New products
A continuous and high-level Research & Development activity to match the needs of our customers and supply the best products.
- Regular marketing of new products
- New targets, new formats, new immunoassays for always innovative products
- Custom services for monoclonal antibodies or immunoassays
New Catalogue 2024
Click and discover...
December 2022
New Antibodies
| Anti-Human BCMA Azide Free B-B54 | Detail |
| Anti-Human BCMA Unconjugated B-B54 | Detail |
New Recombinant proteins |
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| Recombinant Human B Cell Maturation Protein (BCMA) Detail | |
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B-cell maturation antigen (BCMA), also known as tumor necrosis factor receptor superfamily member 17 (TNFRSF17), is a receptor preferentially expressed in mature B lymphocytes, and is important for B cell development and autoimmune response. BCMA, along with two related TNFR superfamily B-cell activation factor receptor (BAFF-R) and transmembrane activator and calcium modulator and cyclophilin ligand interactor (TACI), critically regulate B cell proliferation and survival, as well as maturation and differentiation into plasma cells (1). BCMA is highly expressed on the surface of the malignant plasma from patients with multiple myeloma (mm). BCMA is now clearly recognized as promising novel target for novel mm therapies (ADCC, CAR-T cells, bispecific T-cell engager (1, 2). Accelerate your research and development on this new target of interest with the Diaclone range of related to BCMA products:
(1) Cho S-F, Anderson KC and Tai Y-T (2018) Targeting B Cell Maturation Antigen (BCMA) in Multiple Myeloma: Potential Uses of BCMA-Based Immunotherapy. Front. Immunol. 9:1821. doi: 10.3389/fimmu.2018.01821 (2) Shah, N., Chari, A., Scott, E. et al. B-cell maturation antigen (BCMA) in multiple myeloma: rationale for targeting and current therapeutic approaches. Leukemia 34, 985–1005 (2020). https://doi.org/10.1038/s41375-020-0734-z |
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| Anti-Human CX3CL1 Azide Free B-F51 | Detail |
| Anti-Human CX3CL1 Unconjugated B-F51 | Detail |
| Anti-Human CX3CL1 Azide Free B-K49 | Detail |
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CX3CL1 / Fractalkine is a membrane protein of 373 amino acids, containing multiple domains and is the only known member of the CX3C chemokine family. A soluble (90 kD) version of this chemokine has also been observed. Soluble CX3CL1 potently chemoattracts T cells and monocytes, while the cell-bound chemokine promotes strong adhesion of leukocytes to activated endothelial cells, where it is primarily expressed. CX3CL1 elicits its adhesive and migratory functions by interacting with the chemokine receptor CX3CR1. Fractalkine is found commonly throughout the brain, particularly in neural cells, and its receptor is known to be present on microglial cells. It has been found fractalkine could be essential for microglial cell migration. CX3CL1 is also up-regulated in the hippocampus during a brief temporal window following spatial learning, the purpose of which may be to regulate glutamate-mediated neurotransmission tone. This indicates a possible role for the chemokine in the protective plasticity process of synaptic scaling. |
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| Anti-Human CD48 Azide Free B-P59 | Detail |
| Anti-Human CD48 Unconjugated B-P59 | Detail |
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The CD48 is a 47 kDa protein heavily glycosylated, with five possible asparagine-linked glycosylation sites [Rudd PM (1999) J. Mol. Biol. 293 (2):351–66]. It is expressed on all peripheral blood lymphocytes (PBL) including T cells and monocytes [Vaughan HA (1983) Transpl 36(4):446–50]. It’s a CD2 subfamily member, also known as B-lymphocyte activation marker (BLAST-1) or signalling lymphocytic activation molecule 2 (SLAMF2) [Elishmerenia M (2011) International J Bioch & cell biol, 43(1)25-28]. A soluble form is described and could be a biomarker in some diseases like leukemia, arthritis or asthma [Smith GM (1997) J Clin Immunol 17(6):502-9] [Breuer O (2018) J Immunol Res Sep16]. The CD48 is involved in a wide variety of innate and adaptive immune responses, ranging from granulocyte activity and allergic inflammation to T cell activation and autoimmunity, to CTL or NK function and antimicrobial immunity [McArdel, SL (2016) Clin Immunol. 164:10–20]. Tumor infiltration by CD48+ cells has been described as a good prognostic and its high expression in acute myeloid leukemia is correlated with good pronostic [Wang Z (2020) Clin Sci. 31;134(2):261-271]. |
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New ELISpot format
| Human IFN-γ EasySplit ELISpot Kit | Detail |
| Murine IFN-γ EasySplit ELISpot Kit | Detail |
Diaclone has decided to launch a new line for its Human & Murine IFN-γ ELISpot kits aimed to be used by researchers who run a limited number of wells at the same time.
The EasySplit ELISpot Kit includes everything you need to easily run your assay without wasting material:
- Precoated strip plate
- Detection biotinylated antibody
- Streptavidin Alkaline Phosphatase Conjugate
- Bovine Serum Albumin
- Ready-to-use BCIP/NBT Substrate Buffer
November 2022
New Antibodies
| Anti-Human LRRC15 Azide Free B-G53 | Detail |
| Anti-Human LRRC15 Unconjugated B-G53 | Detail |
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LRRC15 or Leucine-rich repeat-containing protein 15 is a 581 amino acid type I membrane protein with extracellular domain of 517 aa (pro-peptide de 21aa) and no obvious intracellular signaling domains. It has recently been reported as a marker of cancer-associated fibroblasts [Purcell J.W (2018) Cancer Res. 78:4059 - 4072]. This protein has been found to be highly expressed on CAFs within the tumor stroma of many tumor types [Krishnamurty AT , (2022) Nature, 611(7934):148-154 ; Dominguez C (2020) Cancer Discov, 10(2):232-253], as well as directly on cancer cells in tumors of mesenchymal origin such as sarcomas. The expression of LRRC15 is upregulated by the pro-inflammatory cytokine TGFβ. Overexpression of LRRC15 is positively correlated with grade and independently associated with adverse outcome [Ben-Ami E (2020) Cancers (Basel) 12(3): 757]. |
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New Recombinant proteins
Recombinant Human Leucine-Rich Repeat-Containing Protein 15 (LRRC15) Detail
LRRC15 or Leucine-rich repeat-containing protein 15 is a 581 amino acid type I membrane protein with extracellular domain of 517 aa (pro-peptide de 21aa) and no obvious intracellular signaling domains. It has recently been reported as a marker of cancer-associated fibroblasts [Purcell J.W (2018) Cancer Res. 78:4059 - 4072]. This protein has been found to be highly expressed on CAFs within the tumor stroma of many tumor types [Krishnamurty AT , (2022) Nature, 611(7934):148-154 ; Dominguez C (2020) Cancer Discov, 10(2):232-253], as well as directly on cancer cells in tumors of mesenchymal origin such as sarcomas. The expression of LRRC15 is upregulated by the pro-inflammatory cytokine TGFβ. Overexpression of LRRC15 is positively correlated with grade and independently associated with adverse outcome [Ben-Ami E (2020) Cancers (Basel) 12(3): 757].
New Immunoassay Products
Human RANTES ELISA kit Detail
RANTES (regulated on activation, normal T cell expressed and secreted) or chemokine (C-C motif) ligand 5 (also CCL5) is a chemotactic cytokine which in humans is encoded by the CCL5 gene.
It is chemotactic for T cells, eosinophils, and basophils, and plays an active role in recruiting leukocytes into inflammatory sites. With the help of IL-2 and IFN-γ released by T cells, CCL5 induces the proliferation and activation of certain natural-killer (NK) cells. It is also an HIV-suppressive factor released from CD8+ T cells.
Human ST2 ELISA kit Detail
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Human ST2 (also known as IL1RL1) consists of a 310 amino acid (aa) extracellular domain (ECD) with three Ig like domains, a 21 aa transmembrane segment, and a 207 aa cytoplasmic domain with an intracellular TIR domain. Alternate splicing of the 120 kDa human ST2 generates a soluble 60 kDa isoform that lacks the transmembrane and cytoplasmic regions as well as an isoform that additionally lacks the third Ig like domain. The IL-33 binding induces the receptor consisting of ST2 transmembrane and IL-1RAP (IL-1R accessory protein) and activates the MyD88/NF-κB signaling pathway to enhance mast cell, Th2, regulatory T cell (Treg), and innate lymphoid cell type 2 functions. Soluble ST2 can also bind IL-33 directly and act as a decoy receptor, inhibiting its binding to membrane-bound ST2 and subsequent signaling. sST2 levels are increased in patients with active inflammatory bowel disease, acute cardiac and small bowel transplant allograft rejection, colon and gastric cancers, gut mucosal damage during viral infection, pulmonary disease, heart disease, and graft-versus-host disease. Recently, sST2 has been shown to be secreted by intestinal pro-inflammatory T cells during gut inflammation; on the contrary, protective ST2-expressing Tregs are decreased, implicating that ST2/IL-33 signaling may play an important role in intestinal disease. Moreover, sST2 has emerged as a novel cardiovascular biomarker for the presence of ventricular biomechanical overload. IL-33/ST2 unanticipated role in cardiovascular disease has been demonstrated. IL-33/ST2 not only represents a promising cardiovascular biomarker but also a novel mechanism of intramyocardial fibroblast–cardiomyocyte communication that may prove to be a therapeutic target for the prevention of heart failure. |
Concentrations of sST2 have been implicated in the presence and severity of heart failure with standard value for prognostication and treatment monitoring. And recently, interesting studies associates ST2 and Alzheimer’s disease.
Human EpCam ELISA kit Detail
EpCAM (CD326) is a conserved type I transmembrane glycoprotein of 35 kDa expressed on epithelial cells. Initially discovered as a carcinoma cell surface antigen, EpCAM is also expressed in a variety of human epithelia cancers and can be then used as diagnostic or potential prognostic marker and as a potential target for immunotherapeutic strategies. EpCAM overexpression is often linked to poor prognosis, presumably due to its involvement in cancer cell proliferation, migration, and metastasis.
The name EpCAM - or Epithelial Cell Adhesion Molecule - was introduced by Litvinov and al, who showed that EpCAM can mediate Ca2 +-independent homophilic cell - cell adhesion in cells that normally lack cell - cell interactions. Human EpCAM is a polypeptide of 314 amino acids (aa), consisting of a large extracellular domain (N-terminal) of 242 aa, a single-spanning transmembrane domain of 23 aa and a short cytoplasmic domain of 26 aa (C-terminal). The gene encoding for human EpCAM is located on chromosome 2 (location 2p21). The EpCAM protein seems to be highly conserved among vertebrates, showing up to 81% amino acid sequence homology between human and mouse, and up to 99% between human and gorillas.
In healthy adult tissue, EpCAM is expressed at the basolateral cell membrane of epithelia. No expression can be detected in the differentiated cells of normal squamous stratified epithelia. In adults, EpCAM is expressed in most organs and glands, with the highest expression in colon. Generally, the level of expression differs between tissues. EpCAM is typically present in proliferating cells, and less in differentiated cells.
Soluble EpCAM, which likely is a product of intramembrane proteolysis, was first described in sera of cancer patients in 2002. In these studies, serum levels of shed EpCAM in patients were found to be in the low ng/ml range. Biochemical characterization of EpCAM has shown that its extracellular domain tends to aggregate and form multimers, most prominently tetramers.
June 2022
New Antibodies
| Human LCAM Azide free B-R48 | Detail |
| L1 cell adhesion molecule (L1CAM) is a neuronal adhesion molecule, existing in two isoforms: full-length and a variant without exons 2 and 27. It is engaged in homophilic interactions and complexes with many other ligands in a context-dependent manner. In normal tissues, its expression is restricted to nerve bundles and kidney tubules; however, L1CAM is expressed in many tumors, often correlated with poor prognosis and by this way, could be used as prognostic factor in some cancers [Fogel M. J Natl Cancer Inst. 2013 Aug 7; 105(15):1142-50]. L1CAM was shown to be involved in proliferation, invasion and metastasis both in vitro and in vivo [Klostermann S. Anticancer Res. 2009 Dec; 29(12):4919-31]. Activation and modulation of the extracellular signal-related kinase pathway by L1CAM has been documented [Meldolesi J. Trends Pharmacol Sci. 2015 Nov;36(11):769-81]. Inhibition of proliferation of selected tumor cell lines by L1CAM monoclonal antibodies in the absence of immune effector cells has been also shown [Jin C. Expert Rev Anticancer Ther. 2016 Mar; 16(3):359-71]. This protein seems to have an important role in cancerology. | |
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Anti-Human CD226 Azide Free B-G51 |
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Anti-Human CD226 Azide Free B-T40 |
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| Anti-Human CD226 Unconjugated B-G51 | Detail |
| CD226 is a 65 kDa glycoprotein also named DNAM-1 (DNAX Accessory Molecule-1), having one transmembrane domain and being a member of the immunoglobulin superfamily containing two Ig-like domains. It is expressed not only on NK cells but also on monocytes, T cells, and subsets of B cells [Shibuya A (1996). Immunity 4:573–81]. CD226 mediates cellular adhesion to other cells bearing its ligands Nectin2/CD112 and PVR/CD155 both members of the Nectin/Nectin-like family of adhesion molecules [De Andrade LF (2014) Immunol Cell Biol. 92:237–44]. Experiment of cross-linking CD226 with antibodies causes cellular activation. DNAM-1 (CD226) receptor is known to be essential for NK cell–dependent antitumor immunity [Fuchs, A. (2006) Cancer Biol 16, 359–366] [Smyth, MJ (2015) Oncotarget. 2015; 6:28537-28538] | |
New Recombinant proteins
Recombinant Human SARS-CoV-2 Spike RBD Variant Mu B.1.621 (HEK) Detail
Spike protein (S protein) is one of the four structural proteins of Coronavirus (SARS-Cov, SARS-Cov-2, MERS amongst others), S protein plays the most important role in viral attachment, fusion, and entry, and it serves as a target for development of antibodies, entry inhibitors and vaccines. In the S protein, the Receptor Binding Domain (RBD) mediates viral entry of SARS-Cov and SARS-Cov-2 into host cells by its interaction with the membrane receptor ACE2 (Angiotensin-converting enzyme 2). The variant lineage B.1.621 of SARS-Cov-2 was first identified early in 2021 in samples collected in South America, predominantly in Colombia. Named the variant Mu, it is the fifth "variant of interest" to be monitored by WHO since March 2021. It presents 3 mutations (R346K; E484K; N501Y) that suggest it may be more resistant to vaccines and/or previous infections.
Recombinant Human SARS-CoV-2 Spike RBD Variant Omicron hFc, Lineage B.1.1.529 (HEK) Detail
The variant lineage B.1.1.529 of SARS-Cov-2 was first identified in samples collected on November 11 2021 in Botswana and later (14th of November) in South Africa. The 26th of November, WHO named it “the Omicron variant” and was designated as a Variant of Concern. This variant presents 15 mutations in the RBD. Since Its discovery, cases of Omicron Variant were discovered all around the world
Recombinant Human CD25 - IL-2RA (CHO) Detail
IL-2, one of the most important factors in the human immune system, is a potent T-cell growth factor whose major function is the activation of many cells of the immune system including T-cells, B-cells, macrophages and NK cells. These potent actions are mediated by IL-2 binding and signalling through its associated cell surface receptor IL-2R. This receptor is not expressed on normal or unstimulated lymphocytes but is quickly transcribed and expressed on T-cells following activation. This IL-2R is a heterotrimeric protein consisting of three distinct glycopeptide subunits termed IL-2Ra (CD25) specific to IL-2R, IL-2Rb and IL-2Rg. The a and b chains are involved in binding IL-2 while the signal transduction following IL-2 binding is mediated by the g-chain along with the b chain. The IL-2Ra chain or CD25 is a type 1 transmembrane glycoprotein of 251 amino acids and 55kDa. CD25 can also be found as a soluble form in serum and tissue following enzymatic cleavage from expressing cells and can be identified as a 45KDa protein once shed from the membrane. As the expression and subsequent release of CD25 takes place following cell stimulation, the presence of soluble CD25 (sCD25) in circulation is an excellent marker of T-cell activation. A number of disease states linked to over expression of CD25 have previously been described including, autoimmune diseases, transplant rejection, chronic infection, B-cell neoplasm and various types of leukaemia and other forms of cancer. Because of this definite link between CD25 over expression and disease state many therapies for these conditions have evolved to inhibit this over expression of IL-2Ra. More recently CD25 has become the major marker for distinguishing the CD4+ CD25+ subset of T regulatory cells.
September 2021
New Antibodies
| Anti-SARS-CoV-2 RBD domain Azide Free B-B60 | Detail |
| Anti-SARS-CoV-2 RBD domain Azide Free B-D69 | Detail |
| Anti-SARS-CoV-2 RBD domain Azide Free B-R41 | Detail |
| Spike protein (S protein) is one of the four structural proteins of Coronavirus (SARS-Cov, SARS-Cov-2, MERS amongst others), S protein plays the most important role in viral attachment, fusion and entry, and it serves as a target for development of antibodies, entry inhibitors and vaccines. In the S protein, the Receptor Binding Domain (RBD) mediates viral entry of SARS-Cov and SARS-Cov-2 into host cells by its interaction with the membrane receptor ACE2 (Angiotensin-converting enzyme 2). |
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July 2021
New Recombinant proteins
Recombinant Human SARS-CoV-2 Spike RBD Variant Delta Lineage B.1.617.2 (HEK) Detail
Spike protein (S protein) is one of the four structural proteins of Coronavirus (SARS-Cov, SARS-Cov-2, MERS amongst others), S protein plays the most important role in viral attachment, fusion and entry, and it serves as a target for development of antibodies, entry inhibitors and vaccines.
In the S protein, the Receptor Binding Domain (RBD) mediates viral entry of SARS-Cov and SARS-Cov-2 into host cells by its interaction with the membrane receptor ACE2 (Angiotensin-converting enzyme 2).
The variant lineage B.1617.2 of SARS-Cov-2 was first identified in India in late 2020. The WHO named it “the Delta variant” at the end of May 2021. The two mutations in the RBD (L452R and T478K) affect the transmissibility of the SARS-CoV-2 virus. Since the 7th May 2021, the classification of this variant moves from variant under investigation (VUI) to variant of concern (VOC). This variant seems to be responsible in part for the second wave of the pandemic starting in February 2021 in India.
Recombinant Human Interleukin-1 Receptor Accessory Protein IL-1RAP (CHO) Detail
IL-1 Receptor Accessory Protein (IL-1RAP), also known as interleukin-1 receptor member 3 (IL-1 R3), is a member of the Interleukin-1 receptor family of proteins. The IL-1RAP protein is a coreceptor of the IL-1 (alpha and beta), IL-33 and IL-36 receptors involved in IL-1 signalling, activating different signalling pathways implicated in inflammation and proliferation.
IL1-RAP is critical for mediating the effects of IL-33, through the ST2/IL1RAP complex, and IL-36, through the IL-1Rrp2/IL-1RAP complex.
Human IL-1RAP is composed of 3 domains: an extracellular domain (ECD, 347 AA), a transmembrane part (21 AA), and a cytoplasmic domain (182 AA).
IL-1RAP has been identified as a marker of interest in the context of Chronic Myeloid Leukemia (CML) treatment, activating NK Cells and blocking tumor growth. Its overexpression is demonstrated in Hematopoietic Stem and Progenitor Cells (HSPC) and also in Acute Myeloid Leukemia (AML) disease.
New Antibodies
IL-28B
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Anti-Human IL-28B Azide Free |
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B-Z22 |
IL-28A, IL-28B, and IL-29, also named interferonλ2 (IFNλ2), IFNλ3, and IFNλ1, respectively, are class II cytokine receptor ligands that are distantly related to members of the IL-10 family (11-13% aa sequence identity) and the type I IFN family (15-19% aa sequence identity). The expression of IL-28A, B, and IL-29 is induced by virus infection or double stranded RNA. All three cytokines exert bioactivities that overlap those of type I IFNs, including antiviral activity and upregulation of MHC class I antigen expression. They signal through the same heterodimeric receptor complex that is composed of the IL10 receptor β (IL10Rβ) and a novel IL28 receptor α (IL28 Rα, also known as IFNλR1).
The three proteins have been reported to have an anti-proliferative and anti-tumour activity.
RANTES
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Anti-Human RANTES Azide Free |
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B-L39 |
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Anti-Human RANTES Unconjugated |
B-L39 |
RANTES (regulated on activation, normal T cell expressed and secreted) or chemokine (C-C motif) ligand 5 (also CCL5) is a chemotactic cytokine which in humans is encoded by the CCL5 gene.
It is chemotactic for T cells, eosinophils, and basophils, and plays an active role in recruiting leukocytes into inflammatory sites. With the help of IL-2 and IFN-γ released by T cells, CCL5 induces the proliferation and activation of certain natural-killer (NK) cells. It is also an HIV-suppressive factor released from CD8+ T cells.
IL-17B
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Anti-Human IL-17B Azide Free |
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B-B57 |
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Anti-Human IL-17B Azide Free |
B-B58 |
Interleukin-17B is an approximately 20 kDa glycosylated cytokine that plays a role in inflammation and bone growth. IL-17B binds to IL-17 RB and induces the production of inflammatory cytokines and the infiltration of inflammatory immune cells. IL-17B is upregulated in arthritic cartilage where it exacerbates the severity of disease. It is also upregulated in aggressive breast cancer cell lines, and its exaggerated signalling through IL-17 RB promotes tumorigenicity.
IL-1β
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Anti-Human IL-1B Azide Free |
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B-B53 |
Interleukin-1 Beta (IL-1b) is a member of the interleukin-1 family. This family consists of three structures related polypeptides. The first two are IL-1a and IL-1b, each of which has a broad spectrum of both beneficial and harmful biologic actions, and the third is IL-1-receptor antagonist, which inhibits the activities of interleukin-1.
IL-1 (a and b) have similar biological properties, among them, the ability to induce fever, sleep, anorexia and hypotension. IL-1 stimulates the release of pituitary hormones, increases the synthesis of collagenases, resulting in the destruction of cartilage, and stimulates the production of prostaglandins, leading to decrease in the pain threshold. In addition, IL-1 has some host-defence properties. However, whereas IL-1b is a secreted cytokine, IL-1a is predominantly a cell-associated cytokine.
IL-1 has also been implicated in the destruction of beta cells of the islets of Langerhans, the growth of myelogenous leukaemia cells, and the development of atherosclerotic plaques. It is described in
January 2021
FGF2
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Anti-Human FGF2 Azide Free |
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B-G58 |
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Anti-Human FGF2 Azide Free |
B-T42 |
FGF2 Basic fibroblast growth factor, also known as bFGF, FGF2 or FGF-β, is a member of the fibroblast growth factor family. In normal tissue, basic fibroblast growth factor is present in basement membranes and in the subendothelial extracellular matrix of blood vessels. Currently, FGFs comprise a family of nine structurally related proteins (FGF 1–9). FGFs are expressed in specific spatial and temporal patterns and are involved in developmental processes, angiogenesis (Folkman, J, Science, 1987, 235 (4787), 442–447), wound healing, and tumorigenesis (Thomas K, FASEB, 1987, 1, 434–440).
The bFGF is a critical component of human embryonic stem cell culture medium; the growth factor is necessary for the cells to remain in an undifferentiated state.
Expression of FGF2 and FGFRs in normal cells is highly regulated, and termination of FGF2 signaling is achieved through receptor internalization. However, FGF2/FGFR signaling in cancer cells is dysregulated, which may contribute to the pathogenesis of many types of cancer. Several studies have shown that FGF2 is a key tumor-promoting factor in the tumor microenvironment. The following section reviews current knowledge of the molecular pathways associated with FGF2 signaling in cancer, which represents a critical step for the implementation of strategies toward the development of personalized cancer therapy. (Akl, M, Oncotarget, 2016, Vol. 7(28) 44735-44762
CD123
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Anti-Human CD123 Azide Free |
B-V8 |
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Anti-Human CD123 Unconjugated |
B-V8 |
IL-3 is a pleiotropic cytokine, mainly produced by activated T-lymphocytes, regulating the function and production of hematopoietic and immune cells [Ihle (1192) Chem Immunol 51: 65–106]. The CD123 is interleukin-3 receptor sub-unit alpha, a glycoprotein of 360 aa, composed by an extracellular domain of 287aa, a transmembrane domain of 30 aa and by an intracellular domain of 53 aa [Barry SC (1997) Blood 89(3):842–852]. This alpha sub-unit alone binds IL‑3 with low affinity. And even if the beta subunit does not bind IL‑3 by itself, it is required for the high‑affinity binding of IL‑3 to the heterodimeric receptor complex.
The receptor was expressed on the majority of CD34+ hemopoietic progenitors and its expression is rapidly lost during erythroid and megakaryocytic differentiation, moderately decreased during monocytic differentiation and was sustained in the granulocytic lineage [Testa U (1996) Blood 88(9):3391–3406.].
The identification of a subset of dendritic cells in human peripheral blood has been reported to be characterized by the very high expression of CD123 [MacDonald KP, (2002) Blood 100(13):4512–4520]. It is also used as marker for LPDC (Leukemic plasmacytoid dendritic cells).
IL-8
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Anti-Human IL-8 Azide Free |
B-B49 |
Interleukin 8 (IL-8) or CXCL8, Monocyte-Derived Neutrophil Chemotactic Factor (MDNCF), Neutrophil Activating Factor (NAF) and NAD-P1 is a chemokine secreted by monocytes, macrophages and endothelial cells. IL-8 chemoattracts and activates neutrophils.
The predominant form of IL-8 is a 8.4kDa protein containing 72 amino acid residues, which includes five additional N-Terminal amino-acids. IL-8 contains the four conserved cysteine residues present in CXC chemokines and also contains the “ELR” motif common to CXC chemokines that binds to CXCR1 and CXCR2.
Data indicate that IL-8 may participate in the pathogenesis of rheumatoid arthritis via the induction of neutrophil-mediated cartilage damage, and psoriasis. A causative involvement of IL-8 is found within a broad range of clinico-pathological conditions : adult respiratory distress syndrome, asthma, bacterial infections, bladder cancer, graft rejection and influenza infection, due to the now known biological properties of IL-8. This cytokine especially in combinations with other neutrophil activating agents, may prove helpful in the treatment of patients suffering from granulocytopenia, severe infections against which antibiotics are not effective, and immunodeficiency caused by HIV.
IL-37
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Anti-Human IL-37 Azide Free |
B-P47 |
Human interleukin 1 family member 7 (IL1F7), also named IL-37, belongs to the IL1 cytokine family, which currently has ten members [Boraschi, D. (2011) Eur. Cytokine Netw. 22:127]. Expression of IL-37 in macrophages or epithelial cells almost completely suppressed production of pro-inflammatory cytokines [McNamee, E.N (2011) Proc. Natl. Acad. Sci. USA 108:16711], whereas the abundance of these cytokines increased with silencing of endogenous IL-37 in human blood cells. Anti-inflammatory cytokines were unaffected.
IL-37 is normally expressed at low levels in peripheral blood mononuclear cells (PBMC), mainly monocytes, and dendritic cells (DC), and is rapidly up-regulated in the inflammatory context [Nold, M.F (2010) Nat. Immunol. 11:1014], and therefore IL-37 conversely inhibits the production of inflammatory cytokines in PBMC and DC. In addition, IL-37 effectively suppresses the activation of macrophage and DC. It is not controversial that the activation of macrophage and DC and the over-expression of inflammatory cytokines are critical component elements in inflammatory process of atherosclerosis. Therefore, IL-37 may play a protective role in atherosclerosis through inhibition of inflammatory cytokines production and suppression of macrophage and DC activation [McCurdya S (2019) Cytokine. 122:154169].
SARS-CoV-2 Spike S1 Protein
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Anti-SARS-CoV-2 Spike S1 Protein Azide Free |
CR3022 |
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Anti-SARS-CoV-2 Spike S1 Protein Azide Free (IgA) |
CR3022-IgA |
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.
SARS-CoV-2 Nucleoprotein
| 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.
DLL4
| 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.
IL1RAP
| 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.
CD64
| 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