생물학적 소스
mouse
Quality Level
결합
unconjugated
항체 형태
purified immunoglobulin
항체 생산 유형
primary antibodies
클론
120612, monoclonal
양식
lyophilized powder
종 반응성
human
기술
flow cytometry: suitable
immunohistochemistry: 8-25 μg/mL using cell or in fixed tissue sections
동형
IgG2a
UniProt 수납 번호
저장 온도
−20°C
타겟 번역 후 변형
unmodified
유전자 정보
human ... CD209(30835) , CLEC4M(10332)
일반 설명
DC-SIGN1 is a type II protein C-type lectin that binds mannose-rich molecules such as ICAM-3 and ICAM-2 in a calcium dependent manner. DC-SIGN1, a 44kDa molecule, is identical to the HIV-1 binding protein. Analysis of various tissues and cell lines suggests that DC-SIGN1 expression is restricted to dendritic cells, although there is evidence of expression in placenta, resting monocytes, and monocytic cell lines. DC-SIGN2 (DC-SIGNR), located on human chromosome 19p13.3, shares 73-80% amino acid identity with DC-SIGN1. DC-SIGN2 is polymorphic and is primarily transcribed in the liver and lymph nodes but not in monocyte-derived DC. Expression of DC-SIGN2 is restricted to endothelial cells derived from liver sinusoids, lymph nodes sinuses, and capillaries. Membrane and soluble forms of the protein have also been found to be expressed in placenta and some monocytic cell lines.
특이성
Recognizes both human DC-SIGN1 and human DC-SIGN2 on transfected cells and reacts with human dendritic cells. The antibody does not react with parental mouse cells or irrelevant transfectants.
면역원
purified from NIH/3T3 cells transfected with recombinant human DC-SIGN2 (DC-SIGNR).
애플리케이션
Monoclonal Anti-DC-SIGN1/DC-SIGN2 antibody produced in mouse is suitable for flow cytometry and immunohistochemistry at a working concentration of 8-25ug/mL using cell or in fixed tissue sections.
생화학적/생리학적 작용
DC-SIGN1 is involved in molecular interactions between dendritic cells and resting T-cells. DC-SIGN interacts with viruses such as X4, R5, X4R5 HIV-1 strains, HIV-2, and SIV. It captures HIV-1 through its interaction with the gp120 envelope glycoprotein and promotes efficient infection of CD4+ T cells that co-express chemokine receptors. DC-SIGN2 also binds mannose residues in a calcium dependent fashion, including ICAM-3 and HIV-1 gp120. It binds to human and simian immunodeficiency viruses and activates infection in trans.
물리적 형태
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline with 5% trehalose.
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A A Bashirova et al.
The Journal of experimental medicine, 193(6), 671-678 (2001-03-21)
The discovery of dendritic cell (DC)-specific intercellular adhesion molecule (ICAM)-3-grabbing nonintegrin (DC-SIGN) as a DC-specific ICAM-3 binding receptor that enhances HIV-1 infection of T cells in trans has indicated a potentially important role for adhesion molecules in AIDS pathogenesis. A
S Pöhlmann et al.
Journal of virology, 75(10), 4664-4672 (2001-04-20)
Dendritic cells (DCs) efficiently bind and transmit human immunodeficiency virus (HIV) to cocultured T cells and so may play an important role in HIV transmission. DC-SIGN, a novel C-type lectin that is expressed in DCs, has recently been shown to
S Pöhlmann et al.
Proceedings of the National Academy of Sciences of the United States of America, 98(5), 2670-2675 (2001-02-28)
DC-SIGN, a C-type lectin expressed on the surface of dendritic cells (DCs), efficiently binds and transmits HIVs and simian immunodeficiency viruses to susceptible cells in trans. A DC-SIGN homologue, termed DC-SIGNR, has recently been described. Herein we show that DC-SIGNR
E J Soilleux et al.
Journal of immunology (Baltimore, Md. : 1950), 165(6), 2937-2942 (2000-09-07)
DC-SIGN is a C-type lectin, expressed on a dendritic cell subset. It is able to bind ICAM3 and HIV gp120 in a calcium-dependent manner. Here we report the genomic organization of DC-SIGN and map it to chromosome 19p13 adjacent to
T B Geijtenbeek et al.
Cell, 100(5), 575-585 (2000-03-18)
Contact between dendritic cells (DC) and resting T cells is essential to initiate a primary immune response. Here, we demonstrate that ICAM-3 expressed by resting T cells is important in this first contact with DC. We discovered that instead of
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