Verified Samples in WB: Mouse lung

WB 1:500-1:1000

Polyclonal

IgG

Recombinant Mouse CD105 protein expressed by Mammalian

CD105

END, HHT1, ORW, ORW1, CD 105, CD105 antigen, EGLN, FLJ41744, Osler Rendu Weber syndrome 1, RP11 228B15.2, SN6, HHT, ORW1, AI528660, AI662476, CD105, END, Endo, Endoglin, HHT1, ORW, S-endoglin, Edg, Eng

71 kDa

95-100 kDa

Cell membrane, Membrane

Detected on blood vessels. Detected on adult pulmonary artery, capillaries supporting the heart muscle and lung alveolar capillary endothelial cells. Endoglin is restricted to endothelial cells in all tissues except bone marrow and is also found in stromal cells within the connective tissue of intestine, stomach, heart, skeletal muscle, uterus, ovary, oviduct, testis and thymus.

1 mg/mL

Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.

PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4

Antigen Affinity Purification

Immunology, Stem Cells, Cancer, Cardiovascular, Antibody Arrays, Developmental Biology, Signal Transduction

Unconjugated

Endoglin (CD105) is a 90 kDa type I transmembrane glycoprotein of the zona pellucida (ZP) family of proteins. Endoglin and betaglycan/T beta RIII are type III receptors for TGF beta superfamily ligands,sharing 71% aa identity in the transmembrane (TM) and cytoplasmic domains. Endoglin is highly expressed on proliferating vascular endothelial cells,chondrocytes,and syncytiotrophoblasts of term placenta,with lower amounts on hematopoietic,mesenchymal and neural crest stem cells,activated monocytes,and lymphoid and myeloid leukemic cells. Human endoglin cDNA encodes 658 amino acids (aa) including a 25 aa signal sequence,a 561 aa extracellular domain (ECD) with an orphan domain and a two-part ZP domain,a TM domain and a 47 aa cytoplasmic domain. An isoform with a 14 aa cytoplasmic domain (S-endoglin) can oppose effects of long (l) endoglin. The human endoglin ECD shares 65-72% aa identity with mouse,rat,bovine,porcine and canine endoglin. Endoglin homodimers interact with TGF-beta 1 and TGF-beta 3 (but not TGF-beta 2),but only after binding T beta RII. Similarly,they interact with Activin A and BMP-7 via activin type IIA or B receptors,and with BMP-2 via BMPR-IA/AlK-3 or BMPR-IB/AlK-6. BMP-9,however,is reported to bind endoglin directly. Endoglin modifies ligand-induced signaling in multiple ways. For example,expression of endoglin can inhibit TGF-beta 1 signals but enhance BMP-7 signals in the same myoblast cell line.