100-001
4-1BBL, a member of the TNF superfamily, is expressed in B cells, dendritic cells, activated T cells and macrophages. 4-1BBL binds to its receptor 4-1BB, and provides a co-stimulatory signal for T cell activation and expansion. The human 4-1BBL gene codes for a 254 amino acid type II transmembrane containing a 28 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 205 amino acid extracellular domain. The soluble form of 4-1BBL contains the TNF-like portion of the extracellular domain of 4-1BBL. Recombinant human 4-1BBL is a soluble 19.5 kDa protein consisting of 185 amino acid residues.
100-001S
4-1BBL, a member of the TNF superfamily, is expressed in B cells, dendritic cells, activated T cells and macrophages. 4-1BBL binds to its receptor 4-1BB, and provides a co-stimulatory signal for T cell activation and expansion. The human 4-1BBL gene codes for a 254 amino acid type II transmembrane containing a 28 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 205 amino acid extracellular domain. The soluble form of 4-1BBL contains the TNF-like portion of the extracellular domain of 4-1BBL. Recombinant human 4-1BBL is a soluble 19.5 kDa protein consisting of 185 amino acid residues.
100-002
BAFF, a member of the TNF family of ligands, is expressed in T cells, macrophages, monocytes and dendritic cells. BAFF is involved in stimulation of B and T cell function, and is an important survival and maturation factor for peripheral B cells. BAFF signals through three different TNF receptors TACI, BCMA and BAFF-R. The human BAFF gene codes for a 285 amino acid type II transmembrane protein containing a 46 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 218 amino acid extracellular domain. Recombinant human soluble BAFF is a 153 amino acid polypeptide (17.0 kDa), which contains the TNF-like portion of the extracellular domain of BAFF.
100-002-AF
BAFF, a member of the TNF family of ligands, is expressed in T cells, macrophages, monocytes and dendritic cells. BAFF is involved in stimulation of B and T cell function, and is an important survival and maturation factor for peripheral B cells. BAFF signals through three different TNF receptors, TACI, BCMA and BAFF-R. The human BAFF gene codes for a 285 amino acid type II transmembrane protein containing a 46 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 218 amino acid extracellular domain. Recombinant Human soluble BAFF is a 152 amino acid polypeptide (17.0 kDa), which contains the TNF-like portion of the extracellular domain of BAFF.
100-002S
BAFF, a member of the TNF family of ligands, is expressed in T cells, macrophages, monocytes and dendritic cells. BAFF is involved in stimulation of B and T cell function, and is an important survival and maturation factor for peripheral B cells. BAFF signals through three different TNF receptors TACI, BCMA and BAFF-R. The human BAFF gene codes for a 285 amino acid type II transmembrane protein containing a 46 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 218 amino acid extracellular domain. Recombinant human soluble BAFF is a 153 amino acid polypeptide (17.0 kDa), which contains the TNF-like portion of the extracellular domain of BAFF.
100-002S-AF
BAFF, a member of the TNF family of ligands, is expressed in T cells, macrophages, monocytes and dendritic cells. BAFF is involved in stimulation of B and T cell function, and is an important survival and maturation factor for peripheral B cells. BAFF signals through three different TNF receptors, TACI, BCMA and BAFF-R. The human BAFF gene codes for a 285 amino acid type II transmembrane protein containing a 46 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 218 amino acid extracellular domain. Recombinant Human soluble BAFF is a 152 amino acid polypeptide (17.0 kDa), which contains the TNF-like portion of the extracellular domain of BAFF.
100-003
BCA-1/BLC, a CXC chemokine, is expressed in the liver, spleen, lymph nodes, appendix and stomach. It exerts its activities through its only receptor CXCR5. BCA-1/BLC is a potent chemoattractant for B lymphocytes and induces weak chemotactic response in T cells and macrophages. It manifests no activity on neutrophils and monocytes. Recombinant Human BCA-1 is a 10.3 kDa protein containing 87 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines.
100-003S
BCA-1/BLC, a CXC chemokine, is expressed in the liver, spleen, lymph nodes, appendix and stomach. It exerts its activities through its only receptor CXCR5. BCA-1/BLC is a potent chemoattractant for B lymphocytes and induces weak chemotactic response in T cells and macrophages. It manifests no activity on neutrophils and monocytes. Recombinant Human BCA-1 is a 10.3 kDa protein containing 87 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines.
100-004
Human ß-defensin-2 (BD-2) is an antimicrobial peptide which belongs to the distinct family of ß-defensins. Recent studies have shown that the ß-defensins are present in the human airways and may be relevant to the pathogenesis of cystic fibrosis lung disease. Human BD-2 is a 4.3 kDa protein containing 43 amino acid residues.
100-004S
Human ß-defensin-2 (BD-2) is an antimicrobial peptide which belongs to the distinct family of ß-defensins. Recent studies have shown that the ß-defensins are present in the human airways and may be relevant to the pathogenesis of cystic fibrosis lung disease. Human BD-2 is a 4.3 kDa protein containing 43 amino acid residues.
100-005
BDNF is a member of the NGF family of neurotrophic growth factors. Like other members of this family, BDNF supports neuron proliferation and survival. BDNF can bind to a low affinity cell surface receptor called LNGFR, which also binds other neurotrophins such as NGF, NT-3 and NT-4. However, BDNF mediates its neurotrophic properties by signaling through a high affinity cell surface receptor called gp145/trkB. BDNF is expressed as the C-terminal portion of a 247 amino acid polypeptide precursor, which also contains a signal sequence of 18 amino acid residues and a propeptide of 110 amino acid residues. Recombinant Human BDNF is a 27.0 kDa homodimer of two 120 amino acid subunits linked by strong non-covalent interactions. Human and Mouse BDNF sequences are identical.
100-005-AF
BDNF is a member of the NGF family of neurotrophic growth factors. Like other members of this family, BDNF supports neuron proliferation and survival. BDNF can bind to a low affinity cell surface receptor called LNGFR, which also binds other neurotrophins such as NGF, NT-3 and NT-4. However, BDNF mediates its neurotrophic properties by signaling through a high affinity cell surface receptor called gp145/trkB. BDNF is expressed as the C-terminal portion of a 247 amino acid polypeptide precursor, which also contains a signal sequence of 18 amino acid residues and a propeptide of 110 amino acid residues. Recombinant Human/Murine/Rat BDNF is a 27.0 kDa homodimer of two 120 amino acid subunits linked by strong non-covalent interactions.
100-005S
BDNF is a member of the NGF family of neurotrophic growth factors. Like other members of this family, BDNF supports neuron proliferation and survival. BDNF can bind to a low affinity cell surface receptor called LNGFR, which also binds other neurotrophins such as NGF, NT-3 and NT-4. However, BDNF mediates its neurotrophic properties by signaling through a high affinity cell surface receptor called gp145/trkB. BDNF is expressed as the C-terminal portion of a 247 amino acid polypeptide precursor, which also contains a signal sequence of 18 amino acid residues and a propeptide of 110 amino acid residues. Recombinant Human BDNF is a 27.0 kDa homodimer of two 120 amino acid subunits linked by strong non-covalent interactions. Human and Mouse BDNF sequences are identical.
100-005S-AF
BDNF is a member of the NGF family of neurotrophic growth factors. Like other members of this family, BDNF supports neuron proliferation and survival. BDNF can bind to a low affinity cell surface receptor called LNGFR, which also binds other neurotrophins such as NGF, NT-3 and NT-4. However, BDNF mediates its neurotrophic properties by signaling through a high affinity cell surface receptor called gp145/trkB. BDNF is expressed as the C-terminal portion of a 247 amino acid polypeptide precursor, which also contains a signal sequence of 18 amino acid residues and a propeptide of 110 amino acid residues. Recombinant Human/Murine/Rat BDNF is a 27.0 kDa homodimer of two 120 amino acid subunits linked by strong non-covalent interactions.
100-006
CT-1 is a member of the IL-6 family of cytokines which also includes LIF, CNTF, OSM (Oncostatin M), IL-11, IL-6 and possibly NT-1/ BSF-3. CT-1 is a pleiotrophic cytokine which is expressed in various tissues including the adult heart, skeletal muscle, ovary, colon, prostate and fetal lung and signals through the LIF receptor and the gp130 receptor subunit. CT-1 has the ability to induce cardiac myocyte hypertrophy, and enhances the survival of cardiomyocyte and different neuronal populations. Biologically active human CT-1 is synthesized as a 201 amino acid polypeptide lacking a hydrophobic N-terminal secretion signal sequence. Recombinant Human Cardiotrophin-1 is a 21.5 kDa protein consisting of 201 amino acid residues.
100-006S
CT-1 is a member of the IL-6 family of cytokines which also includes LIF, CNTF, OSM (Oncostatin M), IL-11, IL-6 and possibly NT-1/ BSF-3. CT-1 is a pleiotrophic cytokine which is expressed in various tissues including the adult heart, skeletal muscle, ovary, colon, prostate and fetal lung and signals through the LIF receptor and the gp130 receptor subunit. CT-1 has the ability to induce cardiac myocyte hypertrophy, and enhances the survival of cardiomyocyte and different neuronal populations. Biologically active human CT-1 is synthesized as a 201 amino acid polypeptide lacking a hydrophobic N-terminal secretion signal sequence. Recombinant Human Cardiotrophin-1 is a 21.5 kDa protein consisting of 201 amino acid residues.
100-007
CNTF is a potent neural factor that was originally characterized as a vital factor for the survival of chick ciliary neurons in vitro. CNTF is also important for the survival of other neural cell types including primary sensory neurons, motor neurons, basal forebrain neurons and type 2 astrocytes. CNTF is highly conserved across species and exhibits cross-species bioactivity. Recombinant human CNTF is synthesized as a 199 amino acid polypeptide (22.7 kDa) lacking a hydrophobic N-terminal signal for secretion
100-007-AF
CNTF is a potent neural factor that was originally characterized as a vital factor for the survival of chick ciliary neurons in vitro. CNTF is also important for the survival of other neural cell types, including primary sensory neurons, motor neurons, basal forebrain neurons and type 2 astrocytes. CNTF is highly conserved across species and exhibits cross-species bioactivity. Recombinant Human CNTF is synthesized as a 199 amino acid polypeptide (22.8 kDa) lacking a hydrophobic N-terminal signal for secretion.
100-007S
CNTF is a potent neural factor that was originally characterized as a vital factor for the survival of chick ciliary neurons in vitro. CNTF is also important for the survival of other neural cell types including primary sensory neurons, motor neurons, basal forebrain neurons and type 2 astrocytes. CNTF is highly conserved across species and exhibits cross-species bioactivity. Recombinant human CNTF is synthesized as a 199 amino acid polypeptide (22.7 kDa) lacking a hydrophobic N-terminal signal for secretion
100-007S-AF
CNTF is a potent neural factor that was originally characterized as a vital factor for the survival of chick ciliary neurons in vitro. CNTF is also important for the survival of other neural cell types, including primary sensory neurons, motor neurons, basal forebrain neurons and type 2 astrocytes. CNTF is highly conserved across species and exhibits cross-species bioactivity. Recombinant Human CNTF is synthesized as a 199 amino acid polypeptide (22.8 kDa) lacking a hydrophobic N-terminal signal for secretion.
100-008
Epidermal growth factor (EGF) is the founding member of the EGF family that also includes TGFα, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin-binding EGF-like growth factor (HBEGF), epigen, and the neuregulins (NRG) 1 through 6. Members of the EGF family share a structural motif, the EGF-like domain, which is characterized by three intra-molecular disulfide bonds that are formed by six similarly spaced conserved cysteine residues. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. The 1207 amino acid (aa) human EGF precursor contains nine EGF domains and nine LDLR class B repeats. The mature protein consists of 53 aa and is generated by proteolytic excision of the EGF domain proximal to the transmembrane region. Mature human EGF shares 70% aa sequence identity with mature mouse and rat EGF. EGF is present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members. EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2. Biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture.
100-008-AF
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 Human EGF is a 6.2 kDa globular protein containing 53 amino acid residues, including 3 intramolecular disulfide bonds.
100-009
Epidermal growth factor (EGF) is the founding member of the EGF family that also includes TGFα, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin-binding EGF-like growth factor (HBEGF), epigen, and the neuregulins (NRG) 1 through 6. Members of the EGF family share a structural motif, the EGF-like domain, which is characterized by three intra-molecular disulfide bonds that are formed by six similarly spaced conserved cysteine residues. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. The 1207 amino acid (aa) human EGF precursor contains nine EGF domains and nine LDLR class B repeats. The mature protein consists of 53 aa and is generated by proteolytic excision of the EGF domain proximal to the transmembrane region. Mature human EGF shares 70% aa sequence identity with mature mouse and rat EGF. EGF is present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members. EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2. Biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture.
100-009-AF
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 Human EGF is a 6.2 kDa globular protein containing 53 amino acid residues, including 3 intramolecular disulfide bonds.
100-010
EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
100-011
ENA-78 is a CXC chemokine that signals through the CXCR2 receptor. It is expressed in monocytes, platelets, endothelial cells, and mast cells. ENA-78 is a chemoattractant for neutrophils. The three naturally occurring variants of human ENA-78; ENA 5-78, ENA 9-78 and ENA 10-78, contain 74, 70, and 69 amino acid residues, respectively, and possess the same biological activity. ENA-78 contains the four conserved cysteine residues present in CXC chemokines, and also contains the 'ELR' motif common to CXC chemokine that bind to the CXCR1 and CXCR2 receptors. Recombinant human ENA-78 is an 8.0 kDa protein consisting of 74 amino acid residues.
100-011S
ENA-78 is a CXC chemokine that signals through the CXCR2 receptor. It is expressed in monocytes, platelets, endothelial cells, and mast cells. ENA-78 is a chemoattractant for neutrophils. The three naturally occurring variants of human ENA-78; ENA 5-78, ENA 9-78 and ENA 10-78, contain 74, 70, and 69 amino acid residues, respectively, and possess the same biological activity. ENA-78 contains the four conserved cysteine residues present in CXC chemokines, and also contains the 'ELR' motif common to CXC chemokine that bind to the CXCR1 and CXCR2 receptors. Recombinant human ENA-78 is an 8.0 kDa protein consisting of 74 amino acid residues.
100-012
Activin A is a TGF-beta 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 post-menopausal woman 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-beta antagonist, Follistatin. Human Activin A is a 26 kDa disulfide-linked homodimer of two beta A chains, each containing 116 amino acid residues.
100-012S
Activin A is a TGF-beta 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 post-menopausal woman 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-beta antagonist, Follistatin. Human Activin A is a 26 kDa disulfide-linked homodimer of two beta A chains, each containing 116 amino acid residues.
100-013
Eotaxin-2 is a CC chemokine that signals through the CCR3 receptor. It is produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemo attracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Additionally, Eotaxin-2 inhibits the proliferation of multi potential hematopoietic progenitor cells. The mature protein, which also includes a C-terminal truncation, contains 78 amino acid residues (92 a.a. residues for the murine homolog, without C-terminal truncation). Recombinant human Eotaxin-2 is an 8.8 kDa protein containing 78 amino acid residues.