Protein Detection With Elisa

Description: The most affordable qPCR Detection Kit for SARS-CoV-2 on the market.abm’s GenomeCoV19 Detection Kit is a real-time reverse transcription-polymerase chain reaction (RT-qPCR) test intended for the qualitative detection of RNA from SARS-CoV-2 in human nasopharyngeal and oropharyngeal swab specimens from individuals suspected of COVID-19 by their healthcare provider. Our GenomeCoV19 Detection Kit is the most affordable qPCR detection kit on the market at only $1.77 USD/test (limited time pricing for US customers only).This kit is widely used in Europe under the CE-IVD certification and is listed by U.S. Food and Drug Administration (FDA) for distribution in the USA, under Section IV.C.

Description: The most affordable qPCR Detection Kit for SARS-CoV-2 on the market.abm’s GenomeCoV19 Detection Kit is a real-time reverse transcription-polymerase chain reaction (RT-qPCR) test intended for the qualitative detection of RNA from SARS-CoV-2 in human nasopharyngeal and oropharyngeal swab specimens from individuals suspected of COVID-19 by their healthcare provider. Our GenomeCoV19 Detection Kit is the most affordable qPCR detection kit on the market at only $1.77 USD/test (limited time pricing for US customers only).This kit is widely used in Europe under the CE-IVD certification and is listed by U.S. Food and Drug Administration (FDA) for distribution in the USA, under Section IV.C.

Description: Senescence Detection Kit for use in the research laboratory

Description: Members of the IRAK (IL-1R-associated kinase)/Pelle family play a major role in IL-1R/TLR mediated inflammatory responses and in innate immunity. IRAK and IRAK-2 regulate the activity of a signaling cascade that mediates the activation of NF-κB and MAP kinase. IRAK-4 interacts with and phosphorylates IRAK, while IRAK-M is thought to inhibit the recruitment and activation of IRAK-4 and IRAK. The importance of the IRAK family in inflammation and immunity is illustrated by the fact that animals lacking IRAK-4 are impaired in their responses to viral and bacterial challenges and are completely resistant to LPS challenge.;;For images please see PDF data sheet

Description: Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The TLRs act through adaptor molecules to activate various kinases and transcription factors so the organism can respond to potential infection. These adaptor molecules include MyD88, TIRAP, TIRP, TOLLIP, and TRIF. These molecules interact with and activate the IL-1R-associated kinase (IRAK) family, which then activates TNF receptor associated factor (TRAF)-6, and ultimately leads to the activation of NF-κB. While most TLRs utilize more than one adaptor, certain adaptor molecules are essential for individual TLR signaling, e.g., TLR4 signaling is dependent on TIRP expression.;;For images please see PDF data sheet

Description: Antigen stimulation of immune cells triggers Ca++ entry through Ca++ release-activated Ca++ (CRAC) channels. The ORAI family is a recently identified set of proteins that are essential components of these CRAC channels. A missense mutation in the ORAI1 protein in humans is the cause of one form of hereditary severe combined immune deficiency (SCID) which results in ablated T-cell Ca++ entry. It has been suggested that ORAI1 functions as a highly selective Ca++ plasma membrane channel that is gated through interactions with the stromal interaction molecule 1 (STIM1), the store-activated endoplasmic reticulum Ca++ sensor. Like ORAI1, ORAI2 also functions as a highly selective Ca++ plasma membrane channel that is gated through interactions with STIM1, although at a lesser efficacy than ORAI1. Although ORAI3 can also function as Ca++ plasma membrane channel, ORAI3 channels failed to produce detectable Ca++ selective currents in cells co-transfected with ORAI3 and STIM1, indicating that ORAI3 channels undergo a lesser degree of depotentiation than ORAI1 or ORAI2. Na+ currents through ORAI1, 2 and 3 channels were equally inhibited by extracellular Ca++, indicating that each have similar affinities for Ca++ within the selectivity filter. STIM1, in its function as a Ca++ sensor and an activator of CRAC channels, migrates to the plasma membrane from endoplasmic reticulum-like sites which act as cellular Ca++ stores. A related molecule, STIM2, inhibits the STIM1-mediated store-operated Ca++ entry, and can form complexes with STIM1, suggesting these two proteins may play a coordinated role in controlling Ca++ entry. The ORAI antibodies are predicted to have no cross-reactivity to the other ORAI proteins. Similarly, the STIM antibodies will not cross-react with the other STIM protein.;;For images please see PDF data sheet

Description: Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. Grik1, also known as glutamate receptor 5, belongs to the kainate family of glutamate receptors, which are composed of four subunits and function as ligand-activated ion channels. Grik1 is expressed in GABAergic interneurons of the hippocampus and are thought to participate in the formation of various subtypes of kainate receptors with Grik2 and Grik5/KA2. Stimulation of Grik1 leads to intracellular calcium release and activation of protein kinase C. Excessive activation has been associated with psychiatric, neurological and neurodegenerative diseases. Grik2, also known as glutamate receptor 6, may be associated with autosomal recessive mental retardation and possibly other neurological disorders such as schizophrenia. Numerous isoforms of Grik2 are known to exist and may be subject to RNA editing within the second transmembrane domain, which is thought to alter the properties of ion flow. Grik3, also known as glutamate receptor 7, has recently been shown to be an essential subunit of presynaptic kainate autoreceptors at hippocampal mossy fiber synapses as grik3-null mice show significantly reduced short- and long-term synaptic potentiation. Grik4 codes for the KA1 subunit of kainate-type ionotropic gluatamate receptors; mutations in this gene show significant association with both schizophrenia and bipolar disorder. Grik5, also known as kainate-preferring glutamate receptor subunit KA2, does not form homomeric channels, but instead forms heteromers with Grik2. In Grik2- but not Grik1-null mice, Grik5 surface expression is greatly reduced in neurons, indicating that Grik2/Grik5 heteromers are required for exit from the endoplasmic reticulum to the cell surface. ;;For images please see PDF data sheet

Description: The members of the SAP90/PSD-95-associated protein (SAPAP) family (also known as the DLGAP family) specifically interact with PSD-95/SAP90, a membrane-associated guanylate kinase localized at postsynaptic density (PSD) in neuronal cells. The SAPAP proteins are thought to be adaptor proteins that also interact with different synaptic scaffolding proteins, cytoskeletal and signaling components, such as focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (PYK2). SAPAP1, -2 and -4 mRNA are targeted to cell bodies, whereas SAPAP3 mRNA is detected mainly in cell bodies. SAPAP1 protein however, is targeted to the synapse and is not reliant on the synaptic localization of PSD-95 or the synaptic scaffolding molecule (S-SCAM). SAPAP3 protein is targeted to dendrites. Recent experiments have suggested that SAPAP3 may be involved in obsessive-compulsive disorder (OCD), as mice lacking SAPAP3 exhibited OCD-like symptoms which could be relieved by lentiviral-mediated selective expression of SAPAP3 in the striatum of SAPAP3-mutant mice. Multiple isoforms of the SAPAP proteins are known to exist.;;For images please see PDF data sheet

Description: Junctional complexes between the plasma membrane (PM) and endoplasmic/sarcoplasmic reticulum (ER/SR) are a common feature of all excitable cell types and mediate cross talk between cell surface and intracellular ion channels. Junctophilins (JPs) are important components of the junctional complexes. JPs are composed of a carboxy-terminal hydrophobic segment spanning the ER/SR membrane and a remaining cytoplasmic domain that shows specific affinity for the PM. Four JPs have been identified as tissue-specific subtypes derived from different genes: JPH1 is expressed in skeletal muscle, JPH2 is detected throughout all muscle cell types, and JPH3 and JPH4 are predominantly expressed in the brain and contribute to the subsurface cistern formation in neurons. JPH1 is essential for stabilizing the T-tubule and SR membranes to form junctions and provide an environment for the assembly of receptors such as the ryanodine receptor type 1 (RyR1). JPH2-null mice died of embryonic cardiac arrest and human patients with mutations in the JPH2 gene showed hypertrophic cardiomyopathy, demonstrating the importance of this protein. Mice lacking both JPH3 and JPH4 subtypes exhibit serious symptoms such as impaired learning and memory and are accompanied by abnormal nervous functions. A repeat expansion in JPH3 is associated with Huntington disease-like 2. Multiple isoforms of the JPH proteins are known to exist.;;For images please see PDF data sheet

Description: Matrilins (MATNs) are a family of non-collagenous extra-cellular matrix (ECM) proteins consisting of four known members that have been proposed to play key roles in modulating cellular phenotypes during chondrogenesis of mesenchymal stem cells (MSCs). MATN1 and MATN3 are expressed specifically in cartilage and are among the most up-regulated ECM proteins during chondrogenesis. MATN1 is composed of two Willebrand Factor A (vWFA) domains separated by one EGF-like domain, whereas MATN3 is composed of a single N-terminal vWFA domain followed by four epidermal growth factor (EGF) repeats and a coiled-coil domain. MATN1 or MATN3 may play a role in modulating chondrogenesis during the chondrocyte differentiation process. Mutations of MATN1 have been associated with variety of inherited chondrodysplasias, while aberrant expression and processing of MATN3 are hallmarks of conventional cartilaginous neoplasms. The MATN1 promoter region has also been shown to be associated with both susceptibility and disease progression in Adolescent idiopathic scoliosis. Other studies indicate that MATN2 is a permissive substrate for axonal growth and cell migration, and it is required for successful nerve regeneration, while MATN4 could serve as an odontoblast differentiation marker, e.g. in odontoblast stem cell research.;;For images please see PDF data sheet