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: 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