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SARS-CoV-2 Spike S1 Protein
|Anti-SARS-CoV-2 Spike S1 Protein Azide Free||CR3022||Detail|
Coronaviruses are positive-sense RNA viruses having an extensive range of natural hosts and typically affect the respiratory system. SARS-CoV-2 (Severe acute respiratory syndrome coronavirus 2) has four structural proteins, known as the S (spike), E (envelope), M (membrane), and N (nucleocapsid) proteins; the N protein holds the RNA genome, and the S, E, and M proteins together create the viral envelope.
The S protein is a large viral transmembrane protein associated in a trimer manner on the virion surface, giving the virion a corona or crown-like appearance. Functionally it is the protein responsible for allowing the virus to attach to and fuse with the membrane of a host cell via the ACE2 protein. The ectodomains in all CoVs S proteins have similar domain organizations, divided into two subunits: the first one, S1, helps in host receptor binding, while the second one, S2, accounts for fusion. It also acts as a critical factor for tissue tropism and the determination of host range. The S protein is one of the proteins of CoVs capable of inducing most important host immune responses.
|Anti-SARS-CoV-2 Nucleoprotein Azide Free||CR3018||Detail|
Coronaviruses are positive-sense RNA viruses having an extensive range of natural hosts and typically affects the respiratory system. SARS-CoV-2 (Severe acute respiratory syndrome coronavirus 2) has four structural proteins, known as the S (spike), E (envelope), M (membrane), and N (nucleocapsid) proteins; the N protein holds the RNA genome, and the S, E, and M proteins together create the viral envelope.
The N protein is multipurpose. It has two domains with different functions depending on the virus cycle. The first domain, located in the N terminal position, mainly acts in complex formation with the viral genome. The second domain, at the terminal C position, allows the self-assembly of the protein and facilitates the interaction of the M protein necessary for the constitution of the virion. In addition to its structural functions, the N protein seems to be involved in vitro on the infected host cell by disrupting these cellular regulatory pathways.
|Anti-Human DLL4 Azide Free||B-D59||Detail|
|Anti-Human DLL4 Unconjugated||B-D59||Detail|
Delta-like protein 4 (DLL4) is a type I membrane protein belonging to the Notch ligands family. It is one of the growth factors for tumors; involved in cell differentiation; reduced endothelial cells migration, proliferation and sprouting; modulates smooth muscle cells differentiation and maturation, increased vessel sprouting; inhibited tumor growth. Although Dll4 is commonly up-regulated preferentially in tumor vasculature compared with normal vasculature, the mechanisms are still poorly understood.
Previously, Dll4 itself, FGF (fibroblast growth factor), VEGF (vascular endothelial growth factor) and hypoxia were shown to be important in angiogenesis but more recently, another layer of interactions has been found. These include a pathway via angiopoietin-1/Tie2, involving Notch and DLL4 interaction. This has become a major focus in the development of anticancer therapy.
|Anti-Human IL1RAP Azide Free||B-L43||Detail|
|Anti-Human IL1RAP Azide Free||B-R58||Detail|
|Anti-Human IL1RAP Unconjugated||B-L43||Detail|
|Anti-Human IL1RAP Unconjugated||B-R58||Detail|
IL-1 Receptor Accessory Protein (IL-1 RAcP - IL-1RAP - IL-1 R3) is a ubiquitously expressed 70-90 kDa member of the IL-1R family having an extracellular domain containing three Ig-like C2 type domains, a transmembrane region and a cytoplasmic portion with a TIR domain. There are two isoforms identified due to alternative splicing, membrane-bound and soluble forms.
IL-1RAP forms a heterodimer with IL-1R1, IL-1RL1 (also known as ST2, IL-1R4), or IL-1Rrp2 (IL-1R6) and even if it does not directly bind to ligands, it acts as a co-receptor for IL-1, IL-33, and IL-36. This allows IL-1RAP to be a key mediator of vastly different immunologic outcomes.
In chronic myelogenous leukemia and acute myeloid leukemia, gene expression profiling studies have revealed, IL1RAP as a cell-surface biomarker that is expressed by the leukemic but not the normal CD34þ/CD38 hematopoietic stem cell (HSC) compartment.
|Anti-Human CD64 Azide Free||B-T44||Detail|
|Anti-Human CD64 Unconjugated||B-T44||Detail|
CD64 is membrane glycoprotein known as an Fc receptor that binds IgG-type antibodies with high affinity. CD64 is constitutively found on only macrophages and monocytes, but treatment of polymorphonuclear leukocytes with cytokines like IFNγ and G-CSF can induce CD64 expression on these cells.
Four different classes of Fc receptors have been defined: FcγRI (CD64), FcγRII (CD32), FcγRIII (CD16), and FcγRIV. Whereas FcγRI displays high affinity for the antibody-constant region and restricted isotype specificity, FcγRII and FcγRIII have low affinity for the Fc region of IgG but a broader isotype binding pattern.
The Fc receptors link the humoral and cellular branches of the immune system and are key players setting thresholds for B cell activation, regulating the maturation of dendritic cells, and coupling the exquisite specificity of the antibody response to innate effector pathways, such as phagocytosis, antibody-dependent cellular cytotoxicity, and the recruitment and activation of inflammatory cells