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Description:
Calcium ions play a primary role in the regulation of sperm motility. Anti-CATSPER2 belongs to a family of putative cation channels that are specific to spermatozoa and localize to the flagellum. The protein family features a single repeat with six membrane-spanning segments and a predicted calcium-selective pore region. A second, closely linked copy of this gene has been identified. Although multiple transcript variants encoding protein isoforms have been characterized, they seem to be only transcribed from this gene. Additional splice variants have been described but their full-length nature has not been determined.
Description:
The M channel is a slowly activating and deactivating potassium channel that plays a critical role in the regulation of neuronal excitability. The M channel is formed by the association of the protein encoded by the KCNQ2 gene and a related protein encoded by the KCNQ3 gene, both integral membrane proteins. M channel currents are inhibited by M1 muscarinic acetylcholine receptors and activated by retigabine, a novel anti-convulsant drug. Defects in KCNQ2 are a cause of benign familial neonatal convulsions type 1 (BFNC), also known as epilepsy, benign neonatal type 1 (EBN1).
Description:
Wnts are lipid-modified morphogens that control many processes during development, stem cell maintenance and homeostasis and their aberrant regulation has been linked to diseases in man including diabetes, neurodegeneration and cancer. Three distinct receptor families mediate Wnt signalling: Fzs, the single-pass LRP5/6 co-receptors and the atypical tyrosine kinase receptors Ror2 and Ryk. Frizzled proteins can activate canonical Wnt/beta-catenin signalling as well as non-canonical pathways (Wnt/Ca2+ pathways and planar cell polarity). The cysteine-rich domain (CRD) of the frizzled receptors situated on the extracellular part of the receptor is sufficient to bind the Wnt ligands.
Description:
Glycosylphosphatidylinositol (GPI) is a complex glycolipid that anchors many proteins to the cell surface. PIGW acts in the third step of GPI biosynthesis and acylates the inositol ring of phosphatidylinositol.Glycosylphosphatidylinositol (GPI) is a complex glycolipid that anchors many proteins to the cell surface. PIGW acts in the third step of GPI biosynthesis and acylates the inositol ring of phosphatidylinositol (Murakami et al., 2003 [PubMed 14517336]).
Description:
ST6GALNAC4 is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. ST6GALNAC4 prefers glycoproteins rather than glycolipids as substrates and shows restricted substrate specificity, utilizing only the trisaccharide sequence Neu5Ac-alpha-2,3-Gal-beta-1,3-GalNAc. In addition, it is involved in the synthesis of ganglioside GD1A from GM1B. ST6GALNAC4 is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. It is a member of glycosyltransferase family 29.The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein prefers glycoproteins rather than glycolipids as substrates and shows restricted substrate specificity, utilizing only the trisaccharide sequence Neu5Ac-alpha-2,3-Gal-beta-1,3-GalNAc. In addition, it is involved in the synthesis of ganglioside GD1A from GM1B. The encoded protein is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29. Transcript variants encoding different isoforms have been found for this gene.
Description:
Recombinant Human Interleukin-2 is a highly purified protein with a molecular weight of approximately 15,300 Daltons. The chemical name is des-alanyl-1, serine-125 Human Interleukin-2. It is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of the human interleukin-2 gene. Genetic engineering techniques were used to modify the Human IL-2 gene, and the resulting expression clone encodes a modified Human IL-2. This recombinant form differs from native Interleukin-2 in following ways: 1) it is not glycosylated; 2) the molecule has no N-terminal alanine; 3) the molecule has serine substituted for cysteine at amino acid position 125; 4) the aggregation state of molecule is likely to be different from that of native IL-2.
Description:
Thioredoxin Domain-Containing Protein 12 belongs to the thioredoxin superfamily. In this family, proteins possess a thioredoxin fold with a consensus active-site sequence (CxxC) and have roles in redox regulation, defense against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors. TXNDC12 is widely expressed in many tissues and contains one thioredoxin domain.
Description:
Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. As IL-17 shares properties with IL-1 and TNF-alpha, it may induce joint inflammation and bone and cartilage destruction. This cytokine is found in synovial fluids of patients with rheumatoid arthritis, and produced by rheumatoid arthritis synovium. It increases IL-6 production, induces collagen degradation and decreases collagen synthesis by synovium and cartilage and proteoglycan synthesis in cartilage. IL-17 is also able to increase bone destruction and reduce its formation. Blocking of interleukin-17 with specific inhibitors provides a protective inhibition of cartilage and bone degradation.
Description:
Leukemia Inhibitory Factor (LIF) is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. LIF has a number of other activities including cholinergic neuron differentiation, control of stem cell pluripotency, bone and fat metabolism, mitogenesis of certain factor dependent cell lines and promotion of megakaryocyte production in vivo. Human and murine mature LIF exhibit a 78% sequence identity at the amino acid level. Human LIF is equally active on human and mouse cells. Murine LIF is approximately 1000 fold less active on human cells than human LIF.
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