Other Proteins

Complement Component 5a

Thyroid Stimulating Hormone

Glucagon Like Peptide 1

Recombinant Human Nidogen-1 (Legacy Tebubio ref. 167140-17). Recombinant Human Nidogen-1 is a 133.5 kDa protein, consisting of 1,219 amino acids, which corresponds to the mature sequence of the full-length protein.

Recombinant Human Nidogen-1 (Legacy Tebubio ref. 167140-17). Recombinant Human Nidogen-1 is a 133.5 kDa protein, consisting of 1,219 amino acids, which corresponds to the mature sequence of the full-length protein.

Recombinant Human Granzyme B (Legacy Tebubio ref. 167140-18). Recombinant Human Granzyme B is a 235 amino acid protein, which includes the mature 227 amino acid sequence, as well as an 8 amino acid C-terminal His-tag. Due to glycosylation, this protein migrates to an approximate molecular weight of 30-40 kDa, under reducing and non-reducing conditions.

Recombinant Human Granzyme B (Legacy Tebubio ref. 167140-18). Recombinant Human Granzyme B is a 235 amino acid protein, which includes the mature 227 amino acid sequence, as well as an 8 amino acid C-terminal His-tag. Due to glycosylation, this protein migrates to an approximate molecular weight of 30-40 kDa, under reducing and non-reducing conditions.

Recombinant Human Agrin (Legacy Tebubio ref. 167160-08). Agrin is a molecule that resides in the basal lamina of muscle cells and directs key events in post synaptic differentiation. Most notably, Agrin is responsible for the clustering of acetylcholine receptors (AChRs) on the cell surface and their localization to the neuromuscular junction. Several Agrin variants have been identified which arise from alternative mRNA splicings. Agrin splice forms having inserts at two sites in the carboxy terminus designated "y" and "z" display a high affinity for AChRs, while splice forms lacking these inserts associate with AChRs weakly. Muscle alpha-dystroglycan has been postulated to be the receptor for the clustering activity of agrin; however, this is a point of contention. Tyrosine phosphorylation has been implicated as a required early step in AChR aggregation. Interestingly, a unique receptor tyrosine kinase, designated MuSK, has been discovered that interacts with Agrin and is specifically

Recombinant Human Agrin (Legacy Tebubio ref. 167160-08). Agrin is a molecule that resides in the basal lamina of muscle cells and directs key events in post synaptic differentiation. Most notably, Agrin is responsible for the clustering of acetylcholine receptors (AChRs) on the cell surface and their localization to the neuromuscular junction. Several Agrin variants have been identified which arise from alternative mRNA splicings. Agrin splice forms having inserts at two sites in the carboxy terminus designated "y" and "z" display a high affinity for AChRs, while splice forms lacking these inserts associate with AChRs weakly. Muscle alpha-dystroglycan has been postulated to be the receptor for the clustering activity of agrin; however, this is a point of contention. Tyrosine phosphorylation has been implicated as a required early step in AChR aggregation. Interestingly, a unique receptor tyrosine kinase, designated MuSK, has been discovered that interacts with Agrin and is specifically