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Description: Betacellulin is an EGF-related polypeptide growth factor that signals through the EGF receptor. It is produced in several tissues, including the pancreas, small intestine, and in certain tumor cells. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Human Betacellulin is initially synthesized as a glycosylated 32.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce the mature sequence. Recombinant Human Betacellulin is a 9.0 kDa monomeric protein, containing 80 amino acid residues, which comprises the mature EGF-homologous portion of the Betacellulin protein.
Catalog Number: 10772-224
Supplier: Peprotech


Description: Thrombomodulin (TM, CD141, THBD) is an endothelial cell-expressed, transmembrane glycoprotein that can form a complex with the coagulation factor, thrombin. The thrombomodulin/thrombin complex converts protein C to its activated form, protein Ca, which in turn proteolytically cleaves and deactivates factor Va and factor VIIIa, two essential components of the coagulation mechanism. This inactivation reduces the generation of additional thrombin, and thereby effectively prevents continued coagulation. Reduced levels of thrombomodulin can correlate with the pathogenesis of certain cardiovascular diseases, such as atherosclerosis and thrombosis. However, the serum levels of the truncated circulating form of thrombomodulin are typically elevated during inflammation and in the presence of various inflammatory-related diseases. The thrombomodulin protein contains 575 amino acids, including an 18 a.a. signal sequence, a 497 a.a. extracellular domain, a 24 a.a. transmembrane sequence, and a 36 a.a. cytoplasmic region. Recombinant Human Thrombomodulin is a 51.4 kDa, 491-amino-acid length glycoprotein containing the extracellular domain of thrombomodulin.
Catalog Number: 10772-308
Supplier: Peprotech

Description: Myostatin is a TGF-β family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation, and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the activin-binding protein follistatin, and by the propeptide of myostatin. The amino acid sequence of mature myostatin is extremely conserved across species, and is the same in murine, rat, chicken, turkey, porcine, and human. Myostatin is expressed as the C-terminal part of a precursor polypeptide, which also contains a short N-terminal signal sequence for secretion, and a propeptide of 243 amino acids. After dimerization of this precursor, the covalent bonds between the propeptide and the mature ligand are cleaved by furin-type proteases. However, the resulting two proteins remain associated through non-covalent interactions, and are secreted as a latent complex. Recombinant Human/Murine/Rat Myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond.
Catalog Number: 10772-408
Supplier: Peprotech

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.
Catalog Number: 10772-398
Supplier: Peprotech


Description: SPARC/Osteonectin is a secreted, evolutionarily-conserved, collagen-binding glycoprotein that is involved in a variety of cellular activities. It is highly expressed in tissues undergoing morphogenesis, remodeling and wound repair. SPARC/Osteonectin and its related peptides bind to numerous proteins of the extracellular matrix (ECM), affect ECM protein expression, influence cellular adhesion and migration, and modulate growth factor-induced cell proliferation and angiogenesis. SPARC/Osteonectin consists of three domains: an N-terminal acidic region that binds calcium ions with low affinity, a module containing two EF-hand motifs that bind calcium with high affinity, and a cysteine-rich follistatin-like domain. Recombinant Human SPARC/Osteonectin is a glycoprotein containing 286 amino acids that migrates at an apparent MW of 43.7 kDa by SDS-PAGE analysis due to the effect of glycosylation. The calculated molecular weight of Recombinant Human SPARC/Osteonectin is 32.7 kDa.
Catalog Number: 10772-698
Supplier: Peprotech


Description: CYR61 is a member of the CCN family of secreted cysteine-rich regulatory proteins. CYR61 induces angiogenesis by stimulating the proliferation, migration, and adhesion of endothelial cells. Cell migration and adhesion are mediated through binding to specific cell surface integrins and to heparin sulfate proteoglycans. Increased expression of CYR61 is associated with several types of cancer, and correlates with the progression and estrogen independence of human breast cancers. Recombinant Human CYR61 is a 39.4 kDa protein containing 357 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Catalog Number: 10772-624
Supplier: Peprotech


Description: Wnt-7a belongs to the Wnt family of signaling proteins that play a key role in maintaining the integrity of embryonic and adult tissues. It is expressed in placenta, kidney, testis, uterus, fetal lung, and fetal and adult brain. Most Wnt proteins can signal though a mechanism called the canonical Wnt pathway, in which Wnt proteins bind to and activate seven-pass transmembrane receptors of the Frizzled family, ultimately leading to the disruption of β-catenin degradation. Intracellular accumulation of β-catenin increases translocation of the protein into the nucleus, where it binds to TCF/LEF transcription factors to induce the expression of numerous genes. Increased Wnt/β-catenin signaling is associated with tumorigenesis in a diverse set of human cancers. However, Wnt-7a/Frizzled-9 signaling has been shown to act as a tumor suppressor in non-small cell lung cancers. Recombinant Human Wnt-7a is a 35.5 kDa glycoprotein containing 318 amino acids. Due to glycosylation, Wnt-7a migrates between 40-55 kDa by SDS-PAGE gel under unreduced conditions.
Catalog Number: 10772-684
Supplier: Peprotech


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.
Catalog Number: 10772-724
Supplier: Peprotech


Description: TIGAR is a p53-inducible enzyme that catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is a powerful activator of 6-phosphofructose-1 kinase, the rate limiting enzyme of glycolysis. By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing via the pentose phosphate pathway, the major cellular source for NADPH. Recombinant Human TIGAR expressed in
Catalog Number: 10772-836
Supplier: Peprotech


Description: Uteroglobin, which is a member of the Secretoglobin superfamily and is also known as Clara cell phospholipid-binding protein, is a multifunctional protein that can exert anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. The small, non-glycosylated protein named for its high levels of expression in pre-implantation embryos, where it exhibits growth stimulatory effects, is produced and secreted by the non-ciliated, non-mucous Clara cells predominant in the epithelial surfaces of pulmonary airways, as well as other non-ciliated epithelia. Members of the Secretoglobin superfamily demonstrate a high level of structural conservation and are characterized as small, secretory homo- or heterodimers. In addition to sequestering pro-inflammatory mediators and carcinogens, Uteroglobin has been implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. Recombinant Human Uteroglobin is a 16.1 kDa homodimeric protein consisting of 142 amino acid residues.
Catalog Number: 10772-900
Supplier: Peprotech


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.
Catalog Number: 10773-292
Supplier: Peprotech


Description: All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. Recombinant Murine MIP-2 (CXCL2) is a 7.8 kDa protein consisting of 73 amino acids, including the ‘ELR’ motif common to the CXC chemokine family that binds to CXCR1 or CXCR2.
Catalog Number: 10773-228
Supplier: Peprotech

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.
Catalog Number: 10773-428
Supplier: Peprotech

Description: Recombinant Human TPO, Animal Free, 174AA polypeptide18.6kda, which contains the erythropoietin-like domain of the full length TPO protein, source: E.coli, reactivity: Monkey, Leech, Rat, Purity: >98%, Synonym: Thrombopoietin, Megakaryocyte colony-stimulating factor, 10ug
Catalog Number: 10773-600
Supplier: Peprotech

Description: ENA-78 is a CXC chemokine that signals through the CXCR2 receptor. It is expressed in monocytes, platelets, endothelial cells, and mast cells. ENA-78 is a chemoattractant for neutrophils. The three naturally occurring variants of human ENA-78; ENA 5-78, ENA 9-78 and ENA 10-78, contain 74, 70, and 69 amino acid residues, respectively, and possess the same biological activity. ENA-78 contains the four conserved cysteine residues present in CXC chemokines, and also contains the ‘ELR’ motif common to CXC chemokine that bind to the CXCR1 and CXCR2 receptors. Recombinant Human ENA-78 (CXCL5) is an 8.0 kDa protein consisting of 74 amino acid residues.
Catalog Number: 10773-652
Supplier: Peprotech


Description: The MCP proteins are members of the CC chemokine family that signal through CCR2 and, with the exception of MCP-1, other CCR receptors. The MCP proteins chemoattract and activate monocytes, activated T cells, basophils, NK cells, and immature dendritic cells. The MCP family cross-reacts across species. Recombinant Human MCP-4 (CCL13) is an 8.6 kDa protein containing 75 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Catalog Number: 10773-700
Supplier: Peprotech


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