抗人 CD302 抗体对
01AB00763
CD302 molecule (CD302), also known as CLEC13A or DCL1, is a type I transmembrane C-type lectin receptor primarily involved in cell adhesion, migration, endocytosis, and phagocytosis. Structurally, it is a 232-amino-acid protein with a 146-amino-acid extracellular domain, a 21-amino-acid transmembrane segment, and a 43-amino-acid cytoplasmic region. The extracellular domain is predicted to contain eight beta strands and two alpha helices, and CD302 is highly conserved across species, sharing 82% sequence identity with its mouse and rat counterparts. Unlike classical C-type lectin receptors, CD302 lacks the amino acid residues necessary for calcium-dependent sugar binding, suggesting a unique ligand recognition mechanism. CD302 is most abundantly expressed in the liver, followed by the lungs, spleen, and myeloid cells such as monocytes, granulocytes, and dendritic cells. Disease relevance includes its identification as an intergenic splice variant forming a fusion protein with DEC-205/CD205 in Hodgkin's lymphoma cell lines, indicating a potential role in hematological malignancies.
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技术参数
- 靶点基因名
- CD302
- 基因别名
- CLEC13A; DCL1; KIAA0022
- 蛋白别名
- CD302 molecule; CD302
- UniProt
- Q8IX05
- 物种
- Human
产品详情
- 靶点名称
- CD302
- 蛋白名称
- CD302 molecule
- 蛋白别名
- CD302 antigen; C-type lectin BIMLEC; C-type lectin domain family 13 member A; DEC205-associated C-type lectin 1; Type I transmembrane C-type lectin receptor DCL-1; CD antigen CD302
- 靶点基因名
- CD302
- 基因别名
- CLEC13A; DCL1; KIAA0022
- UniProt
- Q8IX05
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
CD302 molecule (CD302), also known as CLEC13A or DCL1, is a type I transmembrane C-type lectin receptor primarily involved in cell adhesion, migration, endocytosis, and phagocytosis. Structurally, it is a 232-amino-acid protein with a 146-amino-acid extracellular domain, a 21-amino-acid transmembrane segment, and a 43-amino-acid cytoplasmic region. The extracellular domain is predicted to contain eight beta strands and two alpha helices, and CD302 is highly conserved across species, sharing 82% sequence identity with its mouse and rat counterparts. Unlike classical C-type lectin receptors, CD302 lacks the amino acid residues necessary for calcium-dependent sugar binding, suggesting a unique ligand recognition mechanism. CD302 is most abundantly expressed in the liver, followed by the lungs, spleen, and myeloid cells such as monocytes, granulocytes, and dendritic cells. Disease relevance includes its identification as an intergenic splice variant forming a fusion protein with DEC-205/CD205 in Hodgkin's lymphoma cell lines, indicating a potential role in hematological malignancies.