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Please note: We are reviewing Western blot images included in the antibody testing data in our catalog, including those provided by third parties. Unless expressly labeled or annotated as “raw-unedited”, Western blot images included in the antibody testing data in our catalog may have been edited, optimized or otherwise adjusted for presentation.
Sequence of this protein is as follows: IRGPLRAQDL GPQPLELKEA FKLFQIQFNR SYLSPEEHAH RLDIFAHNLA QAQRLQEEDL GTAEFGVTPF SDLTEEEFGQ LYGYRRAAGG VPSMGREIRS EEPEESVPFS CDWRKVAGAI SPIKDQKNCN CCWAMAAAGN IETLWRISFW DFVDVSVQEL LDCGRCGDGC HGGFVWDAFI TVLNNSGLAS EKDYPFQGKV RAHRCHPKKY QKVAWIQDFI MLQNNEHRIA QYLATYGPIT VTINMKPLQL YRKGVIKATP TTCDPQLVDH SVLLVGFGSV KSEEGIWAET VSSQSQPQPP HPTPYWILKN SWGAQWGEKG YFRLHRGSNT CGITKFPLTA RVQKPDMKPR VSCPP
Cathepsin W (lymphopain) and cathepsin F comprise a novel subgroup of cathepsin proteases, and are phylogenetically distinct from other human cathepsins. The cathepsin W gene maps to chromosome 11q13.1 and contains ten exons with introns ranging from 81-119 bp. Cathepsin W protein is expressed specifically in CD8+ T lymphocytes. The expression of cathepsin W first occurs during the differentiation of thyrocytes to CD8+ T lymphocytes, just as the thymocytes cease expression of CD4+ receptors. In transfected Cos-7 and HeLa cells, cathepsin W localizes within the rough endoplasmic reticulum. Cathepsin W contains a unique 21 amino acid peptide insertion between the active site histidine and asparagine residues, in addition to a distictive 8-amino acid carboxy-terminal extension. An extended loop struc-ture in the second or beta-sheet domain and an additional disulfide bind are two of several signature features of cathepsin W. Other features of cathepsin W include an additional cysteine, an S2 pocket and an additional residue. Cathepsin W may exist as a dimer with each monomer forming a disulfide bond.
仅用于科研。不用于诊断过程。未经明确授权不得转售。