Disease relevance of LOC494528

• Rat 2 cells stably transformed by murine v-fms (pB5 cells) were infected with retroviruses containing a human cDNA encoding either a full-length human T-cell protein tyrosine phosphatase (TC.PTP) or a truncated form (delta C11.PTP) in which an 11-kDa carboxy-terminal extension had been removed [1].

High impact information on LOC494528

• Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residue [2].
• The established rat thymic epithelial cell line IT-45 R1 produced a polypeptide that resolves as a single band in the region of 11 kDa on NaDodSO4/polyacrylamide gels [3].
• Mimetic peptides corresponding to leucine-rich repeats 1-3, encompassed by a collagen-binding approximately 11-kDa cyanogen bromide fragment of decorin and leucine-rich repeats 4 and 5, previously shown to bind to collagen, were tested for their ability to inhibit collagen bead binding [4].
• These results demonstrate that the particulate cGMP-dependent protein kinase mediates the phosphorylation of the 225-, 132-, and 11-kDa proteins [5].
• The 11-kDa protein is phospholamban based on the characteristic shift in apparent Mr from 11,000 to 27,000 on heating at 37 degrees C rather than boiling prior to electrophoresis [5].

Biological context of LOC494528

• Transfection of COS cells with LARFN5C-Fc cDNA resulted in expression of the predicted protein, and Western blot analysis verified expression of approximately 11 kDa LARFN5C protein in vivo and its developmental regulation [6].

Anatomical context of LOC494528

• The estrone conjugating activity of guinea pig microsomes was similarly activated at lower doses of radiation and declined at higher doses (greater than or equal to 36 megarads), with a target size of 57 +/- 11 kDa [7].
• After a 2-h incubation, PRL-like immunoreactivity in lactating mammary gland medium was composed of 23-, 14-, and 11-kDa forms in the following relative amounts: 65 +/- 9, 17 +/- 1, and 10 +/- 5%, respectively [8].
• C3a exhibits potent chemotactic activity for rat neutrophils, and C3 beta c is a novel basic neutrophil chemoattractant with molecular mass of about 11 kDa, suggesting that both chemoattractants play a role in the neutrophil infiltration into inflammatory site of carrageenin-induced inflammation in rats [9].

Associations of LOC494528 with chemical compounds

• By contrast, T3 promotes incorporation of label into a single major 11 kDa species: this incorporated label is somewhat acid-labile, and the incorporation is abolished by nicotinamide [10].
• Further degradation of the 27 kDa fragment by means of formic acid cleavage at Asp-Pro bonds resulted initially in the formation of two non-immunoreactive fragments of 17 kDa and 11 kDa, indicating that the epitope for 5-B6 has to be localized around the chemical cleavage sites Asp507 and/or Asp510 [11].
• The molecular mass of OR2DSH was determined to be 11 kDa, which is almost the same as those of other heparin derivatives such as 2-O-desulfated heparin (2DSH), 6-O-desulfated heparin (6DSH) and N-desulfated N-reacetylated heparin (NDSNAc-heparin) [12].
• Down-regulated genes included various molecular chaperones, the 11-kDa diazepam binding inhibitor, cyclin D1, and mitochondrial aspartate aminotransferase [13].
• Sodium dodecyl sulfate/gel electrophoresis of the protein produced in this way under non-reducing conditions revealed four protein bands of 18, 16, 14 and 11 kDa [14].

Other interactions of LOC494528

• DFF40 is typically bound to the 45-kDa subunit of DFF (DFF45), and activation of DFF40 may occur as a result of caspase-3-mediated cleavage of DFF45 into 30- and 11-kDa fragments [15].
• Peptide-N-glycosidase F, capable of removing all classes of N-linked oligosaccharides, produced 8 and 11 kDa decreases in NEP 1 and NEP 2, respectively [16].
• Pronase-induced splitting off of a 11 kDa heme-containing fragment of cytochrome b5 did not affect IMP content [17].

Analytical, diagnostic and therapeutic context of LOC494528

• On gel filtration, the apparent M(r) was 11 kDa [18].
• The major component of the 11-22-kDa fraction, photolabelled in an ADP/Ca(2+)-sensitive manner, also migrated at 22 kDa on SDS/PAGE; a minor 11-kDa component was also detected [19].

References