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Related ArticlesThis gene encodes a transmembrane receptor that is associated with lysosomes. The encoded protein, also known as E3 protein, may play a role in hematopoiesis. [provided by RefSeq, Feb 2009]
KLC2 is a 622 amino acid protein that contains six TPR repeats and belongs to the kinesin light chain family. Existing in an oligomeric complex composed of two light and two heavy chain kinesin proteins, KLC2 plays a role in coupling organelle transport with ATPase activity. The gene encoding KLC2 maps to human chromosome 11, which houses over 1,400 genes and comprises nearly 4% of the human genome.
Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase related apoptosis inducing protein kinases). DRAKs contain an N terminal kinase domain and a C terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs
Semaphorin 7a is required for central and peripheral axon growth and is required for proper axon tract formation during embryonic development. Semaphorin 7a is also involved in modulating immune function. Semaphorin 7a expression is highest in the brain and increases in late embryonic and postnatal stages. The Semaphorins constitute a large family of secreted and membrane-tethered cell signaling molecules. They have functions in neural development, immunology, cardiac growth, vascular deve
NR1D1, a NR1 Thyroid Hormone-Like Receptor, is encoded by the same genomic locus as, but transcribed from the opposite strand of, Thyroid Hormone Receptor Alpha (TR Alpha). NR1D1 is a target of Nuclear Receptor ROR Alpha and a transcription regulator that has been shown to affect myocyte differentiation, adipogenesis, and lipoprotein metabolism. Mice lacking NR1D1 show abnormal postnatal cerebellar development. NR1D1 expression has been documented in human skeletal muscle and a variety of mo
BPGM (2,3-bisphosphoglycerate mutase) is a 259 amino acid protein that belongs to the phosphoglycerate mutase family and exists as a homodimer that plays a crucial role in the regulation of hemoglobin oxygen. Specifically, BPGM catalyzes the conversion of 3-phospho-D-glyceroyl phosphate to 2,3-bisphospho-D-glycerate (2,3-BPG), a reaction that is essential for controlling the concentration of 2,3-BPG within the cell. The gene encoding BPGM maps to human chromosome 7, which houses over 1,000 gen