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1636 results for "Peprotech"

1636 Results for: "Peprotech"

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Mouse Recombinant IL-7 (from E. coli)

Supplier: Peprotech

IL-7 is a hematopoietic growth factor that primarily affects early B and T cells. Produced by thymic stromal cells, spleen cells and keratinocytes, IL-7 can also co-stimulate the proliferation of mature T cells in combination with other factors, such as ConA and IL-2. Human and murine IL-7 is cross-species reactive. Recombinant Murine IL-7 is a 15.0 kDa protein containing 130 amino acid residues.

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Rat Recombinant Prolactin (from E. coli)

Supplier: Peprotech

Prolactin is a neuroendocrine hormone secreted by the pituitary gland. Its primary function is to promote and maintain lactation during pregnancy and suckling. In addition, prolactin plays an immunoegulatory role by stimulating the activities of ornithine decarboxylase and protein kinase C, which are important for the proliferation, differentiation, and function of lymphocytes. Recombinant Rat Prolactin is a 22.6 kDa globular protein containing 198 amino acid residues

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Human Recombinant sFas (from E. coli)

Supplier: Peprotech

Fas and Fas Ligand (FasL) belong to the TNF superfamily, and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas triggers apoptosis in Fas-bearing cells. The mechanism of apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD, followed by processing of the pro-enzyme into active forms. These active caspases then cleave various cellular substrates, leading to the eventual cell death. sFasR is capable of inhibiting FasL-induced apoptosis by acting as a decoy receptor that serves as a sink for FasL. The full length Fas (receptor) is a 319 amino acid type I transmembrane protein, which contains a 157 amino acid extracellular domain, a 17 amino acid transmembrane domain, and a 145 amino acid cytoplasmic domain. Recombinant Human sFas Receptor is a 157 amino acid polypeptide (17.6 kDa) corresponding to the TNFR-homologous cysteine-rich extracellular Fas domain.

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Mouse Recombinant CTACK (from E. coli)

Supplier: Peprotech

CTACK is a keratinocyte-derived CC chemokine which signals through the CCR10 receptor. Both CTACK and CCR10 are expressed in normal and irritated epithelial cells. CTACK selectively attracts CLA+ T-cells and directs them into the skin. CTACK contains the four highly conserved cysteine residues present in most CC chemokines. The mature protein contains 88 amino acid residues. Recombinant Murine CTACK (CCL27) is a 10.9 kDa protein containing 95 amino acid residues.

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Rat Recombinant Carboxypeptidase-B (from E. coli)

Supplier: Peprotech

CARBOXYPEPTIDASE-B Recombinant, Purity: Greater than 95% by SDS-PAGE gel and HPLC, Source: E.coli, Reactivity: Rat, Molecular mass of 35.1 kDa protein consisting of 307 amino acids, Synonyms: Cpb1, Size: 50 uG

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Mouse Recombinant Cardiotrophin-1 (from E. coli)

Supplier: Peprotech

CARDIOTROPHIN-1 Recombinant, Purity: Greater than 98% by SDS-PAGE gel and HPLC, Source: E.coli, Reactivity: Murine, Molecular mass of 21.3 kDa protein consisting of 202 amino acid residues, Synonyms: CT-1, Size: 50 uG

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Human Recombinant PDGF-BB (from E. coli)

Supplier: Peprotech

Animal-Free Human PDGF-BB, Recombinat, Purity: Greater than 98% by SDS-PAGE gel and HPLC analyses, Host: E.coli, Synonyms: Platelet-Derived Growth Factor-BB, Glioma-derived growth factor (GDGF), Osteosarcoma-derived Growth Factor (ODGF), Size: 50UG

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Human Recombinant TGF-alpha (from E. coli)

Supplier: Peprotech

TGF-α is an EGF-related polypeptide growth factor that signals through the EGF receptor, and stimulates the proliferation of a wide range of epidermal and epithelial cells. It is produced by monocytes, keratinocytes, and various tumor cells. TGF-α induces anchorage-independent transformation in cultured cells. Human, murine and rat TGF-α are cross-species reactive. Recombinant Human TGF-α is a 50 amino acid polypeptide (5.5 kDa), which shares approximately 40% sequence homology with EGF, including 6 conserved cysteine residues, which form 3 intramolecular disulfide bonds.

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Human Recombinant GASP-1 (from CHO Cells)

Supplier: Peprotech

Growth and differentiation factor-associated serum protein-1 (GASP-1) is a secreted inhibitory TGF-β binding protein that contains multiple protease inhibitor structural domains. It is expressed primarily in the ovary, testis, and brain, and can act as a potent soluble inhibitor of myostatin and GDF-11, but not Activin A. The GASP-1 gene encodes a 571 amino acid protein that contains a 29 amino acid secretion signal sequence, and multiple identifiable structural features, including a WAP domain, a follistatin/Kazal domain, an immunoglobulin domain, two tandem Kunitz domains, and a netrin domain. Recombinant Human GASP-1 is a 542 amino acid protein that migrates at an apparent molecular weight of approximately 55-66 kDa by SDS-PAGE analysis under non-reducing conditions. The calculated molecular weight of Recombinant Human GASP-1 is 59.9 kDa.

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Human Recombinant GDNF (from E. coli)

Supplier: Peprotech

GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRα (α1-α4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson’s disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional human GDNF ligand is a disulfide-linked homodimer consisting of two 15 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring formation known as the cysteine knot configuration. The calculated molecular weight of Recombinant Human GDNF is 30.4 kDa.

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Human Recombinant Growth (from E. coli)

Supplier: Peprotech

Growth Hormone (GH), also known as somatotropin, is a pleiotropic cytokine of the hematopoietic growth factor superfamily, which encompasses most cytokines, hematopoietic growth factors, and related receptors, and includes the related growth hormone receptor, prolactin, placental lactogens, proliferins, and somatolactin (SST). GH is primarily recognized for its anabolic role in stimulating the growth and differentiation of muscle, bone, and cartilage. A number of other functions, including immunomodulatory actions, are also attributed to GH, due in part to the pervasive distribution of its receptors, and the indirect effects associated with GH-stimulated production of insulin-like growth factors (IGFs). Occurring predominantly in the somatotropes of the anterior pituitary, whereupon it is stored in secretory granules, production of GH has also been noted in many other tissues, including those of the hematopoietic system. The production and pulsatile release of circulating GH is very tightly regulated by both negative and positive feedback regulations of pituitary and hypothalamic hormones, such as Pituitary-specific Positive Transcription Factor 1 (POU1F1), Growth Hormone Releasing Hormone (GHRH), and somatostatin (SRIF). Deficient production of GH is associated with dwarfism and reduction of lean body mass, while overproduction is associated with acromegaly and gigantism, as well as breast tumor growth. Recombinant Human Growth Hormone is a 22.3 kDa, single, non-glycosylated polypeptide chain containing 192 amino acid residues.

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Mouse Recombinant PDGF-BB (from E. coli)

Supplier: Peprotech

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 a 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 Murine PDGF-BB is a 24.4 kDa disulfide-linked homodimer of two β chains (218 total amino acids).

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Human Recombinant IFN-?1 (from E. coli)

Supplier: Peprotech

IFN λ1, 2, and 3 (also known as IL-29, IL-28A and IL-28B respectively) are distantly related to the IL-10 family and the interferons. All three IFN-lambdas use a distinct receptor system composed of an IFN-λR1 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 Human IFN-λ1 is a 19.8 kDa protein containing 178 amino acid residues.

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Human Recombinant sTRAIL (from E. coli)

Supplier: Peprotech

TRAIL Receptor-1/DR4 and TRAIL Receptor-2/DR5 belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain," which can activate the cell's apoptotic machinery. These receptors are activated by binding to either membrane-anchored or soluble TRAIL/Apo2L. The DR4 and DR5 receptors are both produced as type I transmembrane proteins, which contain an extracellular domain, a transmembrane domain, and a cytoplasmic domain. The recombinant soluble forms of DR4 and DR5 consist of the TNFR-homologous, cysteine-rich portion of their respective extracellular domains. Recombinant Human sTRAIL Receptor-1 is a 22.7 kDa protein (215 amino acid residues) consisting of the TNFR homologous, cysteine-rich portion of the extracellular domain.

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Anti-TPO Rabbit Polyclonal Antibody

Supplier: Peprotech

Produced from sera of rabbits immunized with highly pure Recombinant Human TPO. Anti­Human TPO­specific antibody was purified by affinity chromatography employing an immobilized Human TPO matrix.

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Human GM-CSF Standard ABTS ELISA Development Kit, PeproTech, Inc.

Supplier: Peprotech

PeproTech's Human GM-CSF ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant human GM-CSF in a sandwich ELISA format.

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Human Recombinant VEGF (from E. coli)

Supplier: Peprotech

VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. Substantial evidence implicates VEGF in the induction of tumor metastasis and intra-ocular neovascular syndromes. VEGF signals through three receptors; fms- like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Recombinant Human VEGF

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Human Recombinant sFas (from CHO Cells)

Supplier: Peprotech

Fas Ligand (FasL) is a member of the TNF superfamily that is expressed on the cell surface of activated T cells. Binding of FasL to Fas Receptor triggers apoptosis in Fas-bearing cells. FasL has the ability to kill T cells and activated B cells, which leads to down-regulation of the immune response. The mechanism of Fas-induced apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD, followed by processing of the pro-enzyme into active forms. These active caspases then cleave various cellular substrates, leading to the eventual cell death. Both human and murine sFasL are fully active on human and murine cells. Recombinant Human sFas Ligand is a 17.9 kDa protein comprising the TNF-homologous region of FasL and contains an 8-residue N-terminal His-Tag.

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Human Recombinant LIGHT (from Hi-5 Insect Cells)

Supplier: Peprotech

LIGHT belongs to the TNF family of ligands, and can signal through the herpes virus entry mediator type A receptor (HVEM, TNFRSF14), LTβR, or bind to a decoy receptor, DcR3. It is expressed in splenocytes, activated PBL, CD8+ tumor infiltrating lymphocytes, granulocytes, and monocytes. LIGHT has the ability to active NF-κB, to co-stimulate the activation of lymphocytes and to induce apoptosis in certain human tumor cells. The human LIGHT gene encodes for a 240 amino acid type II transmembrane protein containing a 37 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 182 amino acid extracellular domain. Recombinant Human LIGHT has a calculated mass of 19.3 kDa, containing 177 amino acid residues. Due to glycosylation, LIGHT migrates between 20.0-22.5 kDa by SDS-PAGE under non-reducing conditions.

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Mouse Recombinant Leptin (from E. coli)

Supplier: Peprotech

Encoded by the ob (obese) gene, Leptin is an adipose-derived cytokine that suppresses appetite and increases thermogenesis. Leptin exerts its anorectic effect via signaling through a hypothalamic receptor termed OB-R. Leptin has been shown to reduce body weight, food consumption, and plasma glucose levels in various Recombinant Murine Leptin is a 16.2 kDa protein containing 147 amino acid residues.

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Human Recombinant IL-22 (from E. coli)

Supplier: Peprotech

IL-22 Recombinant, Purity: > 98% by SDS-PAGE gel and HPLC, Source: E.coli, Reactivity: Human, Molecular mass of 33.6 kDa, non-disulfide-linked, homodimeric protein consisting of two 147 aa polypeptide chains, Synonyms: Interleukin-22, IL-TIF, Size: 50 uG

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Human Recombinant IL-7 (from E. coli)

Supplier: Peprotech

Animal-Free Human IL-7, Recombinat, Purity: Greater than 98% by SDS-PAGE gel and HPLC analyses, Host: E.coli, hematopoietic growth factor that primarily affects early B and T cells, Synonyms: Lymphopoietin 1(LP-1), pre-B cell factor, Size: 50UG

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Human Recombinant sCD23 (from E. coli)

Supplier: Peprotech

CD23, the low affinity receptor for IgE, belongs to the C-type lectin structural family and plays a role in the regulation of IgE synthesis and IgE mediated activities. It is found both as a transmembrane receptor protein and in a soluble form, which is generated by proteolytic cleavage of membrane-bound CD23. The predominant soluble form of CD23 (sCD23) consists of 172 amino acids corresponding to the extracellular domain of the full length precursor. sCD23, in addition to binding IgE, also exerts a number of IgE-independent activities, such as promoting the activation and differentiation of B-cells and stimulating the release of pro-inflammatory cytokines from monocytes. Recombinant Human sCD23 is a 19.2 kDa non-glycosylated protein containing 172 amino-acid residues.

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Human Recombinant IFN-omega (from E. coli)

Supplier: Peprotech

IFN-ω is a type I interferon that can be induced by virus-infected leukocytes. Members of the type I interferon family, which includes IFN-α, IFN-β, and IFN-ω, signal through the IFNAR-1/IFNAR-2 receptor complex, and exert antiviral and antiproliferative activities. IFN-ω exhibits about 75% sequence homology with IFN-α, and contains two conserved disulfide bonds that are necessary for full biological activity. Recombinant Human IFN-ω is a 19.9 kDa protein consisting of 172 amino acid residues.

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Human Recombinant p16-INK4a (from E. coli)

Supplier: Peprotech

p16-INK4a is a nuclear protein that regulates the cell cycle by inhibiting cyclin-dependent kinase-4 (CDK4) and CDK6. p16-INK4a inhibits CDK activity by binding to the CDK molecules in a manner that interferes with their ability to interact with cyclin D. This activity has the effect of suppressing tumor formation and growth, and of inducing replicative senescence in various normal cells, including stem cells. The expression of p16-INK4a steadily increases with age, and tends to accumulate in stem cell compartments. The deletion, rearrangement, or mutation of the p16-INK4a gene is frequently found in melanomas, as well as in certain other types of cancer. Recombinant Human p16-INK4a is a 16.5 kDa protein containing 156 amino acid residues.

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Human Recombinant MIP-1beta (from E. coli)

Supplier: Peprotech

Both MIP-1α and MIP-1β are structurally and functionally related CC chemokines. They participate in host response to invading bacterial, viral, parasite and fungal pathogens, by regulating the trafficking, and activation state, of selected subgroups of inflammatory cells (e.g. macrophages, lymphocytes and NK cells). While both MIP-1α and MIP-1β exert similar effects on monocytes, their effect on lymphocytes differ; with MIP-1α selectively attracting CD8+ lymphocytes, and MIP-1β selectively attracting CD4+ lymphocytes. Additionally, MIP-1α and MIP-1β have also been shown to be potent chemoattractants for B cells, eosinophils and dendritic cells. Both human and murine MIP-1α and MIP-1β are active on human and murine hematopoietic cells. Recombinant Human MIP-1β (CCL4) is a 7.6 kDa protein containing 69 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.

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Human Recombinant IGF-I (from E. coli)

Supplier: Peprotech

The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro . IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant Human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. The calculated molecular weight of Recombinant Human IGF-I is 7.6 kDa.

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Human Recombinant KLF4-TAT (from HEK293 Cells)

Supplier: Peprotech

KLF4 is a member of the Kruppel-like factor (KLF) family of zinc finger transcription factors. Members of this family share 3 contiguous C2H2-type zinc fingers at the carboxyl terminus that comprise the DNA-binding domain. KLF4 is highly expressed in skin and gut epithelial tissues, but is also found in various other cells and tissues, including vascular endothelial cells, lymphocytes, lung, and testis. It is an important regulator of the cell cycle, transcription, and cell differentiation. Together with Sox2, Oct4, and cMyc, KLF4 can induce the reprogramming of primary human fibroblasts to a pluripotent state. KLF4 and other transcription factors can be introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing transcription factors into primary, as well as transformed, cells. Recombinant Human KLF4-TAT is a 483 amino acid protein, including a 13-residue C-terminal TAT peptide, with a calculated molecular weight of 51.7 kDa. PeproTech’s Recombinant Human KLF4-TAT is a mixture of the expected sequence beginning at Met1 and a truncated isoform beginning at Tyr54. Due to post-translational modifications, SDS-PAGE gel shows bands at approximately 72 and 66kDa, under reduced conditions.

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Human Recombinant MIP1A (from E. coli)

Supplier: Peprotech

Both MIP-1α and MIP-1β are structurally and functionally related CC chemokines. They participate in host response to invading bacterial, viral, parasite and fungal pathogens, by regulating the trafficking, and activation state, of selected subgroups of inflammatory cells (e.g. macrophages, lymphocytes and NK cells). While both MIP-1α and MIP-1β exert similar effects on monocytes, their effect on lymphocytes differ; with MIP-1α selectively attracting CD8+ lymphocytes, and MIP-1β selectively attracting CD4+ lymphocytes. Additionally, MIP-1α and MIP-1β have also been shown to be potent chemoattractants for B cells, eosinophils and dendritic cells. Both human and murine MIP-1α and MIP-1β are active on human and murine hematopoietic cells. Recombinant Human MIP-1α is a 7.8 kDa protein containing 70 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines. Manufactured using all Animal-Free reagents.

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Human Neuroserpin Standard ABTS ELISA Development Kit, PeproTech, Inc.

Supplier: Peprotech

PeproTech's Human Neuroserpin ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant human Neuroserpin in a sandwich ELISA format.

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