You Searched For: Ultrasound+Gels

Supplier: Peprotech

Description: FGF-10 is a heparin-binding growth factor that belongs to the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-10 is most related to KGF/FGF-7, and is expressed during the development and, preferentially, in adult lungs. It signals through the FGFR 2b. Recombinant Human FGF-10 is a 19.3 kDa protein consisting of 170 amino acid residues.

Supplier: Peprotech

Description: IL-17E is a disulfide-linked homodimer of two 145 amino acid polypeptide chains. It belongs to the IL-17 family of structurally-related cytokines that share a highly conserved C-terminal region, but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers. IL-17E stimulates secretion of IL-8, and induces activation of the transcription factor NF-κB in cells that express the IL-17BR receptor. Recombinant Human IL-17E is a 33.8 kDa disulfide-linked homodimer of two 146 amino acid polypeptide chains.

Catalog Number: (75790-114)

Supplier: Prosci

Description: Mucin-15 is a single-pass type I membrane protein member of the Mucin family. Mucins are a family of high molecular weight, heavily glycosylated proteins (glycoconjugates) produced by epithelial tissues in most metazoans. A key characteristic of Mucins is their ability to form gels. Therefore they are a key component in most gel-like secretions, serving functions from lubrication to cell signalling to forming chemical barriers. Mucin-15 is expressed in many tissues. Mucin-15 is highly glycosylated (N- and O-linked carbohydrates). Mucin-15 may play a role in the cell adhesion to the extracellular matrix.

Catalog Number: (76304-094)

Supplier: Peprotech

Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP2 is a cysteine-rich, secreted protein produced by bone cells, and is most abundant in the brain. IGF-BP2 has been shown to inhibit IGF-II action in human breast and ovarian carcinoma cells. Recombinant Human IGF-BP2 is a 31.5 kDa protein consisting of 289 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.

Supplier: Peprotech

Description: IL-1α is a non-secreted, proinflammatory cytokine produced in a variety of cells, including monocytes, tissue macrophages, keratinocytes, and other epithelial cells. Both IL-1α and IL-1β bind to the same receptor and have similar, if not identical, biological properties. These cytokines have a broad range of activities including the stimulation of thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, mitogenic FGF-like activity, and the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1β is a secreted cytokine, IL-1α is predominantly a cell-associated cytokine. Recombinant Rat IL-1α is a 17.7 kDa protein containing 155 amino acid residues.

Supplier: Peprotech

Description: FGF-9 is a heparin-binding growth factor that belongs to the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-9 targets glial cells, astrocytes cells and other cells that express the FGFR 1c, 2c, 3b, 3c, and 4. Recombinant Human FGF-9 is a 23.2 kDa protein consisting of 206 amino acid residues.

Supplier: Peprotech

Description: Resistin belongs to a family of tissue-specific cytokines termed FIZZ (found in inflammatory zones) and RELM. The four known members of this family, resistin, RELMα, RELMβ, and RELMγ, share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Resistin is an adipose-derived cytokine (adipokine) whose physiological function and molecular targets are largely unknown. Studies have shown that resistin suppresses insulin's ability to stimulate glucose uptake, and postulated that resistin might be an important link between obesity and Type 2 diabetes. Other studies have indicated that resistin expression is severely suppressed in obesity, and that it may act as a feedback regulator of Adipogenesis. Recombinant Rat Resistin is a 20.0 kDa, disulfide-linked, homodimeric protein composed of two 94 identical amino acid chains linked by a single disulfide bond.

Supplier: Peprotech

Description: The Fibroblast Growth Factor (FGF) Superfamily is comprised of multifunctional proteins that serves to regulate several complex biological processes related to the development, restoration, and/or redistribution of prenatal and postnatal tissue, as well as angiogenesis, wound healing, nerve regeneration, chronic inflammation, and cancer growth. Members of the FGF Superfamily function through paracrine, autocrine and intracrine pathways to promote spatial and temporal integrations of several cell responses, such as proliferation, growth, differentiation, and migration. Fibroblast growth factor binding protein 1 (FGF-BP-1) is a secreted glycoprotein, which contains both a heparin-binding domain and a distinct FGF-binding region, that is shed into circulation where it acts as a chaperone molecule for FGFs, most notably FGF-acidic and FGF-basic. Once secreted, FGF-BP-1 can bind FGFs in a reversible manner to mobilize them from inactive storage on heparan sulfate proteoglycans in the extracellular matrix, and deliver them to high affinity receptors on the cell surface where they can exert biological function, all the while protecting against proteolytic degradation. Expressed within the squamous epithelium, FGF-BP-1 functions synergistically with FGFs as a mitogen for keratinocytes and an antagonist for angiogenesis under normal physiological conditions and instances of tissue repair, while also acting as an angiogenic switch for the malignant progression of epithelial cells. First discovered at elevated levels within A431 human epidermoid carcinoma cells, FGF-BP-1 is also expressed at elevated levels in many squamous cell carcinomas and tumors where it has been shown to be a rate-determining factor, interacting with the heparan sulfate proteoglycan perlecan to potentiate neovascularization of tumor masses. Recombinant Human FGF-BP-1 expressed in E. coli is a 24.0 kDa protein containing 212 amino acid residues.

Catalog Number: (76303-590)

Supplier: Peprotech

Description: The three mammalian isoforms of TGF-beta, TGF-beta1, beta2, and beta3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-beta isoform from a latent complex involves proteolytic processing of the complex and/or induction of conformational changes by proteins such as thrombospondin-1. The physiological role of TGF-beta3 is still unknown, but its expression pattern suggests a role in the regulation of certain development processes. Recombinant Human TGF-beta3 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.

Supplier: Peprotech

Description: Programmed cell death protein 1 (PD-1), or CD279, is a type I inhibitory transmembrane receptor of the CD28 receptor family that, along with its B7 family ligands, programmed death ligand 1 (PD-L1) and programmed death ligand 2 (PD-L2), belongs to the immunoglobulin superfamily. While other CD28 family members are expressed predominantly in T cells, PD-1 is widely expressed and found in multiple lymphocytes including T cells, B cells, myeloid, and NKT cells upon activation. PD-1 is a negative regulator of immune response, and is referred to as an inhibitory immune checkpoint molecule. Ligation with PD-L1 or PD-L2 results in inhibited activation, proliferation, and cytokine secretion (e.g. IFN-gamma, IL-10) in T cells, ultimately dampening immune response. Despite the strong homology between PD-L1 and PD-L2, each ligand appears to display distinct lymphokine expression patterns and potency. Blockage of PD-1 ligation by monoclonal antibodies has been proven to be an effective anti-tumor treatment by allowing the immune response to remain active and attack the tumorigenic cells that otherwise would have escaped detection. PD-1 and its ligands have been implicated in numerous autoimmune diseases, inflammatory liver disease and cancers. The naturally occurring human PD-1 monomer consists of a 150 amino acid extracellular domain, a 21 amino acid transmembrane domain, and a 97 amino acid cytoplasmic domain. PeproTech's CHO cell-derived Recombinant Human PD-1 Fc is a glycosylated, disulfide-linked homodimer of 501 amino acid residues whose monomer consists of the 268-amino-acid length mature PD-1 sequence fused to the 231-amino-acid length Fc portion of human IgG1 by two glycines. The calculated molecular weight of monomeric CHO cell-derived Recombinant Human PD-1 Fc is 55.3 kDa, however, due to glycosylation, it migrates at an apparent molecular weight of approximately 180-200 kDa by SDS-PAGE analysis under non-reducing conditions.

Supplier: Peprotech

Description: Vitronectin is a secreted glycoprotein that is synthesized in the liver. It circulates primarily in monomeric form, but can undergo conformational change to a structure that forms disulfide-linked multimers. The multimeric vitronectin can efficiently bind to, and incorporate into, the extracellular matrix. Within the matrix, vitronectin can support cell adhesion through binding to various integrins and other proteoglycans. Additionally, recombinant vitronectin can function as a chemically defined matrix component in human embryonic stem cell renewal media. Recombinant Human Vitronectin is a 459 amino acid, single-chain, monomeric protein, which migrates at an apparent molecular weight of 75 kDa by SDS-PAGE under reducing conditions. The calculated molecular weight of Recombinant Human Vitronectin is 52.2 kDa. Manufactured using all Animal-Free reagents.

Supplier: Brandtech

Description: <p><span style="color:black">Powerful and popular oil-free diaphragm vacuum pumps are suitable for a wide variety of laboratory applications such as rotary evaporation, centrifugal concentration, gel drying, vacuum filtration, solid phase extraction, and degassing procedures.</span></p>

New Product

Supplier: Peprotech

Description: The IL-1 family is comprised of 11 structurally related ligands, including recently re-named IL-36 α (IL-1F6), β (IL-1F8) and γ (IL-1F9). IL-36γ is highly expressed in psoriatic plaques and in tissues containing epithelial cells. IL-36γ signals through the IL-1Rrp2 (IL-1R6) receptor, which is primarily expressed on certain dendritic cells. The interaction of the IL-1Rrp2 receptor with IL-36 ligands induces dendritic cell maturation and activation. IL-36γ also functions as an agonist of NF-κB, and can stimulate the inflammatory response in bronchial epithelial cells. Recombinant Human IL-36γ is a 17.0 kDa protein containing 152 amino acid residues. Manufactured using all Animal-Free reagents.

Supplier: Peprotech

Description: PDGFs are disulfide-linked dimers consisting of two 12.0-13.5 kDa polypeptide chains, designated PDGF-A and PDGF-B chains. The three naturally occurring PDGFs, PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types, including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGFs are stored in platelet α-granules, and are released upon platelet activation. The PDGFs are involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGFs have been identified and named PDGFR-α and PDGFR-β. PDGFR-α is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-β interacts with only PDGF-BB and PDGF-AB. Recombinant Human PDGF-AB is a 26.4 kDa disulfide-linked dimer, consisting of one α chain and one β chain (234 total amino acids).

Supplier: Peprotech

Description: FGF-basic is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-basic is a non-glycosylated, heparin-binding growth factor that is expressed in the brain, pituitary, kidney, retina, bone, testis, adrenal gland, liver, monocytes, epithelial cells and endothelial cells. FGF-basic signals through FGFR 1b, 1c, 2c, 3c and 4. Recombinant Rat FGF-basic is a 16.3 kDa protein consisting of 145 amino acid residues.

Catalog Number: (CACB354249)

Supplier: Corning

Description: Collagen I is found in most tissues and organs, but is most plentiful in dermis, tendon, and bone. Used as a thin coating in cell and tissue culture, it is often used to enhance cell attachment and proliferation. When applied as a gel it can be used to promote expression of cell-specific morphology and function. Collagen I is commonly used to culture endothelial cells, hepatocytes, muscle cells, and a variety of other cell types. The HC formulation of rat tail collagen I is used for three dimensional applications requiring a sturdy gel that provides a maximal 3D support matrix (guidelines are included with product).

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