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Related ArticlesThe protein encoded by the LAMP2 gene is a member of a family of membrane glycoproteins. This glycoprotein provides selectins with carbohydrate ligands and is thought to play a role in tumor cell metastasis. It may also function in the protection, maintenance, and adhesion of the lysosome. Alternative splicing of the gene produces two known products, LAMP2a and LAMP2b. Isoform LAMP2a is highly expressed in placenta, lung and liver and has low expression in brain and skeletal muscle. The i
This gene was identified based on homology to Pichia pastoris GSA7 and Saccharomyces cerevisiae APG7. In the yeast, the protein appears to be required for fusion of peroxisomal and vacuolar membranes. The protein shows homology to the ATP-binding and catalytic sites of the E1 ubiquitin activating enzymes. [provided by RefSeq, Jan 2009].
RAB proteins are GTPases that regulate vesicular trafficking and reside in specific intracellular compartments. RAB9 has been localized to components of the endocytic/exocytic pathway. It has been implicated in the recycling of membrane receptors, such as the mannose 6-phosphate receptor from early endosomes to the trans Golgi network.
The androgen receptor gene is more than 90 kb long and codes for a protein that has 3 major functional domains: the N-terminal domain, DNA-binding domain, and androgen-binding domain. The protein functions as a steroid-hormone activated transcription factor. Upon binding the hormone ligand, the receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen responsive genes. This gene contains 2 polymorphic trinucleotide r
Members of the GATA family share a conserved zinc finger DNA-binding domain and are capable of binding the WGATAR consensus sequence. GATA-1 is erythroid-specific and is responsible for the regulated transcription of erythroid genes. It is an essential component in the generation of the erythroid lineage. GATA-2 is expressed in embryonic brain and liver, HeLa and endothelial cells, as well as in erythroid cells. Studies with a modified GATA consensus sequence, AGATCTTA, have shown that GATA