Other Proteins

Recombinant Murine Flt3-Ligand (Legacy Tebubio ref. 167250-31L). Flt3-Ligand is a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand binds to cells expressing the tyrosine kinase receptor Flt3. Flt3-Ligand, by itself does not stimulate proliferation of early hematopoietic cells, but synergizes with other CSFs and interleukins to induce growth and differentiation. Unlike SCF, Flt3-Ligand has no activity on mast cells. Multiple isoforms of Flt3-Ligand have been identified. The predominant biologically active form is anchored to the cell surface as the extracellular domain of a transmembrane protein (209 a.a.). The membrane-bound isoform can be proteolytically cleaved to generate a biologically active soluble isoform. Recombinant Murine Flt3-Ligand is a soluble 18.6 kDa protein consisting of 163 amino acid residues.

Recombinant Murine Flt3-Ligand (Legacy Tebubio ref. 167250-31L). Flt3-Ligand is a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand binds to cells expressing the tyrosine kinase receptor Flt3. Flt3-Ligand, by itself does not stimulate proliferation of early hematopoietic cells, but synergizes with other CSFs and interleukins to induce growth and differentiation. Unlike SCF, Flt3-Ligand has no activity on mast cells. Multiple isoforms of Flt3-Ligand have been identified. The predominant biologically active form is anchored to the cell surface as the extracellular domain of a transmembrane protein (209 a.a.). The membrane-bound isoform can be proteolytically cleaved to generate a biologically active soluble isoform. Recombinant Murine Flt3-Ligand is a soluble 18.6 kDa protein consisting of 163 amino acid residues.

Recombinant Murine IFN-lambda2 (Legacy Tebubio ref. 167250-33). IFN lambda1, 2, and 3 (also known as IL-29, IL-28A and IL-28B respectively) are distantly related to the IL-10 family and interferons. All three IFN-lambdas use a distinct receptor system composed of an IFN- lambdaR1 subunit (also called CRF2-12) and IL-10R2 subunit (also called CRF2-14). Signaling through this receptor system induces antiviral defenses similar to, but distinct from, that of type I interferons. Recombinant Murine IFN- lambda2 is a 19.8 kDa protein containing 175 amino acid residues.

Recombinant Murine IFN-lambda2 (Legacy Tebubio ref. 167250-33). IFN lambda1, 2, and 3 (also known as IL-29, IL-28A and IL-28B respectively) are distantly related to the IL-10 family and interferons. All three IFN-lambdas use a distinct receptor system composed of an IFN- lambdaR1 subunit (also called CRF2-12) and IL-10R2 subunit (also called CRF2-14). Signaling through this receptor system induces antiviral defenses similar to, but distinct from, that of type I interferons. Recombinant Murine IFN- lambda2 is a 19.8 kDa protein containing 175 amino acid residues.

Recombinant Murine Noggin (Legacy Tebubio ref. 167250-38). Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-beta family, and regulate their activity by inhibiting their access to signaling receptors. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant Murine Noggin is a 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.

Recombinant Murine Noggin (Legacy Tebubio ref. 167250-38). Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-beta family, and regulate their activity by inhibiting their access to signaling receptors. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant Murine Noggin is a 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.

Recombinant Murine BD-2 (Legacy Tebubio ref. 167250-40). Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The alpha-defensins are distinguished from the beta-defensins by the pairing of their three disulfide bonds. To date, six human beta-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. beta-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Murine BD-2 is a 5.5 kDa protein containing 51 amino acid residues.

Recombinant Murine BD-2 (Legacy Tebubio ref. 167250-40). Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The alpha-defensins are distinguished from the beta-defensins by the pairing of their three disulfide bonds. To date, six human beta-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. beta-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Murine BD-2 is a 5.5 kDa protein containing 51 amino acid residues.

Recombinant Murine BD-3 (Legacy Tebubio ref. 167250-41). Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The alpha-defensins are distinguished from the beta-defensins by the pairing of their three disulfide bonds. To date, six human beta-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. beta-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Murine BD-3 is a 4.6 kDa protein containing 41 amino acid residues.