"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. Recombinant Human BD-3 is a 5.1 kDa protein containing 45 amino acid residues.

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.

Supplier: Peprotech

TRAIL/Apo2L is a cytotoxic protein, which activates rapid apoptosis in tumor cells, but not in normal cells. TRAIL-induced apoptosis is achieved through binding to two death-signaling receptors, DR4 and DR5. These receptors belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain," which activates the cell's apoptotic machinery. The full length human TRAIL/Apo2L is a 281 amino acid protein, consisting of a 17 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 243 amino acid extracellular domain. Recombinant Human sTRAIL/Apo2L is a 168 amino acid polypeptide (19.6 kDa), consisting of the TNF-homologous portion of the extracellular domain of the full length TRAIL/Apo2L protein.

Supplier: Peprotech

TWEAK belongs to the TNF family of ligands, and signals through TWEAKR, also known as TNFRSF12A. TWEAK is expressed in a variety of tissues, including the adult heart, pancreas, skeletal muscle, small intestine, spleen and peripheral blood lymphocytes. TWEAK has the ability to induce NF-κB activation and chemokine secretion, and to exert an apoptotic activity in certain cells, such as HT-29 human adenocarcinoma cells when cultured in the presence of IFN-γ. TWEAK also promotes proliferation and migration of endothelial cells. The human TWEAK gene encodes for a 249 amino acid type II transmembrane protein, which contains a 21 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 207 amino acid extracellular domain. Recombinant Human TWEAK is a soluble 17.0 kDa polypeptide (154 amino acid residues) comprising the TNF-homologous region of TWEAK, and is generated by proteolytic processing of the full length membrane-anchored TWEAK protein.

Supplier: Peprotech

TNFRI belongs to the TNFR superfamily of transmembrane proteins, and is expressed in most cell types. Binding of either TNF-α or TNF-β to TNFRI initiates a signal transduction pathway that results in the activation of the transduction factor NF-κB, whose target genes are involved in the regulation of inflammatory responses, and, in certain cells induce apoptosis. Soluble TNF Receptor I (sTNFRI) is capable of inhibiting TNF-α and TNF-β activities by acting as a decoy receptor that serves as a sink for the TNF ligands. The human TNFRI gene encodes for a 455 amino acid type I transmembrane protein, which contains a 21 amino acid signal sequence, a 190 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 221 amino acid cytoplasmic domain. Recombinant Human sTNF Receptor Type I is an 18.3 kDa protein (162 amino acid residues) comprising the cysteine-rich, ligand-binding portion of the extracellular domain of the TNFRI protein.

Supplier: Peprotech

TWEAKR belongs to the TNF family of transmembrane proteins, and contains a cytoplasmic "death domain," which can activate a cell's apoptotic machinery. It is expressed in the spleen, thymus, peripheral blood lymphocytes, colon, and small intestine. Signal transduction by TWEAKR can be activated by either membrane-anchored or soluble TWEAK. Recombinant Human TWEAK Receptor is a 53 amino acid polypeptide (5.6 kDa) comprising the entire extracellular domain of the full-length TWEAKR protein.

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AITRL, a member of the TNF superfamily, is expressed in endothelial cells, and signals through the AITR receptor. AITRL regulates T-cell proliferation and survival, and effectuates the interaction between T lymphocytes and endothelial cells. The AITRL gene codes for a type II transmembrane protein comprised of 177 amino acids, including a 28 amino acid cytoplasmic region, a 21 amino acid transmembrane domain and a 128 amino acid extracellular domain. Recombinant Human AITRL is a 14.4 kDa protein, containing 127 amino acid residues corresponding to the extracellular domain of AITRL.

Supplier: Peprotech

TL-1A belongs to the TNF superfamily of ligands. It is expressed predominantly in endothelial cells, and to a lesser extent in the placenta, lung, kidney, skeletal muscle, pancreas, small intestine and colon. TL-1A inhibits endothelial cell proliferation and angiogenesis, and has been shown to induce NF-κB activation, caspase activity, and apoptosis in responding cell lines. TL-1A interacts with TNFRSF25/DR3 receptor, but can also bind to a decoy receptor TNFRSF21/DR6. Recombinant Human TL-1A is a 22.0 kDa polypeptide of 194 amino acid residues.

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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HVEM belongs to the TNF Receptor superfamily of transmembrane proteins, and plays a role in the activation of T-cells and other lymphocytes. It is expressed in various cells and tissues, including spleen, thymus, lung, macrophages, and T-cells. HVEM activation induces a signaling cascade that results in the induction of transcription factors NF-κB and AP-1. LIGHT (TNFSF14) and TNF-β (TNFSF1) function as the ligands for HVEM, which can also bind specifically to herpes simplex virus glycoprotein D. Soluble HVEM can act as a “receptor decoy” resulting in inhibition of the activity of the HVEM ligands, LIGHT and TNF-β. Recombinant Human HVEM-Fc is a 376 amino acid fusion protein that contains an N-terminal domain corresponding to the extracellular region of HVEM, and a C-terminal domain corresponding to residues 102 to 330 of human IgG1. The calculated molecular weight of Recombinant Human HVEM-Fc is 41.4 kDa.

Supplier: Peprotech

OX40L, a member of the TNF superfamily of structurally related proteins, exists primarily as a type II membrane-bound, non-covalently linked, homotrimeric protein. It is expressed on antigen-presenting cells (APCs), such as dendritic cells and activated B-cells, as well as on various other cells such as vascular endothelial cells, mast cells, and natural killer cells. OX40L signals specifically through the OX40 receptor, which is expressed predominantly on CD4+ T cells, but also on certain activated CD8+ T cells. OX40/OX40L functions as a costimulatory signal, which is required for a productive interaction between antigen-presenting cells and their target T-cells. It enhances cell proliferation and survival, and increases expression of RANTES, IL-2, IL-3, and IFNγ. OX40/OX40L signaling plays an important role in immuno-regulatory communication, enabling the immune system to distinguish between “friend vs. foe” during activation; a mechanism typically termed immuno-tolerance. Recombinant Human sOX40 Ligand is a glycosylated 133 amino acid protein corresponding to the extracellular TNF homologous domain of the full length transmembrane protein. It migrates with an apparent molecular mass of 15.5 – 25.0 kDa on SDS-PAGE. Recombinant Human sOX40 Ligand has a calculated, theoretical molecular weight of 15.4 kDa.

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The Semphorins are a large family of phylogenetically conserved proteins that play a pivotal role in maintaining homeostasis in the immune system. Twenty members of this family have been identified and categorized into eight subclasses based on sequence similarity and distinctive structural features. CD100, also known as Sema4D, is a 150 kDa transmembrane class IV semaphorin. Studies have shown that CD100 can induce monocyte migration, T-cell activation, and B-cell survival, as well as T/B cell and T/DC “cooperation”. The CD100 precursor contains 862 amino acids, including a 21 a.a. signal sequence, a 713 a.a. extracellular domain, a 21 a.a. transmembrane sequence, and a 107 a.a. cytoplasmic region. The extracellular sequence contains several structural features, including a 479 a.a. “sema” domain, a 79 a.a. Ig-like sequence, and a 52 a.a. “Plexin-type repeat”. Recombinant Human sCD100 is a 78.9 kDa protein comprising the extracellular domain of CD100 (711 amino acids). SDS-PAGE analysis run under non-reducing conditions shows a mixture of disulfide linked dimer and monomer.

Supplier: Peprotech

IFN-γ is an acid-labile interferon produced by CD4 and CD8 T lymphocytes, as well as activated NK cells. IFN-γ receptors are present in most immune cells, which respond to IFN-γ signaling by increasing the surface expression of class I MHC proteins. This promotes the presentation of antigen to T-helper (CD4+) cells. IFN-γ signaling in antigen-presenting, cells and antigen-recognizing B and T lymphocytes, regulates the antigen-specific phases of the immune response. Additionally, IFN-γ stimulates a number of lymphoid cell functions, including the anti-microbial and anti-tumor responses of macrophages, NK cells, and neutrophils. Human IFN-γ is species-specific and is biologically active only in human and primate cells. Recombinant Murine IFN-γ is a 15.6 kDa protein containing 134 amino acid residues.

Supplier: Peprotech

EGF is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through a receptor known as c-erbB, which is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). Recombinant Murine EGF is a 6.0 kDa globular protein containing 53 amino acid residues, including 3 intramolecular disulfide bonds.

Supplier: Peprotech

RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic cells. These dendritic cells then stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, promote the survival of RANK + T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells, including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant Murine sRANK Ligand is a 19.4 kDa polypeptide comprising the TNF-homologous region of RANKL (174 amino acid residues).

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. Recombinant Murine LIGHT is a 20.1 kDa protein containing 183 amino acid residues, comprising the TNF-homologous region of the LIGHT extracellular domain.