The C11orf73 Polyclonal Antibody (PACO8075) is a valuable tool for researchers studying the C11orf73 protein, which has been implicated in various cellular processes and diseases. This antibody, produced in rabbits, exhibits high reactivity with human samples and has been validated for use in Western blot applications. By specifically binding to the C11orf73 protein, this antibody enables precise detection and analysis in different cell types, making it ideal for investigations in molecular biology and disease research.
C11orf73, also known as chromosome 11 open reading frame 73, is a protein with potential roles in gene regulation, cell signaling, and disease development. Its involvement in these processes suggests its relevance in studies related to cancer, genetic disorders, and other pathological conditions. By understanding the function of C11orf73, researchers can uncover new insights into disease mechanisms and potentially identify therapeutic targets for intervention.
chromosome 11 open reading frame 73;C11orf73;FLJ43020;HSPC138;HSPC179;L7RN6 ;
UniProt Protein Function:
C11orf73: Acts as a specific nuclear import carrier for HSP70 proteins following heat-shock stress: acts by mediating the nucleoporin-dependent translocation of ATP-bound HSP70 proteins into the nucleus. HSP70 proteins import is required to protect cells from heat shock damages. Does not translocate ADP-bound HSP70 proteins into the nucleus. Belongs to the OPI10 family. Following heat-shock treatment. Interacts with ATP-bound HSP70 proteins. Interacts with NUP62 and NUP153 (via F-X-F-G repeats)Protein type: Cell development/differentiationChromosomal Location of Human Ortholog: 11q14.2Cellular Component: cell junction; cytosol; intracellular; nucleoplasm; nucleusMolecular Function: Hsp70 protein binding; protein transporter activityBiological Process: protein import into nucleus; protein transport
UniProt Protein Details:
NCBI Summary:
This gene encodes an evolutionarily conserved nuclear transport receptor that mediates heat-shock-induced nuclear import of 70 kDa heat-shock proteins (Hsp70s) through interactions with FG-nucleoporins. The protein mediates transport of the ATP form but not the ADP form of Hsp70 proteins under conditions of heat shock stress. Structural analyses demonstrate that the protein forms an asymmetric homodimer and that the N-terminal domain consists of a jelly-roll/beta-sandwich fold structure that contains hydrophobic pockets involved in FG-nucleoporin recognition. Reduction of RNA expression levels in HeLa cells using small interfering RNAs results in inhibition of heat shock-induced nuclear accumulation of Hsp70s, indicating a role for this gene in regulation of Hsp70 nuclear import during heat shock stress. [provided by RefSeq, Apr 2016]
