outgrowth

Expression system: E. coli
Length: 29-151, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 20-865, Full Length of Mature Protein
Activity: ELISA

Expression system: E. coli
Length: 213-450, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-380, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-315, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1888-2201, Partial
Activity: Not Tested

Expression system: E. coli
Length: 34-330, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 509-794, Extracellular Domain
Activity: Not Tested

Expression system: E. coli
Length: 21-182, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 1631-1907, Partial
Activity: Not Tested

Expression system: E. coli
Length: 21-143, Full Length of Mature Protein
Activity: Cell Activity

Expression system: HEK293 Cells
Length: 1-370, Full Length
Activity: Not Tested

Signal Regulatory Protein α (SIRPα) is a monomeric approximately 90 kD type I transmembrane glycoprotein. The 504 amino acid human SIRPα contains two Ig-like C1-type domains and one Ig-like V-type domain. SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation

Expression system: HEK293 Cells
Length: 31-370, Extracellular Domain
Activity: BLI

Expression system: HEK293 Cells
Length: 28-579, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 26-546, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 31­542, Partial
Activity: Not Tested

Spondin-2, also referred to as mindin, belongs to the F-spondin family of secreted extracellular matrix proteins. Spondins are characterised by the presence of F-spondin domains 1 and 2 (FS1 and FS2) at the N-terminus and a thrombospondin-type 1 repeat (TSR1) domain at the C-terminus. Spondin-2 functions as a pattern-recognition molecule for bacterial and viral pathogens and as an integrin ligand for inflammatory cell recruitment and T cell priming. In addition to its roles in promoting neuron outgrowth and inhibiting both cancer and angiogenesis, Spondin-2 plays an important role in the initiation of the immune response and is involved in inflammatory processes.

Expression system: E. coli
Length: 1-412, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 36-139, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 32-373, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 29-409, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 29-409, Partial
Activity: Not Tested

Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5) was identified as a metastatic driver. CEACAM5 overproduction enriched for an epithelial gene expression pattern and facilitated tumor outgrowth at metastatic sites. Tissues from patients with metastatic breast cancer confirmed elevated levels of CEACAM5 in lung metastases relative to breast tumors, and an inverse correlation between CEACAM5 and the mesenchymal marker vimentin was demonstrated.