"Peprotech"

Supplier: Peprotech

VCAM is a 110 kDa, cell surface integral membrane glycoprotein that belongs to the Ig-related superfamily of adhesion molecules. The primary function of VCAM-1 is the mediation of leukocyte-endothelial cell adhesion and signal transduction. VCAM-1 may play a vital role in the development of several diseases, including atherosclerosis and rheumatoid arthritis. The human VCAM-1 gene codes for a 715 amino acid transmembrane glycoprotein containing a 19 amino acid cytoplasmic domain, a 22 amino acid transmembrane domain, and a 674 amino acid extracellular domain. Recombinant Human VCAM-1 is a 74.1 kDa glycoprotein comprising the extracellular domain (674 amino acid residues) of VCAM-1. Monomeric glycosylated VCAM-1 migrates at an apparent molecular weight of approximately 90.0 kDa by SDS-PAGE analysis under reducing conditions.

Supplier: Peprotech

RELMα belongs to a unique family of tissue-specific cytokines termed FIZZ (found in inflammatory zone) and RELM. The four known members of this family, resistin, RELMα, RELMβ, and RELMγ, are 85-94 amino acid, secreted proteins sharing a 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. RELMα and resistin are secreted exclusively by adipocytes, while RELMβ is expressed in the epithelium of the colon and small bowel. The physiological role and molecular targets of RELMα are still unknown. Recombinant Murine RELMα is a 10.0 kDa monomeric protein containing 89 amino acid residues.

Supplier: Peprotech

BCMA, a member of the TNF receptor superfamily, binds to BAFF and APRIL. BCMA is expressed on mature B-cells and other B-cell lines, and plays an important role in B-cell development, function and regulation. BCMA also has the capability to activate NF-κB and JNK. The human BCMA gene codes for a 184 amino acid type I transmembrane protein, which contains a 54 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 107 amino acid cytoplasmic domain. Recombinant soluble Human BCMA is a 50 amino acid polypeptide (5.3 kDa) comprising the TNFR homologous region of the BCMA protein.

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

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.

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Produced from sera of rabbits immunized with highly pure Recombinant Murine IL-5. Anti­Murine IL-5­specific antibody was purified by affinity chromatography employing an immobilized Murine IL-5 matrix.

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 (.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 Murine 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

LIF is a pleiotrophic factor produced by multiple cell types, including T cells, myelomonocytic lineages, fibroblasts, liver, heart and melanoma. LIF promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Other activities include the stimulation of acute phase protein synthesis by hepatocytes, stimulation of differentiation of cholinergic nerves, and suppression of adipogenesis by inhibiting the lipoprotein lipase in adipocytes. While human LIF is active on mouse cells and is widely used in the maintenance of murine ESC to prevent spontaneous differentiation, mouse LIF is not active on human cells due to its inability to bind to the human LIF receptor. Recombinant Human LIF is a 19.6 kDa protein containing 180 amino acids residues, including three disulfide bonds.

Supplier: Peprotech

HCC-1 is a CC chemokine that signals through the CCR1 receptor and chemoattracts blood monocytes. It is secreted by various tissues, including skeletal muscle, heart, spleen, liver, bone marrow and plasma. Mature HCC-1 is found in four different forms, which are distinguished by differential N-terminal truncation and contain 74, 72, 71, or 66 amino acid residues. Recombinant Human HCC-1 (CCL14) is a 7.8 kDa protein consisting of 66 amino acids, including the four highly conserved residues present in CC chemokines.

Supplier: Peprotech

Produced from sera of rabbits immunized with highly pure Recombinant Murine MIP-2 (CXCL2). Anti­Murine MIP-2 (CXCL2)­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: Peprotech

Produced from sera of goats immunized with highly pure Recombinant Human MCP-4 (CCL13). Anti­Human MCP-4 (CCL13)­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: Peprotech

IL-21 is a pleiotropic cytokine produced by CD4+ T cells in response to antigenic stimulation. Its action generally enhances antigen-specific responses of immune cells. The biological effects of IL-21 include: inducing the differentiation of T-cell-stimulated B-cells into plasma cells and memory B-cells; the stimulation of IgG production in conjunction with IL-4; and the induction of apoptotic effects in naïve B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T-cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the γ chain (γc) found in other cytokine receptors, including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R interaction triggers a cascade of events, which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3. Recombinant Human IL-21 is a 15.4 kDa protein consisting of 132 amino acid residues.

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Relaxin-3 is a secreted protein structurally related to insulin that is expressed primarily in the brain and central nervous system. Relaxin-3 has been identified as the ligand for the GPCR135 receptor, previously known as “somatostatin-like” or “angiotensin-like” peptide receptor, and has also been identified for binding specifically to the LGR7 receptor, previously identified as an “orphan” G protein-coupled receptor. Signaling by relaxin-3 through its target receptors is, most likely, part of a CNS processing system, activated in response to signaling by neuropeptides and other factors. Intracerebroventricular injections of relaxin-3 have been shown to cause a significant increase of food intake and body weight in Wistar rats. Recombinant Human Relaxin-3 is a 5.5 kDa, disulfide-linked, heterodimeric protein consisting of a 24 amino acid A-chain and a 27 amino acid B-chain.

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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-1 is a 5.0 kDa protein containing 47 amino acid residues.

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Lin28 is a RNA-binding protein that belongs to a diverse family of structurally-related transcription factors. Lin28 is found abundantly in embryonic stem cells (ESCs), and to a lesser extent in placenta and testis. Lin28 has been shown to block let-7 microRNA processing and maturation, a necessary step in the differentiation of stem cells and certain cancer cell lines. Together with Sox2, Oct4, and Nanog, Lin28 can induce the reprogramming of primary human fibroblasts to a pluripotent state. Lin28 and other regulatory proteins can be introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing proteins into primary, as well as transformed, cells. Recombinant Human Lin28-TAT is a 24.4 kDa protein containing 222 amino acid residues, including a 13-residue C-terminal TAT peptide.

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FGF-17 is a heparin-binding growth factor that is a member 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-17 signals through the FGFR 1c, 2c, 3c, and 4. FGF-17 signals induction and patterning of embryonic brain. Recombinant Human FGF-17 is a 22.7 kDa protein consisting of 195 amino acid residues.