TNFSF8/CD30 Ligand Extracellular Domain (human, recombinant) - 深圳欣博盛生物科技有限公司

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TNFSF8/CD30 Ligand Extracellular Domain (human, recombinant)

品牌： Cayman

产品货号： 40213-200 µg

规格： 200 µg

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数量： - +

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产品名称:

TNFSF8/CD30 Ligand Extracellular Domain (human, recombinant)
别名:

CD153|CD30L|TNFSF8|Tumor Necrosis Factor Ligand Superfamily Member 8
产品描述:

CD30 ligand (CD30L), also known as TNF superfamily member 8 (TNFSF8), is a single-pass type II membrane glycoprotein and member of the TNF and TNF receptor cytokine superfamily.{66556} It is composed of a cytoplasmic, transmembrane, and extracellular domain and forms non-covalent homotrimers.{66557,66556} CD30L is expressed on activated T cells, as well as on B cells, macrophages, and granulocytes.{66556,66558} It binds to CD30, inducing NF-κB- or ERK/MAPK-dependent downstream signaling that is involved in cell proliferation, cell activation, and the T cell-dependent immune response in a cell type- and cell activation status-dependent manner.{66556,66558,66559,52838,52839} CD30L can bind to both membrane-associated and soluble CD30, but binding to soluble CD30 prevents its binding to the membrane-bound form.{66556} CD30L is found on cells of various hematological cancers, including Hodgkin lymphoma and anaplastic large cell lymphoma, and expression of TNFSF8 is increased in leukocytes in autoimmune and inflammatory diseases, such as systemic lupus erythematosus (SLE) and asthma.{66559} Cayman’s TNFSF8/CD30 Ligand Extracellular Domain (human, recombinant; Fc-tagged) protein can be used for binding assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of CD30L (amino acids 63-234) fused to human IgG1 Fc at its N-terminus, consists of 429 amino acids, has a calculated molecular weight of 47.8 kDa, and a predicted N-terminus of Arg23 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 60-65 kDa by SDS-PAGE under reducing conditions.
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-80
运输温度:

-80
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Lyophilized from sterile PBS, pH 7.4
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365
产地:

美国
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≥95% estimated by SDS-PAGE
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