Immunology Antibodies

<p>Ova (323-339) is an epitope of interest from egg white albumen, which is widely used in allergy research. Ovalbumin is a glycoprotein that is sufficiently large and complex to be mildly immunogenic. It has been demonstrated that ovalbumin contains B-cell epitopes which are recognized by specific IgE antibodies, and CD4 T cell epitopes restricted by the MHC I-Ad molecule in mice and by HLA-D molecule in human.OVA (323-339) can be used to study binding of class II MHC-peptide and T-cell activation in PBMCs by ELISPOT assays. This method quantifies peptide-epitope specificity and IFN-γ releasing effector cells. It has been shown that OVA (323-339) was responsible for 25-35% of T-cell response of isolated BALB/c mouse. An investigation has demonstrated that OVA and OVA (323-339) induced similar lung inflammation and a Th2-like dominant immune response in mouse model.</p>

Arginase antibody was raised in rabbit using arginase isolated from bovine liver as the immunogen.

Rabbit IgG protein is a versatile antibody that plays a crucial role in various biological processes. It is commonly used in Life Sciences research, diagnostics, and therapeutic applications. Rabbit IgG protein exhibits high affinity and specificity for its target antigen, making it an excellent tool for detecting and quantifying specific molecules in samples.

<p>PD-1 inhibitors and PD-L1 inhibitors are a group of checkpoint inhibitors being developed for the treatment of cancer.PD-1 and its ligand PD-L1 are critical in regulating T cell activation, tolerance and immunopathology. PD-1 is an immune checkpoint and guards against autoimmunity through two mechanisms. First, it promotes apoptosis of antigen-specific T-cells in lymph nodes. Second, it reduces apoptosis in regulatory T cells. Several types of cancer cells overexpress PD-L1 in order to escape from the PD-1/PD-L1 immunosurveillance mechanism. In this way, Human PD - L1 inhibitor V could be used in the treatment of cancers that overexpress PD-L1.</p>

<p>Annexin A1 (2-12) is derived from the Annexin A1 protein which is a member of the Ca2+ dependent phospholipid binding protein family of Annexins A1 to A13. Structurally Annexin is comprised of a C-terminal core region and an N-terminal region. Calcium binding sites featured in the core region allow Annexin A1 to bind to cell membranes to induce membrane aggregation in a calcium dependent manner. Furthermore Annexin A1's N-terminal region performs extracellular signalling through forming complexes with SH2 domain containing proteins. Different lengths of the Annexin family's N-terminus contributes to how the Annexins effect key processes such as cell proliferation, apoptosis, growth and differentiation.Annexin A1 can be categorised as being both anti-inflammatory and pro-inflammatory. One example of how Annexin A1 demonstrates anti-inflammatory properties is through activating the formyl peptide receptor family's (FGRs) downstream cascade. Consequently the extracellular regulated kinase (ERK) and mitogen-activated protein kinase (MAPK) are phosphorylated, causing subsequent transcription factors involved in the regulation of T cells to generate anti-inflammatory effects. Another is through inhibiting phospholipase A2 which prevents the release of inflammatory factors and the formation of arachidonic acid precursors. This property has contributed to inflammation studies such as where the inhibition of pro-inflammatory prostaglandins by Annexin A1 was used to investigate leukocyte aggregation.During its anti-inflammatory role Annexin A1 uses the active peptide Ac2-26 located on its N-terminus. It is evident Annexin A1 can be labelled as being pro-inflammatory due to it inducing pro-inflammatory cytokines, following its phosphorylation by PKC. This results in its translocation into the nucleus of BV-2 microglial cells.</p>

Pyruvate kinase antibody (IgG fraction) was raised in goat using pyruvate kinase isolated from rabbit Muscle as the immunogen.

<p>Tetanus Toxin P2 (830 - 844) is a protein that is derived from the single-chain polypeptide neurotoxin produced by Clostridium tetani. The neurotoxins produced by Clostridium tetani are among the most potent molecules known to humankind. Once in the body, the toxin binds to the basal lamina at the neuromuscular junction. From here, the toxin is transported to inhibitory interneurons in the spinal cord, where it prevents the release of neurotransmitters, which causes spastic paralysis.The P2 protein has antigenic properties that are reflective of the neurotoxin released by Clostridium tetani. Therefore, P2 is a suitable epitopes for CD4+ T cells and can be used to stimulate the release of IFNg, which is a cytokine that promotes macrophage activity and coordinates lymphocyte endothelium interactions.</p>

<p>SMAP -18 is a truncated form of sheep myeloid anti-microbial peptide-29 (SMAP-29). SMAP-29 displays extremely high anti-microbial activity against fungi and gram-negative bacteria including Pseudomonas strains and multidrug-resistant pathogens, however it also has high cytotoxic activity to human cells. The carboxyl terminal is more hydrophobic and may be responsible for higher hemolytic activity of SMAP-29, whereas the anti-microbial activity has been attributed to the N-terminal amphipathic alpha-helix region (residues 1-18). SMAP-18 displays much higher cell selectivity as compared to parental SMAP-29 because of their decreased hemolytic activity and retained anti-microbial activity.The cathelicidins are a large family of structurally diverse host defence peptide (HDP- formerly called antimicrobial peptides) found in mammalian species including humans. All members of the cathelicidin family contain an N-terminal cathelin domain and a C-terminal domain of varied structure that displays anti-microbial activity.</p>

<p>Myocarditis is an inflammatory heart disease often associated with a previous viral infection. Evidence has suggested that myocarditis may be due to autoimmune responses directed against cardiac tissue. The inflammatory immune response caused after infection may break tolerance by mechanisms of molecular mimicry, bystander activation, and loss of immune regulation. Experimental autoimmune myocarditis (EAM) is a model of inflammatory heart disease generated by immunizing susceptible rats or mice with cardiac myosin or its myocarditic epitopes. In the EAM model, cellular infiltrates consist primarily of T cells and macrophages, and T lymphocytes responsive to cardiac myosin can transfer disease. Cardiac myosin is a large peptide, which is composed of two H chains and two pairs of L chains. Proteolysis of myosin yields three subfragments including a globular head or subfragment 1 (S1) region, an alpha helical coiled coil rod comprised of subfragment 2 (S2), and light meromyosin (LMM). In the Lewis rat, the S2 subfragment has been shown to produce the most severe myocarditis.</p>

<p>PMX 53 is a potent antagonist of CD88, a G protein-coupled receptor for C5a (complement protein). C5a is a protein fragment released from cleavage of complement component C5 by protease C5-convertase into C5a and C5b fragments. C5a, the other cleavage product of C5, acts as a highly inflammatory peptide, encouraging complement activation, formation of the MAC, attraction of innate immune cells, and histamine release involved in allergic responses. The origin of C5 is in the hepatocyte, but its synthesis can also be found in macrophages, where it may cause local increase of C5a. C5a is a chemotactic agent and an anaphylatoxin- it is essential in the innate immunity but it is also linked with the adaptive immunity. The increased production of C5a is connected with a number of inflammatory diseases.By antagonising the C5a receptor, PMX can be used to modulate inflammatory responses, obesity, development and cancers.</p>

<p>SPA4 is a surfactant protein-A (SP-A)-derived peptide which is an antagonist of toll-like receptor-4 (TLR4). SP-A and TLR4 have been identified as important pathogen-pattern recognition receptors (PPRRs). SP-A represents the majority of SPs and plays a key role in fighting pathogens and down-regulating inflammation, whereas TLR4 recognises pathogens and endogenous stress proteins and induces the inflammatory and adaptive immune responses.Over-activation of TLR4 induces inflammatory response via NF-KB and TNF-α cytokine. SPA4 has been shown to bind to TLR4 and inhibit the release of TNF-α in response to the most potent TLR4-ligand: Gram-negative bacteria-derived lipopolysaccharide (LPS), however SPA4 does not interfere with LPS binding to TLR4. The suppression of LPS-TLR4 signalling by SPA4 peptide alleviates inflammatory response.</p>

Purified Human IgM protein (Fab mu)

Human IgM protein (Fab mu) (HRP) conjugate

<p>The AH1 peptide is a H2-Ld-restricted epitope derived from the sequence of the gp70 envelope protein of the ecotropic mammalian C-type retrovirus, murine leukaemia virus (MuLV, emv-1).The envelope gene products of MuLV are expressed in a variety of tumour cells, including B16 melanoma, lymphomas and leukaemia's. AH1 peptide is a tumour-associated antigen and is highly expressed on CT26 and C51 tumour cells.</p>

<p>A20FMDV2, a peptide derived from the foot and mouth disease virus, inhibits the epithelial-specific integrin alphavβ6 and here is labelled with 4-fluorobenzoyl as the light version of the PET ligand 4-[18F]Fluorobenzoyl A20FMDV2 which can be used for in vivo imaging.</p>

<p>Heat shock protein gp96 inhibitor which binds to and antagonizes gp96 mediated lipopolysaccharide (LPS) induced cytokine production. Anti-inflammatory in a number of in vivo and in vitro models.</p>

<p>Protease activated receptors (PARs) are a distinctive four-member family of seven transmembrane G protein-coupled receptors (GPCRs) widely expressed in inflammatory cells. PARs are cleaved by certain serine proteases to expose a tethered ligand domain, this ligand domain then binds to and activates the receptors to initiate multiple signalling cascades. These PAR-activating proteases therefore represent PAR agonists. This PAR-4 agonist peptide represents the N-terminal sequence of the 'tethered ligand' and is therefore capable of activating the receptor independently of N-terminal proteolysis.</p>

Protein A antibody (biotin) was raised in goat using Protein A [Staphylococcus aureus] as the immunogen.

<p>C5a receptor peptide antagonist which can ameliorate experimentally-induced colon inflammation in mice. It can also reduce fibrillar amyloid deposits, decrease hyperphosphorylated tau levels and rescue cognitive function in a mouse model of Alzheimer's Disease. Also improves hindlimb grip strength and slows disease progression in the hSOD1G93A-mouse model of amyotrophic lateral sclerosis. Orally active and brain penetrant.</p>

<p>Ara h 6 is one of the major allergenic proteins from peanut (Arachis hypogaea) which contains approximately 13 potential allergenic proteins. Ara h 6 is a member of the 2S albumins (conglutinins) belonging to the prolamin superfamily which also includes Ara h 2. 2S albumins contain major food allergens from seeds of many mono- and dicotyledon plants and share a common compact structure that renders the proteins highly resistant to proteolysis.Ara h 6 contains multiple disulphide-bridged cysteine residues, resulting in a tightly coiled, heat-stable, protease resistant core structure that may be important for allergenicity. In mouse models Ara h 2 and Ara h 6 are the main cause of effector responses such as mast cell degranulation and anaphylaxis.This peptide represents a tryptic peptide of Ara h 6. The phenylalanine residue at position 11 of this peptide is isotopically labelled with carbon-13 (9) and nitrogen-15 (1), giving this peptide a mass increase of 10 compared to the unlabelled peptide.</p>