Q96RL6
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
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