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Product CategoryVEGF Receptor 1 (also known as FLT) belongs to the src gene family and shows tyrosine protein kinase activity that is important for the control of cell proliferation and differentiation. The protein acts as a receptor for VEGF, VEGFB and PGF. An alternatively spliced form of the gene produces a soluble protein (sFlt1) which binds vascular endothelial growth factor (VEGF) with high affinity. sFlt1 has a higher affinity for VEGF indicating that it may function as an inhibitor in the VEGF respo
Human papilloma viruses (HPVs) can be classified as either high risk or low risk according to their association with cancer. HPV16 and HPV18 are the most common of the high risk group while HPV6 and HPV11 are among the low risk types. Approximately 90% of cervical cancers contain HPV DNA of the high risk types. Mutational analysis have shown that the E6 and E7 genes of the high risk HPVs are necessary and sufficient for HPV transforming function. The specific interactions of the E6 and E7
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. This gene encodes a member of the potassium channel, voltage-gated, subfamily H. This member is a pore-forming (alpha) subunit of a voltage-gated
Modulation of the chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. The N-terminal tail of core histones undergoes different posttranslational modifications including acetylation, phosphorylation and methylation. These modifications occur in response to cell signal stimuli and have a direct effect on gene expression. In most spec
Alpha-L-fucosidase,AFU is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
The connexin family of proteins form hexameric complexes called connexons that facilitate movement of low molecular weight proteins between cells via gap junctions. Connexin proteins share a common topology of four transmembrane alpha-helical domains, two extracellular loops, a cytoplasmic loop and cytoplasmic N- and C-termini. Many of the key functional differences between connexins arise from specific amino-acid substitutions in the most highly conserved domains: the transmembrane and extr