Antibody News

TRPM8 is a transmembrane homo-tetramer ion channel that is activated by cold temperatures, cooling agents, and menthol stimuli. It belongs to a subgroup within the larger family of TRP cation channels (including the TRPV1 capsaicin receptor) that are named after the melastatin protein. These proteins are also known chanzymes due to their C-terminus enzyme domains. TRPM8 contains a voltage sensor as well as a binding domain for channel agonists such as menthol and icilin. Upon activation, it allows sodium and calcium entry, causing the creation of an action potential through depolarization. It is expressed in sensory neurons where it appears to play a role in neurite outgrowth, signaling, and apoptosis in response to noxious stimuli.

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The protein encoded by SNF5 is a component of the chromatin-remodeling protein complex responsible for relieving repressive chromatin structures by allowing the transcriptional machinery to access targets more effectively. SNF5 has been found to be a tumor suppressor, and mutations within it are associated with some malignant tumors. Two transcript variants encoding different isoforms exist. Scurr’s group published interesting findings on effector proteins in senescence in Cell¹. There, they immunoblotted with the SNF5 antibody to monitor B-Raf and IGFBP7 protein expression levels in several melanoma cell lines, and found that lentiviral-silencing of secreted IGFBP7 does not affect  senescence in melanocytes and fibroblasts.

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. OS9 forms part of the HRD1 ubiquitin ligase complex (SYVN1/HRD1 and SEL1L) which is involved in the retro-translocation of misfolded proteins from the ER to cytosol for ubiquitin-dependent degradation. OS9 has been shown to specifically protect some proteins from this process before maturation, ensuring biological functionality.

MMP2 is a peptidase enzyme that belongs to the large family of matrix metalloproteinases (MMPs) which degrade the extracellular matrix (ECM) with different substrate specificities. Aberrant and unregulated expression of MMPs via deregulation of key negative check controls is strongly associated with increased tumor invasiveness, metastasis potential, and angiogenesis. This uncontrolled behavior is in direct contrast to the tightly controlled physiological systems of embryonic development, tissue remodeling, and rebuilding. MMP2 antibody immunostaining was paired with sophisticated computed tomography as viable prognostic indication assessment method for small lung adenocarcinomas¹.  The Japanese group that did these studies also identified CD34, MMP9, VEGF, and TIMP-2 as other markers. Ribeiro-Silva’s...

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. TLR proteins in general recognize pathogen-associated molecular patterns (PAMPs) present on a diverse range of exogenous and endogenous ligands – including infectious agents - and regulate the cytokine production required for effective immunity development. Specifically, TLR9 detects unmethylated CpG dinucleotides. Studies in human glioblastoma with the TLR9 antibody found varying TLR9 RNA levels, suggesting that treatment with immunostimulating...

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. This was discovered when a 53BP1 antibody was applied to mitotic cells to demonstrate the absence of a full DDR response that was also sensitive to suppression by high levels of cyclin-dependent kinase1 (CDK1) activation. Additionally, the ubiquitination cascade was known to be involved in 53BP1 recruitment to DNA damage sites within cells, but Mallette’s group used a 53BP1 antibody to pinpoint the degradation of the JMJD2A/KDM4A tandem tumor domain via an E3 ubiquitin ligase ...

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.  This leads to nuclear translocation of various NF-kB complexes, predominantly the p50/RelA dimer.  The non-canonical pathway activates the RelB/p52 NF-kB complex using a mechanism that relies on the inducible processing of p100 instead of degradation of IκBα. [1,2]

World DNA Day celebrates the anniversary of the discovery of the double helix and publication of the findings by Watson, Crick, Wilkins and Franklin as well as the completion of the Human Genome Project in 2003. Congress officially declared April 25^th as DNA day to commemorate both scientific achievements. Learn more about DNA in our infographic below.

Resources

1. Science Centres 
   
2. DNAFTB.org 
   
3. ...

The Wnt gene family is made up of structurally related genes encoding secreted signaling proteins. These proteins have been implicated in oncogenesis and developmental processes, such as cell fate regulation and embryogenesis patterning. There is high evolutionary conservation among species for the Wnt5A protein. Rao’s group from China used the Wnt5A antibody in their immunohistochemical expression survey on a wide variety of renal epithelial neoplasms in hopes of determining if Wnt5A is a useful immunohistochemical marker that allows a definitive differential diagnosis between renal oncocytomas and other subtypes within the spectrum of renal cell carcinomas (RCCs)¹. Some interesting neuroscience studies detailing synaptic plasticity and chronic pain were performed with the Wnt5A antibody in HIV patients².

Transient receptor potential A1 (TRPA1) is an ion channel found on the plasma membrane of many cell types that functions in diverse sensory processes such as pain and temperature. The TRPA1 ion channel is specifically expressed in nociceptive neurons, as well as neurons who express the related protein TRPV1. In fact, Brierly et al used a TRPA1 antibody to discover that this ion channel is largely present on smaller neurons vs larger ones (1). A typical inflammatory response instigates tissue repair and eradication of harmful agents after tissue has been damaged. While TRPA1 elicits mostly a positive response, it can also cause chronic inflammation, which can lead to other diseases such as rheumatoid arthritis, chronic itching and asthma (2).

Cell death via apoptosis is a basic cellular function occurring through the cell death receptor family and their ligands which signal through downstream adaptor molecules and the caspase protease family. Caspases have a precursor form composed of a prodomain, and large and small catalytic subunit, and are activated through a cleavage adjacent to an aspartate to liberate units and allow formation of an a2b2 tetramer. Caspase 3 is a cytoplasmic caspase with two isoforms (one acts as a dominant negative inhibitor), and is involved in the activation cascade for apoptosis execution. Caspase 3 cleaves/activates SREBPs, Caspase 7, and Caspase 9. A Caspase 3 antibody was used by Berges and colleagues to assist in their detailed characterizations of...

Osteoprotegerin (OPG) is a secretory glycoprotein that is a family member of the TNF receptor (TNFR) superfamily. Osteoprotegerin protects bone by blocking osteoclastogenesis and increasing bone density. Unlike other TNFRs, osteoprotegerin lacks a transmembrane domain as well as any apparent cell-associated signals. High levels of osteoprotegerin mRNA are found in specialized tissues such as lung, heart, kidney, and placenta. There is evidence that osteoprotegerin plays a role in degenerative arterial disease. Sandra et al used ELISA studies employing the osteoprotegerin antibody with hopes of understanding the bone resorption that occurs with the bone tumor ameloblastoma (1). Their findings seem to suggest that ameloblastoma secretes RANKL and TNF alpha. Some interesting studies looking at bone loss in inflammatory bowel disease (IBD) used the...