5-HT1B receptor blocking peptide Reference: GTX89298-PEP The neurotransmitter serotonin (5-hydroxytryptamine; 5-HT) exerts a wide variety of physiologic functions through a multiplicity of receptors and may be involved in human neuropsychiatric disorders such as anxiety, depression, or migraine. These receptors consist of several main groups subdivided into several distinct subtypes on the basis of their pharmacologic characteristics, coupling to intracellular second messengers, and distribution within the nervous system (Zifa and Fillion, 1992 [PubMed 1359584]). The serotonergic receptors belong to the multigene family of receptors coupled to guanine nucleotide-binding proteins.[supplied by OMIM, Oct 29]
Recombinant Human TGF-α Reference: GFH209-50 Tumor growth factor alpha (TGF-α) is a member of the epidermal growth factor (EGF) family. TGF-α function is mediated through binding the EGF receptor (EGFR) to activate receptor tyrosine kinase signaling. TGF-α functions as a mitogen to activate epithelial cell proliferation, growth, and differentiation. In the gastric mucosa, TGF-α production inhibits gastric acid secretion and therefore plays a central role in the pathogenesis of the stomach disease. TGF-α is also produced in adult macrophages, brain cells, keratinocytes, and is widely expressed in cancer cells.
GPR94 blocking peptide Reference: GTX89299-PEP This gene encodes a member of a family of adenosine triphosphate(ATP)-metabolizing molecular chaperones with roles in stabilizing and folding other proteins. The encoded protein is localized to melanosomes and the endoplasmic reticulum. Expression of this protein is associated with a variety of pathogenic states, including tumor formation. There is a microRNA gene located within the 5' exon of this gene. There are pseudogenes for this gene on chromosomes 1 and 15. [provided by RefSeq, Aug 212]
Recombinant Human TGF-α Reference: GFH209-100 Tumor growth factor alpha (TGF-α) is a member of the epidermal growth factor (EGF) family. TGF-α function is mediated through binding the EGF receptor (EGFR) to activate receptor tyrosine kinase signaling. TGF-α functions as a mitogen to activate epithelial cell proliferation, growth, and differentiation. In the gastric mucosa, TGF-α production inhibits gastric acid secretion and therefore plays a central role in the pathogenesis of the stomach disease. TGF-α is also produced in adult macrophages, brain cells, keratinocytes, and is widely expressed in cancer cells.
CILP blocking peptide Reference: GTX89301-PEP Major alterations in the composition of the cartilage extracellular matrix occur in joint disease, such as osteoarthrosis. This gene encodes the cartilage intermediate layer protein (CILP), which increases in early osteoarthrosis cartilage. The encoded protein was thought to encode a protein precursor for two different proteins; an N-terminal CILP and a C-terminal homolog of NTPPHase, however, later studies identified no nucleotide pyrophosphatase phosphodiesterase (NPP) activity. The full-length and the N-terminal domain of this protein was shown to function as an IGF-1 antagonist. An allelic variant of this gene has been associated with lumbar disc disease. [provided by RefSeq, Sep 21]
Recombinant Human TGF-α Reference: GFH209-1000 Tumor growth factor alpha (TGF-α) is a member of the epidermal growth factor (EGF) family. TGF-α function is mediated through binding the EGF receptor (EGFR) to activate receptor tyrosine kinase signaling. TGF-α functions as a mitogen to activate epithelial cell proliferation, growth, and differentiation. In the gastric mucosa, TGF-α production inhibits gastric acid secretion and therefore plays a central role in the pathogenesis of the stomach disease. TGF-α is also produced in adult macrophages, brain cells, keratinocytes, and is widely expressed in cancer cells.
NMDAR1 blocking peptide Reference: GTX89302-PEP The protein encoded by this gene is a critical subunit of N-methyl-D-aspartate receptors, members of the glutamate receptor channel superfamily which are heteromeric protein complexes with multiple subunits arranged to form a ligand-gated ion channel. These subunits play a key role in the plasticity of synapses, which is believed to underlie memory and learning. Cell-specific factors are thought to control expression of different isoforms, possibly contributing to the functional diversity of the subunits. Alternatively spliced transcript variants have been described. [provided by RefSeq, Jul 28]
Recombinant Human TGF-α (Animal-Free) Reference: GFH209AF-10 Tumor growth factor alpha (TGF-α) is a member of the epidermal growth factor (EGF) family. TGF-α function is mediated through binding the EGF receptor (EGFR) to activate receptor tyrosine kinase signaling. TGF-α functions as a mitogen to activate epithelial cell proliferation, growth, and differentiation. In the gastric mucosa, TGF-α production inhibits gastric acid secretion and therefore plays a central role in the pathogenesis of the stomach disease. TGF-α is also produced in adult macrophages, brain cells, keratinocytes, and is widely expressed in cancer cells.
NLRP3 (Internal) blocking peptide Reference: GTX89303-PEP This gene encodes a pyrin-like protein containing a pyrin domain, a nucleotide-binding site (NBS) domain, and a leucine-rich repeat (LRR) motif. This protein interacts with the apoptosis-associated speck-like protein PYCARD/ASC, which contains a caspase recruitment domain, and is a member of the NALP3 inflammasome complex. This complex functions as an upstream activator of NF-kappaB signaling, and it plays a role in the regulation of inflammation, the immune response, and apoptosis. Mutations in this gene are associated with familial cold autoinflammatory syndrome (FCAS), Muckle-Wells syndrome (MWS), chronic infantile neurological cutaneous and articular (CINCA) syndrome, and neonatal-onset multisystem inflammatory disease (NOMID). Multiple alternatively spliced transcript variants encoding distinct isoforms have been identified for this gene. Alternative 5' UTR structures are suggested by available data; however, insufficient evidence is available to determine if all of the represente
Recombinant Human TGF-α (Animal-Free) Reference: GFH209AF-50 Tumor growth factor alpha (TGF-α) is a member of the epidermal growth factor (EGF) family. TGF-α function is mediated through binding the EGF receptor (EGFR) to activate receptor tyrosine kinase signaling. TGF-α functions as a mitogen to activate epithelial cell proliferation, growth, and differentiation. In the gastric mucosa, TGF-α production inhibits gastric acid secretion and therefore plays a central role in the pathogenesis of the stomach disease. TGF-α is also produced in adult macrophages, brain cells, keratinocytes, and is widely expressed in cancer cells.
Melanoma gp100 blocking peptide Reference: GTX89304-PEP This gene encodes a melanocyte-specific type I transmembrane glycoprotein. The encoded protein is enriched in melanosomes, which are the melanin-producing organelles in melanocytes, and plays an essential role in the structural organization of premelanosomes. This protein is involved in generating internal matrix fibers that define the transition from Stage I to Stage II melanosomes. This protein undergoes a complex pattern of prosttranslational processing and modification that is essential to the proper functioning of the protein. A secreted form of this protein that is released by proteolytic ectodomain shedding may be used as a melanoma-specific serum marker. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jan 211]
Recombinant Human TGF-α (Animal-Free) Reference: GFH209AF-100 Tumor growth factor alpha (TGF-α) is a member of the epidermal growth factor (EGF) family. TGF-α function is mediated through binding the EGF receptor (EGFR) to activate receptor tyrosine kinase signaling. TGF-α functions as a mitogen to activate epithelial cell proliferation, growth, and differentiation. In the gastric mucosa, TGF-α production inhibits gastric acid secretion and therefore plays a central role in the pathogenesis of the stomach disease. TGF-α is also produced in adult macrophages, brain cells, keratinocytes, and is widely expressed in cancer cells.