Antibodies

p73 has been identified as a long-lost cousin of the p53 tumor suppressor protein. It has high homology with both p53 and with p63, a gene implicated in the maintenance of epithelial stem cells. The presence of significant homology between the DNA-binding domains of p53, p63, and p73 suggest that they have overlapping functions. Targeted disruption of p73 leads to defects hippocampal dysgenesis, hydrocephalus, chronic inflammation, and infections.

The OS9 protein is a lectin/glycoprotein that maintains endoplasmic reticulum (ER) quality control and ER-associated degradation (the so-called ERAD pathway) of newly synthesized proteins. It is essential for the recognition of terminally misfolded non-glycosylated proteins and improperly folded glycoproteins, and binds to them to allow first their retention in the ER, and then second, subsequent transfer to the degradation machinery. The cation-selective channel TRPV4 is OS9's major target.

Caspase 6, also known as Apoptotic protease Mch-2, belongs to the peptidase C14A family. It functions as a downstream enzyme in the caspase activation cascade and is responsible for the execution of apoptosis. Its overexpression promotes programmed cell death.

Diseases associated with CASP6 include thoracic cancer and myocardial infarction.  Among its related super-pathways are DR3 Signaling and Apoptosis and the survival FAS signaling cascade.

The survivin anti-apoptotic protein is the smallest member of a large family of proteins such as X-linked IAP, c-IAP1 and 2, IAP-like protein-2, melanoma IAP, Livin, and NAIP. Survivin regulates basic physiological events such as the cell cycle, tumor progression, fetal development, and cell migration.

The Toll-like receptor 9 (TLR9) protein, also known as CD289, belongs to the family of Toll-like receptor (TLR) proteins which play a large role in pathogen recognition and the activation of innate immunity. Scientists using TLR9 antibodies have found that TLRs are highly conserved from Drosophila to humans, with a high degree of structural and functional homology^1,2.

Glioma-associated oncogene 1 (Gli1) is a transcription factor within the DNA-binding zinc-finger protein family. The Sonic Hedgehog signaling pathway (SHH), which assists in embryonic development and maintaining stem cell populations in adults, activates the Gli1 protein. In the SHH Pathway, the hedgehog ligand binds to patched transmembrane protein receptor (PTC). PTC is an inhibitor of SMO, a protein receptor, and when the hedgehog ligand is present, SMO is not inhibited.

The 53BP1 (p53 binding protein 1) was initially believed to be a p53 transcriptional enhancing partner, but it has now been established as an ataxia telangiectasia mutated (ATM) substrate. As a late DNA damage response (DDR) marker, 53BP1 appears during the telophase and cytokinesis phase of mitotic mammalian cells¹.

GAPDH is a 146 kD tetramer glycolytic pathway metabolic enzyme responsible for reversibly phosphorylating glyceraldehyde 3-phosphate. It may have other possible functions in transcriptional activation. GAPDH is highly expressed due to this housekeeping role, and its prevalent expression has allowed its use as an internal loading control – traditionally for mRNA expression comparisons – but also in protein studies.

NF-kappa-B is a ubiquitous transcription factor involved in several biological processes such as inflammation, immunity, differentiation, cell growth, tumor genesis and apoptosis. Unlike the majority of transcription factors that reside in the nucleus, NFkB is predominantly bound to IkBs protein inhibitors and is located in the cytoplasm. There are two major signaling pathways involved in the activation of NFkB, canonical and non-canonical. [1] In the canonical NF-kB pathway, NF-kB activation is dependent on the inducible degradation of IkBs, particularly IkBa.

Isotype controls are primarily used as negative controls in flow cytometry but they can also be used for immunohistochemistry. They are used to approximate the non-specific target primary antibody binding due to protein-protein interactions, binding to Fc receptors on target cells, non-specific protein-protein interactions, and cell autofluorescence.