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Supplier: Peprotech

Description: Produced from sera of goats immunized with highly pure Recombinant Human sCD40 Ligand. Anti­Human sCD40 Ligand­specific antibody was purified by affinity chromatography employing an immobilized Human sCD40 Ligand matrix.

Catalog Number: (10776-422)

Supplier: Peprotech

Description: Produced from sera of goats immunized with highly pure Recombinant Murine IL-18BP. Anti­Murine IL-18BP­specific antibody was purified by affinity chromatography and then biotinylated.

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: Wnt-1 is a secreted protein that signals through the Frizzled family of cell surface receptors, and is required for normal embryonic development. Wnt-1 activation induces a complex signaling cascade that ultimately leads to the increased expression of over fifty genes. An important component of Wnt-1 signaling is the stabilization, and resulting accumulation, of the intracellular signaling protein, β-catenin. Wnt signaling induces and maintains the transformed phenotype, and, in certain embryonic cell lines, supports self-renewal in the absence of significant differentiation. Elevated levels of Wnt proteins are associated with tumorigenesis, and are present in numerous human breast cancers. Mature human Wnt-1 is a glycosylated protein containing 343 amino acid residues. Recombinant Human Wnt-1 is a 38.4 kDa, non-glycosylated protein containing 343 amino acid residues.

Catalog Number: (10771-604)

Supplier: Peprotech

Description: PeproTech's Rat IL-1α ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant Rat IL-1α in a sandwich ELISA format.

Supplier: Peprotech

Description: 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: 5UG

Supplier: Peprotech

Description: EG-VEGF is a secreted angiogenetic mitogen growth factor expressed in the steroidogenic glands, ovary, testis, adrenal gland, and placenta. EG-VEGF induces proliferation, migration, and fenestration (formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. The murine EG-VEGF gene codes for a 105 amino acid polypeptide containing an N-terminal signal sequence of 19 amino acids. Recombinant Murine EG-VEGF is a 9.6 kDa protein consisting of 86 amino acid residues, including ten cysteine residues that potentially form five pairs of intra-molecular disulfide bonds.

Supplier: Peprotech

Description: 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.

Supplier: Peprotech

Description: 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 are cross-species reactive.  Recombinant Human IL-7 is a 17.4 kDa protein containing 153 amino acid residues.Manufactured using all Animal-Free reagents.

Supplier: Peprotech

Description: RELMβ (Resistin-like molecule β/FIZZ2) is a disulfide-linked, homodimeric protein expressed in the epithelium of the colon and small bowel. The biological functions of RELMβ, and its molecular targets, are not fully known, but it has been suggested that it plays a regulatory role during inflammation, and may also act to establish links among adipose tissue, the intestine and the liver. Interestingly, the molecular structure of RELMβ is highly homologous to that of the adipose-derived cytokines, resistin and RELMα. These proteins 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. Recombinant Murine RELMβ is an 18.0 kDa protein, consisting of two identical 83 amino acid polypeptide chains linked by a single disulfide bond.

Supplier: Peprotech

Description: Activin A is a TGF-β family member that exhibits a wide range of biological activities, including regulation of cellular proliferation and differentiation, and promotion of neuronal survival. Elevated levels of Activin A in human colorectal tumors and in postmenopausal women have been implicated in colorectal and breast cancers, respectively. The biological activities of Activin A can be neutralized by inhibins and by the diffusible TGF-β antagonist, follistatin. Activin A binds to the two forms of activin receptor type I (Act RI-A and Act RI-B) and two forms of activin receptor type II (Act RII-A and Act RII-B). Activins are homodimers or heterodimers of different β subunits. They are produced as precursor proteins with an amino terminal propeptide that is cleaved to release the C-terminal bioactive ligand. Recombinant Human/Murine/Rat Activin A is a 26.0 kDa disulfide-linked homodimer of two βA chains, each containing 116 amino acid residues.

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Supplier: Peprotech

Description: Semaphorins are a large group of structurally-related, secreted, GPI-anchored, transmembrane, cell-signaling molecules. There are 8 major classifications of Semaphorins (the first seven ordered by number, 1-7, and the eighth designated V for virus), which are characterized by the existence of a conserved 500 amino acid SEMA domain at the amino terminus. Classes 3, 4, 6, and 7 are found in vertebrates only, whilst class 5 is found in both vertebrates and invertebrates. Each class is then divided into additional subgroups based on shared structural characteristics. Semaphorins primarily function as axon growth cone guidance factors during neuronal development. Semaphorin 3A acts as a chemo-repellent to axons, and an inhibitor of the growth of axons by signaling through receptors, Neuropilin-1 and Plexin-A. PeproTech's CHO cell-derived Recombinant Human Semaphorin 3A Fc is a glycosylated, disulfide-linked homodimer of 1,976 amino acid residues, which includes the SEMA domain, immunoglobulin c2-like domain, and the C-terminal basic Arg/Lys-rich domain of the mature sequence, as well as an 8-residue N-terminal His-tag and a 230-residue C-terminal Fc region linked by two glycines. Recombinant Human Semaphorin 3A Fc has a calculated molecular weight of 226.2 kDa and therefore runs above the 200kDa marker by SDS-PAGE analysis under nonreducing conditions. When run under reducing conditions, this protein migrates as three distinct bands that, due to glycosylation, run higher than expected at apparent molecular weights of approximately 120-130 kDa, 90-100 kDa, and 35-40 kDa.

Supplier: Peprotech

Description: 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 Rat sRANK Ligand is a 19.4 kDa polypeptide comprising the TNF homologous region of RANKL (174 amino acid residues).

Supplier: Peprotech

Description: Viral MIP-2 (vMIP-2) is a chemokine analog encoded by the human herpes virus, and has been shown to have antagonist activity towards several chemokine receptors. Recombinant Viral MIP-2 is a 7.9 kDa protein consisting of 70 amino acids, including the four highly conserved cysteine residues present in CC chemokines.

Supplier: Peprotech

Description: 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.

Supplier: Peprotech

Description: PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors, such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity ( Notari, I. et al. J Biol Chem., Vol. 281, 38022-38037 ) should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic agent for the treatment of vasculature-related neurodegenerative diseases, such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF also has the potential to be useful in the treatment of various angiogenesis-related diseases including a number of cancers. Recombinant Human PEDF is a 44.5 kDa non-glycosylated protein containing 400 amino acid residues.