This website uses cookies to ensure you get the best experience on our website.
- Table of Contents
Facts about Sister chromatid cohesion protein PDS5 homolog A.
Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays a significant role in DNA repair. .
Human | |
---|---|
Gene Name: | PDS5A |
Uniprot: | Q29RF7 |
Entrez: | 23244 |
Belongs to: |
---|
PDS5 family |
Cell proliferation-inducing gene 54 protein; DKFZp686B19246; FLJ41012; KIAA0648MGC131948; PDS5; PDS5, regulator of cohesion maintenance, homolog A (S. cerevisiae); PIG54; SCC-112MGC161503; Sister chromatid cohesion protein 112; sister chromatid cohesion protein PDS5 homolog A
Mass (kDA):
150.83 kDA
Human | |
---|---|
Location: | 4p14 |
Sequence: | 4; NC_000004.12 (39822863..39977956, complement) |
Highest level in colon. Low levels in lung, ovary, breast and kidney. Reduced level in renal tumor tissue. Isoform 2 is expressed in kidney.
Nucleus. Associated with chromatin through most of the cell cycle. Dissociates from chromatin in late prophase, reassociates during late telophase.
You are now ready to use the PDS5A marker to detect bovine serum albumin. This article will help you to detect bovine serum albumin. We will also discuss how to clean and record the results. This article will cover all the basics you need to know about the bovine serum albumin marker. It is important to understand its purpose.
Detection methods of the PDS-5A marker are available in the market today. This test uses the cohesin-binding ability of sororin to determine the replication process. Sororin recruits cohesin into chromatin and allows it there to stay for hours. This is a dynamic process, and the interaction of sororin and cohesin requires a previously unknown property of cohesin in the replicated DNA.
Overexpression of PDS5A may cause breast cancer cell migration, proliferation, and invasion. A GEPIA website prediction revealed a link between CDCA5 and PDS5A. Also, western blot analysis confirmed that CDCA5A was positively correlated with PDS5A. These findings suggest that PDS5A/CDCA5 may be a potential target for the treatment of breast carcinoma.
The PDS5B and PDS5A markers are not redundant. They serve complementary roles by activating Chk1 as well as preventing cohesin degrading. The loss of one Pds5 proteins will not compensate for another. This makes the Pds5A marker a good choice for recording the test result. These are just a few examples of Pds5 markers.
Pds5B's N-terminal region is closer to cohesin and DNA interface. This is significant because Pds5B regulates inter-cellular cohesin-DNA interactions, and may also modulate its ATPase activity. The Pds5B marker also inhibits the cohesin escape gate in vitro. The proximity map suggests that Pds5 proteins may be required for cohesin binding to ensure that DNA-protein interaction is maintained.
Pds5B, and PDS5A do not play an essential role in cohesion but they both play important roles for cell adhesion. Both the Pds5B and PDS5A subunits play important roles in cohesion. The Pds5 Subunits may have direct impacts on cohesin's hydrolyzing and ATP-binding activities. They may also need additional molecules or post-translational modification.
The Pds5B mark is a highly-curled protein. It is similar in density to tetrameric cophesin. It is possible Pds5B could have become dissociated during the sample preparation. If this happens, then the Pds5B markers will be absent. During sample preparation, some cohesin complexes are dissociated by the Pds5B markers.
The Pds5B marker can be obtained by co-expressing bonsai trimers with SA1. The Pds5B mark binds to tetrameric compoundes, while the Pds5A marker does not bind to Smc1B-Smc3B dimers. Scc1 is required for interaction between Pds5B and the cohesin dimer. The full-length complexes of these complexes were purified using glycerol density gradient centrifugation. They were then stained with silver.
PMID: 15019998 by Kumar D., et al. SCC-112, a novel cell cycle-regulated molecule, exhibits reduced expression in human renal carcinomas.
PMID: 11076961 by Sumara I., et al. Characterization of vertebrate cohesin complexes and their regulation in prophase.