What Is MDM2 Antibody?

MDM2 Antibody (SMP14), a monoclonal MDM2 antibody of high quality (also known as HdmX antibody, HDM2 antibody) that can detect the MDM2 protein from mouse, rat, and human. MDM2 Antibody (SMP14), is available in both the non-conjugated anti MDM2 antibody form and multiple conjugated anti MDM2 antibodies forms, including agarose (HRP), PE (FITC) and multiple Alexa Fluor (r) conjugates. 

MDM, also known as murine double minute-2, was first identified in a murine transform system. MDM2 functions to bind to p53 and prevent p53-mediated transactivation cotransfected reporter constructions. MDM2 is expressed in high numbers of human sarcomas. You can know more about MDM2 antibodies online via https://www.bosterbio.com/anti-mdm2-antibody-pa1378-1-boster.html.

Tumor cells that express MDM2 more than normal can tolerate high levels p53 expression. These results suggest that MDM2 expression may be one of the mechanisms by which tumorigenesis can be stopped. MDM2 Antibody (SMP14), is an important reagent in cancer research. The most frequently mutated human cancer gene, p53, has been identified. 

The expression of p53 causes inhibition of cell growth and prevents cells from progressing from the G1 phase to the S phase of their cell cycle. Importantly, p53 is responsible for the arrest of cells during the G1 phase. This happens after cells are exposed to DNA-damaging substances.

MDM2 is a ubiquitin-ligase for P53. It plays a key role in stabilizing p53. MDM2 can be found on chromosome 12 of the q arm. MDM2's interaction with p300 is enhanced by Akt-mediated Phosphorylation at Ser166 and Ser186. This allows MDM2-mediated degradation and ubiquitination of p53. 


Know All About GRP94 Antibody

Glucose regulated protein 94 (GRP94), is an endoplasmic reticulum-resident member of the heat shock protein90 (HSP90). It plays a crucial role in regulating biological functions. This includes chaperoning cellular protein in the ER lumen and maintaining calcium homeostasis. 

Recent reports have highlighted the clinical and functional relevance of GRP94 expression in the progression and metastasis of a variety of cancers. The current review focuses on GRP94's physiological as well as pathophysiological functions in cancer cells. You can know more about GRP94 antibodies through this website.

GRP94, a 803-amino acid protein that belongs to the heat shock protein90 family, is an 803-amino acid protein. It functions as a molecular chaperone and aids in the transport and processing of secreted protein. GRP94 and its N terminal fragment stimulate CTL expansion, maturation and differentiation of human monocyte-derived Dendritic Cells (MDDC). 

It is involved in acquired and innate immunity, maturation, and chemotaxis dendritic cell maturation, Ab production, and cross-priming. GRP94 expression suppressed A23187-induced Apoptosis, and stabilized calcium homeostasis. GRP94 can be found in colon carcinoma or liver metastases cells and human gastric carcinoma BGC-823 cell lines.

Polysomes synthesize secretory proteins and they are translocated to the endoplasmic reticulum. These proteins can be modified in ER by amino-linked glycosylation, disulfide bond formation and folding. To ensure proper protein folding, the ER includes a number of molecular chaperones including Grp94. Grp94, a glucose-regulated protein, has sequence homology with Hsp90.