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

Combined with the antibody and molecular biology engineering expertise of the mAbexperts team, we can cater for your needs in: antigen development, large scale antibody or recombinant protein productions and VHH technology.


 

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New Antibodies

January 2021

FGF2

Anti-Human FGF2 Azide Free

    

B-G58

Detail

Anti-Human FGF2 Azide Free

 

B-T42

Detail

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

Anti-Human CD123 Azide Free

 

B-V8

Detail

Anti-Human CD123 Unconjugated

 

B-V8

Detail

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

Anti-Human IL-8 Azide Free

 

B-B49

Detail

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

Anti-Human IL-37 Azide Free

 

B-P47

Detail

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

Anti-SARS-CoV-2 Spike S1 Protein Azide Free

 

CR3022

 

Detail

Anti-SARS-CoV-2 Spike S1 Protein Azide Free (IgA)

 

CR3022-IgA

 

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.


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


 

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