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>   首页   >   产品   >   一抗   >   免疫学   >   SIGLEC5 Antibody (C-term)   

SIGLEC5 Antibody (C-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - SIGLEC5 Antibody (C-term) AP1623b
    The anti-Siglec5 C-term Pab (Cat. #AP1623b) is used in Western blot to detect Siglec5 in mouse liver tissue lysate.
  • 1 - SIGLEC5 Antibody (C-term) AP1623b
    SIGLEC5 Antibody (Cat. #AP1623b) western blot analysis in SK-BR-3 cell line lysates (35ug/lane).This demonstrates the SIGLEC5 antibody detected the SIGLEC5 protein (arrow).
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession O15389
Reactivity Human, Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 60715 Da
Antigen Region 482-513 aa
Additional Information
Gene ID 8778
Other Names Sialic acid-binding Ig-like lectin 5, Siglec-5, CD33 antigen-like 2, Obesity-binding protein 2, OB-BP2, OB-binding protein 2, CD170, SIGLEC5, CD33L2, OBBP2
Target/Specificity This SIGLEC5 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 482-513 amino acids from the C-terminal region of human SIGLEC5.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsSIGLEC5 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name SIGLEC5
Synonyms CD33L2, OBBP2
Function Putative adhesion molecule that mediates sialic-acid dependent binding to cells. 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.
Cellular Location Membrane; Single-pass type I membrane protein.
Tissue Location Expressed by monocytic/myeloid lineage cells. Found at high levels in peripheral blood leukocytes, spleen, bone marrow and at lower levels in lymph node, lung, appendix, placenta, pancreas and thymus. Expressed by monocytes and neutrophils but absent from leukemic cell lines representing early stages of myelomonocytic differentiation
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

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.

REFERENCES

Erickson-Miller, C.L., et al., Exp. Hematol. 31(5):382-388 (2003).
Patel, N., et al., J. Biol. Chem. 274(32):22729-22738 (1999).
Cornish, A.L., et al., Blood 92(6):2123-2132 (1998).
Kim, H.S., Cytogenet. Cell Genet. 84 (1-2), 96 (1999).

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