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Supplier: PeproTech, Inc.

Description: GLP-1 is a proglucagon-derived peptide hormone secreted primarily by intestinal L cells during feeding. Its major physiological function is the stimulation of pancreatic β cells to release appropriate amounts of insulin after glucose absorption. Other biological actions exhibited by GLP-1 include the suppression of plasma glucagon levels, inhibition of gastric motility, and promotion of satiety. The secretion of GLP-1 from intestinal L cells is stimulated by nutrients, hormones, and neural inputs. On the other hand, insulin has been reported to inhibit GLP-1 release, indicating that a feedback loop mechanism regulates GLP-1 secretion. In addition to being the precursor of GLP-1, proglucagon, whose primary structure is highly conserved in mammalian species, is also the precursor for other members of the glucagon family of peptide hormones, including glicentin-related pancreatic peptide (GRPP), glucagons, and GLP-2. Recombinant Human GLP-1 is a 3.3 kDa polypeptide consisting of 31 amino acid residues.

Supplier: PeproTech, Inc.

Description: Produced from sera of rabbits immunized with highly pure Recombinant Human IL-3. Anti­Human IL-3­specific antibody was purified by affinity chromatography employing an immobilized Human IL-3 matrix.

Supplier: PeproTech, Inc.

Description: Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-β 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.

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Supplier: PeproTech, Inc.

Description: Produced from sera of rabbits immunized with highly pure Recombinant Human Flt3-Ligand. Anti­Human Flt3-Ligand­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: PeproTech, Inc.

Description: 4-1BB receptor, a member of the TNFR superfamily of receptors, is mainly expressed on the surface of T cells, but also found in B cells, monocytes, and various transformed cell lines. 4-1BB receptor binds to 4-1BBL to provide a co-stimulatory signal for T lymphocytes. Signaling by 4-1BB receptor has been implicated in the antigen-presentation process and generation of cytotoxic T cells. The human 4-1BB receptor gene codes for a 255 amino acid type I transmembrane protein containing a 17 amino acid N-terminal signal sequence, a 169 amino acid extracellular domain, a 27 amino acid transmembrane domain and a 42 amino acid cytoplasmic domain. Recombinant Human 4-1BB Receptor is a 167 amino acid polypeptide (17.7 kDa), which contains the cysteine-rich TNFR-like extracellular domain of 4-1BB receptor.

Supplier: PeproTech, Inc.

Description: Produced from sera of goats immunized with highly pure Recombinant Human Resistin. Anti­Human Resistin­specific antibody was purified by affinity chromatography employing an immobilized Human Resistin matrix.

Supplier: PeproTech, Inc.

Description: BMPs (Bone Morphogenetic Proteins) belong to the TGF-β superfamily of structurally related signaling proteins. BMP-2 is a potent osteoinductive cytokine, capable of inducing bone and cartilage formation in association with osteoconductive carriers such as collagen and synthetic hydroxyapatite. In addition to its osteogenic activity, BMP-2 plays an important role in cardiac morphogenesis, and is expressed in a variety of tissues, including lung, spleen, brain, liver, prostate ovary and small intestine. The functional form of BMP-2 is a 26 kDa protein composed of two identical 114 amino acid polypeptide chains linked by a single disulfide bond. Each BMP-2 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 23 amino acid signal sequence for secretion, and a 259 amino acid propeptide. After dimerization of this precursor, the covalent bonds between the propeptide (which is also a disulfide-linked homodimer) and the mature BMP-2 ligand are cleaved by a furin-type protease. Recombinant Human BMP-2 is a 26.0 kDa homodimeric protein consisting of two 115 amino acid polypeptide chains. Manufactured using all Animal-Free reagents.

Supplier: PeproTech, Inc.

Description: Vimentin is a class III intermediate filament protein predominantly found in cells of mesenchymal origins, such as vascular endothelium and blood cells, where it functions as a major cytoskeletal component. Due to its importance and abundance in the cytoskeletal structure of mesenchymally-derived cells, vimentin is frequently used as a developmental marker within cells of mesenchymal origin or cells undergoing epithelial-mesenchymal transition, which can occur during both normal and metastatic growth. An active participant within several critical processes of cellular organization and protein regulation, vimentin is involved in the anchorage of organelles within the cytoplasmic matrix, development of astrocytes, and the disassembly of cellular components during the execution phase of apoptosis. Abnormalities in the normal physiological pathways of vimentin have been implicated in deficient motility and directional migration involved in wound healing, cellular growth and development, as well as the adhesion-site accumulation of vimentin on lens epithelial cells in cases of dominant cataracts. Recombinant Human Vimentin is a 54.3 kDa protein consisting of 471 amino acid residues, including a 6-residue C-terminal His-Tag.

Supplier: PeproTech, Inc.

Description: The Insulin/Relaxin structural family of proteins consists of at least seven members, each containing an insulin-like heterodimeric structure of two polypeptide chains held together by two inter-chain disulfide bonds. The INSL5/INSL7 hybrid contains the β-chain of INSL7 (Relaxin-3), linked to the α-chain of INSL5. The INSL5/INSL7 hybrid protein can specifically activate the G protein-coupled receptors, GPCR135 and GPCR142, but unlike Relaxin-3, does not induce significant activation of the LGR7 receptor. Recombinant Human INSL5/INSL7 Hybrid is a heterodimeric, 5.2 kDa protein consisting of a 27 amino acid β-chain linked to a 21 amino acid α-chain by two disulfide bonds.

Supplier: PeproTech, Inc.

Description: Produced from sera of rabbits immunized with highly pure Recombinant Human EGF. Anti­Human EGF­specific antibody was purified by affinity chromatography employing an immobilized Human EGF matrix.

Supplier: PeproTech, Inc.

Description: Produced from sera of rabbits immunized with highly pure Recombinant Murine IL-4. Anti­Murine IL-4­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: PeproTech, Inc.

Description: Produced from sera of rabbits immunized with highly pure Recombinant Human Flt3-Ligand. Anti­Human Flt3-Ligand­specific antibody was purified by affinity chromatography employing an immobilized Human Flt3-Ligand matrix.

Supplier: PeproTech, Inc.

Description: Eotaxin-2 is a CC chemokine that signals through the CCR3 receptor. It is produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3, including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Additionally, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which also includes a C-terminal truncation, contains 78 amino acid residues (92 a.a. residues for the murine homolog, without C-terminal truncation). Eotaxin-2 contains the four conserved cysteine residues present in CC chemokines. Recombinant Murine Eotaxin-2 (CCL24) is a 10.3 kDa protein containing 93 amino acid residues.

Supplier: PeproTech, Inc.

Description: 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 α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-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 β-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. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Human BD-1 is a 3.9 kDa protein containing 36 amino acid residues.

Supplier: PeproTech, Inc.

Description: IL-22 is a member of the IL-10 family of regulatory cytokines, which includes IL-10, IL-19, IL-20, IL-22, IL-24 and IL-26. Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the liver and pancreas. IL-22 signals through a receptor system consisting of IL-10Rβ/CRF2-4 and IL-22R, both of which are members of the class II cytokine-receptor family. Recombinant Human IL-22 is a 33.6 kDa, non-disulfide-linked, homodimeric protein consisting of two 147 amino acid polypeptide chains.

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Supplier: PeproTech, Inc.

Description: Produced from sera of rabbits immunized with highly pure Recombinant Human β-NGF. Anti­Human β-NGF­specific antibody was purified by affinity chromatography and then biotinylated.