1636 Results for: "Peprotech"

Supplier: Peprotech

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. BD-4 is expressed in the testes, stomach, uterus, neutrophils, thyroid, lungs and kidneys. In addition to its direct antimicrobial activities, BD-4 is chemoattractant towards human blood monocytes. Recombinant Human BD-4 is a 6.0 kDa protein containing 50 amino acid residues.

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Angiopoietin-1 (ANG-1) is a secreted ligand for Tie-2, a tyrosine-kinase receptor expressed primarily on vascular endothelial cells and early hematopoietic cells. ANG-1/Tie-2 signaling promotes angiogenesis during the development, remodeling, and repair of the vascular system. Transgenic mice lacking expression of either ANG-1 or Tie-2 fail to develop a fully functional cardiovascular system and die before birth. Postnatally, the angiogenic activity of ANG-1/Tie-2 is required during normal tissue repair and remodeling of the female endometrium in the menstrual cycle. ANG-1/Tie-2 signaling appears to be regulated by Angiopoietin-2 (ANG-2), a natural antagonist for Tie-2 that exerts its effects through an internal autocrine loop mechanism. In addition to suppressing endothelial cell activation by inhibiting the expression of adhesion and inflammatory molecules, Ang-1 enhances endothelial cell survival and capillary morphogenesis, and lessens capillary permeability. As such, ANG-1 has potential to become an effective therapeutic agent for treating various endothelium disorders, including several severe human pulmonary diseases. The efficacy of cell-based Ang-1 gene therapy for acute lung injury (ALI) has recently been studied in a rat model of ALI. The results of this study show that such therapy can markedly improve lung condition and suggest that Ang-1 therapy may represent a potential new strategy for the treatment and/or prevention of acute respiratory distress injury (ARDI), a significant cause of morbidity and mortality in critically ill patients. Recombinant Human ANG-1, derived from

Supplier: Peprotech

Serum amyloid A proteins (SAA) represents a family of apolipoproteins that circulates in association with high-density lipoproteins (HDL). The level of Apo-SAA, normally 1-5 μg/ml in plasma, increases 500-1000 fold within 24 hours of an inflammatory stimulus and, under these conditions, is the most abundant HDL apolipoprotein. The human SAA gene codes for a 122 amino acid nonglycosylated polypeptide, which contains an 18 amino acid N-terminal sequence. Recombinant Human Apo-SAA1 is an 11.7 kDa protein containing 105 amino acid residues.

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IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP6, which specifically inhibits IGF-II actions, is produced by bone cells and is the major IGF-BP present in cerebrospinal fluid. IGF-BP6 has been shown to inhibit IGF-II-dependent cancers such as neuroblastoma, colon cancer and rhabdomyosarcoma. Recombinant Human IGF-BP6 has a calculated mass of 22.3 kDa and consists of 213 amino acid residues, including the IGF-BP domain and thyroglobulin type-I domain. Recombinant Human IGF-BP6 migrates at an apparent molecular weight of approximately 23.0-30.0 kDa by SDS-PAGE analysis under non-reducing conditions.

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Complement 5a (C5a) is an enzymatically generated glycoprotein belonging to the anaphylatoxin family of structurally and functionally related proteins. Generated upon the activation of the complement system, C5a, together with C4a, C3a, and the membrane attack complex (C5b-9), functions as a central player in host defense by inducing smooth muscle cell contraction, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes through cell degranulation. In addition to acting as a direct mediator of localized inflammatory response, C5a also initiates both the synthesis and release of IL-8 from monocytes and bronchial epithelial cells, stimulates the proliferation of neurons and hepatocytes, and functions as a potent chemoattractant. Where C5a deficiency, a rare defect of the complement pathway caused by the mutation of the C5a gene, is associated with susceptibility to severe infections, excessive C5a activation has been linked to liver fibrosis, sepsis, adult respiratory distress syndrome, rheumatoid arthritis, Alzheimer’s disease, and ischemic heart disease. Human C5a shares 60% and 54% sequence identity to mouse and rat C5a, respectively. The human C5 gene encodes a 1,676 amino acid glycoprotein that is comprised of a disulfide-linked C5 alpha and a C5 beta chain, the former of which contains the active, 74 amino acid C5a anaphylatoxin chain. Recombinant Human C5a is an 8.28 kDa glycoprotein containing the 74 amino acid residues of the C5a anaphylatoxin chain.

Supplier: Peprotech

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Furin is a calcium-dependent serine endoprotease that processes numerous proproteins of different secretory pathways into their mature forms by cleaving at the carboxyl side of the recognition sequence, R-Xaa-(K/R)-R, where Xaa can be any amino acid. Recombinant Human Furin is a 63.9 kDa protein, corresponding to residues 131 through 715 of the Furin precursor, plus a C-terminal His-tag.

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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 Human FGF-basic is a 17.2 kDa protein consisting of 154 amino acid residues.

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APRIL, a member of the TNF superfamily, is expressed in monocytes, macrophages, certain transformed cell lines, certain cancers of the colon, and lymphoid tissues. APRIL, along with another TNF family member, BAFF, competes for two receptors, TACI and BCMA. APRIL has the ability to stimulate proliferation of various tumor cell lines, including Jurkat T cells and MCF-7 carcinoma cells. Like BAFF, APRIL also stimulates the proliferation of B and T cells. The human APRIL gene codes for at least four alternatively spliced transcriptional variants, which give rise to different isoforms of the APRIL precursor protein. All isoforms can be cleaved by the protease, furin, to release a soluble C-terminal fragment, which comprises the TNF-like receptor binding of the APRIL precursor. Recombinant Murine APRIL is a soluble 21.9 kDa protein, consisting of 192 amino acid residues.

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TNF-β is a potent mediator of inflammatory and immune responses. It belongs to the TNF family of ligands, and signals through TNFR1 and TNFR2. TNF-β is produced by activated T and B lymphocytes, and has similar activities to TNF-α. Like TNF-α, TNF-β is involved in the regulation of various biological processes, including cell proliferation, differentiation, apoptosis, lipid metabolism, coagulation, and neurotransmission. TNF-β is secreted as a soluble polypeptide, but can form heterotrimers with lymphotoxin-β, which effectively anchors the TNF-β to the cell surface. TNF-β is cytotoxic to a wide range of tumor cells. Recombinant Human TNF-β is a secreted 172 amino acid protein (18.6 kDa) which forms an active non-disulfide-linked homotrimer structure in solution.

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Animal-Free Human IL-37 Recombinant Protein, Purity: >95%, Source: E.coli, Biological Activity: By its ability to bind Interleukin-18 Binding Protein isoform a (IL-18 BPa) in functional ELISA, Synonyms: Int

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MDC is a CC chemokine that is produced in B cells, macrophages, monocyte-derived dendritic cells, activated NK cells and CD4 T cells. It signals through the CCR4 receptor. MDC chemoattracts monocytes, dendritic cells and NK cells, and exerts HIV-suppressive activity. The 67 amino acid form of MDC displays reduced chemoattractant activity, but retains HIV-suppressive activity. Recombinant Murine MDC (CCL22) is a 7.8 kDa protein containing 68 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.

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Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to, specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, as they are frequently used in the analysis and production of proteins. Kex-2 cleaves at the carboxyl end of the recognition sequences Arg-Arg/X and Lys-Arg/X. Recombinant Yeast Kex-2 is a 60.4 kDa protease consisting of 558 amino acid residues.

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IL-5 is a hematopoietic growth factor that stimulates the proliferation and activation of eosinophils. Produced by mast cells, T cells, and eosinophils, IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. Elevated levels of IL-5 lead to Eosinophilia, which may result in the induction of asthma and other allergic diseases. Human and murine IL-5 are cross-species reactive. Recombinant Human IL-5 is a 26.5 kDa disulfide-linked homodimeric protein containing two 116 amino acid chains.

Supplier: Peprotech

PeproTech's Rat IFN-γ ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant rat IFN-γ in a sandwich ELISA format.

Supplier: Peprotech

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 Human IL-1α is an 18.0 kDa protein containing 159 amino acid residues.

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

Supplier: Peprotech

PDGF-AB Recombinant, Purity: >98%, SDS-PAGE gel & HPLC, Source: E.coli, Reactivity: Human, Molecular mass of 25.5kDa disulfide-linked dime, Synonyms: Platelet-Derived Growth Factor-AB, Glioma-derived growth factor, Osteosarcoma-derived, Size: 50 uG

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Recombinant HumansCD28 Fc, Purity: Greater than 95% by SDS-PAGE gel and HPLC analyses, Source: CHO cells, Determined by its ability to bind its principal binding partner (B7-1) in a functional ELISA, Synonyms: T-cell-specific surface glycoprotein CD28, Size: 1MG

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MIP-3α is a CC chemokine, expressed in the liver, lymph nodes, appendix, PBL and lungs that can signal through the CCR6 receptor. MIP-3α is chemotactic towards lymphocytes and dendritic cells. Additionally, it promotes the adhesion of memory CD4+ T cells, and inhibits colony formation of bone marrow myeloid immature progenitors. Recombinant Murine MIP-3α (CCL20) is a 7.9 kDa protein containing 70 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.

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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-1α 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 Rat MIP-1β (CCL4) is a 7.8 kDa protein containing 69 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.

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CD22 is a B-lineage restricted 135 kDa glycoprotein whose cell surface expression is limited to resting and activated B lymphocytes. The physiological role of CD22 is still unknown. Targeted disruption of CD22 in mice results in a reduced level of surface IgM on peripheral B cells, suggesting a role for CD22 in limiting antigen receptor signaling. CD22 is a member of the Ig gene superfamily that uniquely binds a sialic acid-dependent ligand. Recombinant Human sCD22 is a soluble 75.0 kDa protein which corresponds to the extracellular domain of CD22.

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OTOR, also called Otoraplin and MIAL, is a secreted cytokine of the MIA/OTOR family. Members of this family, which include MIA, MIA2, and TANGO, share a Src homology-3 (SH3)-like domain. OTOR is predominantly expressed in the cochlea of the inner ear, and, to a lesser extent, in fetal brain tissue and some cartilage tissues. OTOR appears to be involved in early chondrogenesis of the otic capsule, which is required for normal inner ear development and auditory function. Recombinant Human OTOR is a 12.7 kDa globular protein containing 112 amino acid residues.

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CXCL16 is a member of the CXC chemokine family and signals through the CXCR6 receptor. CXCL16 may play a role in attracting lymphocyte subsets during inflammation and may facilitate certain immune responses. The chemokine domain of CXCL16 contains six cysteine residues, including the four highly conserved cysteine residues characteristic of CXC chemokines. The CXCL16 gene codes for a 273 amino acid polypeptide, which includes a 29 amino acid cytoplasmic domain and transmembrane sequence containing approximately 20 amino acids. The extracellular portion of CXCL16 contains a chemokines domain and an extended C-terminal “mucin-like stalk” sequence. The extracellular domain contains 89 amino acid residues (86 a.a. residues for the murine homolog). Recombinant Human CXCL16 is a 10.1 kDa protein containing 89 amino acid residues.

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IL-36RA Recombinant, Purity: >/= 98% by SDS-PAGE gel and HPLC, Source: E.coli, Reactivity: Mouse, Molecular mass of 17 kDa protein containing 154 aa residues, Synonyms: Interleukin-36RA, FIL1 delta, IL-1F5, IL-1HY1, IL-1L1, IL-1ra Homolog 1, Size: 500 uG

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IL-34 Recombinant, Purity: > 95% SDS-PAGE gel & HPLC, Source: HEK293 cells, Reactivity: Human, Molecular mass of 52.5 kDa homodimeric glycoprotein consisting of 460 aa residues, including a C-terminal His-Tag, Synonyms: Interleukin-34, C16orf77, Size: 50 uG

Supplier: Peprotech

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to, specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Carboxypeptidase-B sequentially cleaves C-terminal K and R residues. Recombinant Rat Carboxypeptidase-B is a 35.1 kDa protein consisting of 307 amino acids.

Supplier: Peprotech

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

Supplier: Peprotech

Human FSTL1 Recombinant Protein, Purity: >95% by SDS and HPLC, Source: CHO cells, Biological Activity: Measured by its binding ability in a functional ELISA, Synonyms: Follistatin-like protein 1, FSL1, Follistatin-rel

Supplier: Peprotech

PeproTech's Murine IFN-γ ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant murine IFN-γ in a sandwich ELISA format.

Supplier: Peprotech

Recombinant Murine BD-2, Purity: Greater than 98% by SDS-PAGE gel and HPLC analyses, Source: E.coli, expressed on some leukocytes and at epithelial surfaces, Synonyms: Beta-Defensin 2, DEFB2, DEFB4A, Skin-Antimicrobial Peptide 1, SAP1, Size: 100UG