Biosimilar Antibodies
B-CK, Human, mAb CK-BYK/21E10, Hycult Biotech, HM2110
The monoclonal antibody CK-BYK/21E10 recognizes human creatine kinase B-type, also known as B-CK. Human B-CK is a protein of 381 amino acids (~45 kDa), expressed in a number of tissues. B-CK is most abundant in adult brain, approx. 5-fold lower in the stomach, 10-fold lower in the heart and barely detectable in liver. In brain, whereas most B-CK has been shown to be cytosolic, several of the reactions requiring B-CK are membrane-associated. B-CK belongs to the creatine kinase (CK) isoenzymes that catalyse the synthesis of phosphocreatine (PCr) and its subsequent use in the regeneration of ATP in cell types where the consumption of ATP is rapid and/or sudden. In the brain the different CK isoforms constitute an energy shuttle wherein ATP produced in the mitochondria is used by a mitochondrial CK [e.g. ubiquitous mitochondrial creatine kinase (uMi-CK)] to generate PCr, which is then transported and used by a cytoplasmic CK [e.g. brain creatine kinase (B-CK)] to regenerate ATP at discrete cellular sites of high ATP turnover. B-CK appears to have a role in regenerating ATP needed for the transport of ions and neurotransmitters since CKB has been localized to brain synaptic plasma membranes, possibly coupled to Na+/K+-ATPase and acetylcholine receptor-rich membranes. Expression of B-CK is developmentally controlled: in rat, brain CK protein at birth is extremely low and increases 10-fold until week 4. This reflects the many energy-demanding processes in brain during brain development.
Host
Human
Reactivity
Applications
Conjugation
B-FABP, Human, mAb 1F5, Hycult Biotech, HM2299
The monoclonal antibody clone 1F5 recognizes human brain fatty acid binding protein (B-FABP, FABP7) of both natural and recombinant origin. The B-FABP protein is derived from the human FABP7 gene. FABPs are small intracellular proteins (~13-14 kDa) with a high degree of tissue specificity that bind long chain fatty acids. They are abundantly present in various cell types and play an important role in the intracellular utilization of fatty acids, transport and metabolism. There are at least nine distinct types of FABP, each showing a specific pattern of tissue expression. Due to its small size, FABP leaks rapidly out of ischemically damaged necrotic cells leading to a rise in serum levels. Ischemically damaged tissues are characterized histologically by absence (or low presence) of FABP facilitating recognition of such areas. B-FABP is localized in the brain and other neural tissues.
Host
Human
Reactivity
Applications
Conjugation
B-FABP, Human, mAb 2D2, Hycult Biotech, HM2300
The monoclonal antibody clone-2D2 recognizes human brain fatty acid binding protein (B-FABP, FABP7) of both natural and recombinant origin. The B-FABP protein is derived from the human FABP7 gene. FABPs are small intracellular proteins (~13-14 kDa) with a high degree of tissue specificity that bind long chain fatty acids. They are abundantly present in various cell types and play an important role in the intracellular utilization of fatty acids, transport and metabolism. There are at least nine distinct types of FABP, each showing a specific pattern of tissue expression. Due to its small size, FABP leaks rapidly out of ischemically damaged necrotic cells leading to a rise in serum levels. Ischemically damaged tissues are characterized histologically by absence (or low presence) of FABP facilitating recognition of such areas. B-FABP is localized in the brain and other neural tissues.
Host
Human
Reactivity
Applications
Conjugation
B-FABP, Human, pAb, Hycult Biotech, HP9029
The polyclonal antibody recognizes human brain fatty acid binding protein (B-FABP) of both natural and recombinant origin. The B-FABP protein is derived from the human FABP7 gene. FABPs are small intracellular proteins (~13-14 kDa) with a high degree of tissue specificity that bind long chain fatty acids. They are abundantly present in various cell types and play an important role in the intracellular utilization of fatty acids, transport and metabolism. There are at least nine distinct types of FABP, each showing a specific pattern of tissue expression. Due to its small size, FABP leaks rapidly out of ischemically damaged necrotic cells leading to a rise in serum levels. Ischemically damaged tissues are characterized histologically by absence (or low presence) of FABP facilitating recognition of such areas. B-FABP is localized in the brain and other neural tissues.
Host
Human
Reactivity
Applications
Conjugation
Basophils, Human, mAb 2D7, Hycult Biotech, HM2279
Unlock the secrets of immune response with our precision-targeted 2D7 monoclonal antibody, the definitive marker for basophils. This innovative tool zeroes in on a unique 7.2-7.5 kDa protein exclusive to basophil secretory granules, enabling researchers to track basophil activation with unparalleled clarity. As gatekeepers of inflammatory and allergic reactions, basophils are pivotal in the release of histamine and cytokines, and in prompting B cells to produce IgE. Originating in the bone marrow, these critical cells circulate in the bloodstream, ready to converge at inflammation sites. With the 2D7 antibody, detect the subtle interplay of basophils in allergic conditions with exacting specificity—excluding interference from lymphocytes, monocytes, eosinophils, neutrophils, and mast cells. Elevate your research with the precision of 2D7 antibody in immunohistochemistry and western blot applications, and illuminate the role of basophils in human health and disease.
Host
Human
Reactivity
Applications
Conjugation
Beta-3 integrin subunit, Human, mAb BV4, Hycult Biotech, HM2035
The monoclonal antibody BV4 recognizes human beta3 integrin subunit present in Platelet glycoprotein GPIIb-IIIa (integrin alphaIIb/beta3, CD41/CD61) and in the vitronectin receptor (integrin alphaV/beta3, CD51/CD61). Intergins are a family of heterodimeric membrane glycoproteins expressed on diverse cell types which function as the major receptors for extracellular matrix and as cell-cell adhesion molecules. As adhesion molecules they play an important role in numerous biological processes such as platelet aggregation, inflammation, immune function, wound healing, tumour metastasis and tissue migration during embryogenesis. In addition integrins are involved in signaling pathways, transmitting signals both into an out from cells. All integrins consist of two non-covalently associated subunits, alpha and beta. At least 12 different alpha subunits and 8 beta subunits have been identified. The beta subunits all contain 56 conserved cysteines (except beta4 which has 48) which are arranged in four repeating units. The beta3 subunit is a 93kDa protein that contains a large loop in the N-terminus stabilized by intrachain disulphide bonding with the first cysteine-rich repeat. Platelet glycoprotein GPIIb-IIIa is expressed on platelets and megakaryoblasts. It is constitutively expressed and becomes activated on triggered platelets. Platelet glycoprotein GPIIb-IIIa binds to fibrinogen, fibronectin, vWF, vitronectin and thrombospondin. Next to this it is also a receptor for several soluble adhesive proteins.Vitronectin receptor is expressed on endothelial cells, some B cells, monocytes/macrophages, platelets and tumour cells. Vitronectin receptor binds next to vitronectin to fibrinogen, vWF, thrombospondin, fibronectin, osteopontin and collagen. Defects in human beta3 integrin are a cause of Glanzmann thrombasthenia, which is an autosomal recessive disorder characterized by mucocutaneous bleeding and the inability of this integrin to recognize macromolecular or synthetic peptide ligands.
Host
Human
Reactivity
Applications
Conjugation
Beta-defensin 1, Human, pAb, Hycult Biotech, HP9059
Antimicrobial proteins (AMP) are a fundamental element of the primary response against pathogens. AMP’s are small endogenous cationic molecules expressed by phagocytic and epithelial cells. The antimicrobial activity of AMP’s is directed towards a broad spectrum of pathogens, like Gram-positive & negative bacteria, viruses, yeast and fungi. AMP’s aid in innate and adaptive immunity via direct inactivation and by immunomodulatory activity like leukocyte migration. Defensins are the most prominent mammalian AMP’s. Three defensin peptide families are identified, the α-, β-, and θ-defensins. They are characterized by a triple-stranded β-hairpin structure, six disulfide-linked cysteine residues and a positive charge. They are synthesized as preproteins and undergo processing to become a fully active peptide. Defensins are divided in alpha- and beta-defensins depending on their disulfide bridging pattern. α- and β-defensins modify cell migration and maturation, induce cytokines and trigger histamin and prostaglandin D2 release from mast cells. There are six α-defensins: HNP (human neutrophil peptide)-1 to -4, HD5 & 6. Human beta-defensin 1(hBD-1) is considered a prominent AMP in epithelial defense against infection. High expression levels have been found in the kidney and female reproductive tract, especially in pregnant women. Besides antimicrobial activity, hBD1 has an effect on chemoattractive immature dendritic cells and probably memory T cells. After reduction of disulphide-bridges hBD-1 becomes a potent antimicrobial peptide against the opportunistic pathogenic fungus Candida albicans and against anaerobic Gram positive commensals of Bifidobacterium and Lactobacillus species.
Host
Human
Reactivity
Applications
Conjugation
Beta-defensin 2, Human, clone HB12G9, Hycult Biotech, HM2390
Monoclonal antibody HB12G9 recognized human beta defensin-2 (HBD2). hBD-2 is a cysteine-rich cationic 41 amino acid antimicrobial peptide of 4-5 kDa. Human BD-2 is produced by epithelial cells upon stimulus by lipopolysaccharides and proinflammatory cytokines TNFα and IL1β. Contact of keratinocytes with gram-negative bacteria results in rapid induction of hBD-2 protein. hBD-2 has been described as a dynamic component of the local epithelial defense system of the skin, intestinal and respiratory tract, where it functions by protecting surfaces from infection. Its local expression has been associated with skin lesions like psoriasis as well as infected lung epithelia of patients with cystic fibrosis. Furthermore, in inflammatory bowel disease (IBD), expression of hBD-2 is increased in patients with IBD compared to healthy persons. The NF-kB pathway has been recognized as a key component in the induction of hBD-2 expression, however, other studies have observed induction mediated by the mitogen-activated protein kinase (MAPK) pathways. Thus, increased expression of hBD-2 in epithelial cells is associated with the proinflammatory response. This is supported by the finding that the anti-inflammatory cytokines IL-10 and IL-13 downregulate the synthesis of hBD-2 in atopic dermatitis.
Host
Human
Reactivity
Applications
Conjugation
Beta-defensin 2, Human, pAb, Hycult Biotech, HP9057
The polyclonal antibody recognizes human beta-defensin 2 (hBD-2). hBD-2 is a cystein-rich cationic 41 amino acid antimicrobial peptide of 4-5 kDa. Human BD-2 is produced by epithelial cells upon stimulus by lipopolysaccharides and proinflammatory cytokines TNFα and IL1β. Contact of keratinocytes with gram-negative bacteria results in rapid induction of hBD-2 protein. hBD-2 has been described as a dynamic component of the local epithelial defense system of the skin, intestinal and respiratory tract, where it functions by protecting surfaces from infection. Its local expression has been associated with skin lesions like psoriasis as well as infected lung epithelia of patients with cystic fibrosis. Furthermore, in inflammatory bowel disease (IBD), expression of hBD-2 is increased in patients with IBD compared to healthy persons. The NF-kB pathway has been recognized as a key component in the induction of hBD-2 expression, however, other studies have observed induction mediated by the mitogen-activated protein kinase (MAPK) pathways. Thus, increased expression of hBD-2 in epithelial cells is associated with the proinflammatory response. This is supported by the finding that the anti-inflammatory cytokines IL-10 and IL-13 downregulate the synthesis of hBD-2 in atopic dermatitis.
Host
Human
Reactivity
Applications
Conjugation
Beta1 Integrin, Human, mAb BV7, Hycult Biotech, HM2033
The monoclonal antibody BV7 recognizes human ß1-integrin. Beta-1 integrin is a ubiquitously expressed ~89 kDa type I transmembrane protein functioning as receptor when heterodimerized with one alpha subunit. It belongs to the integrin beta chain family consisting of four different genes, encoding multiple β-integrins via alternative splicing. Ligand-recognition depends on the composition of the heterodimer: either collagen, fibronectin, VCAM1, laminin, cytotactin, osteopontin, epiligrin, thrombospondin and CSPG4 can bind to the integrin-complex. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. Isoform beta-1B interferes with isoform beta-1A resulting in a dominant negative effect on cell adhesion and migration (in vitro). In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi’s sarcoma lesions. When associated with α7, β1-integrin regulates cell adhesion and laminin matrix deposition. BV7 is active on HT-29 colon carcinoma cells and on HCCP-2998 tumor cells. It is involved in promoting endothelial cell motility and angiogenesis. Furthermore, β1-integrin plays a mechanistic adhesive role during telophase, and is required for the successful completion of cytokinesis. Upon activation integrins in general, including β1-integrin, are known to exhibit global structural rearrangements and exposure of ligand binding sites. β1-integrin modulation is of importance in tissue repair and regeneration. In cultured primary hippocampal neurons, astrocytes and tissues, cell surface expression of amyloid beta fibrils (key hallmark of Alzheimer’s disease) selectively co-localized with β1-integrin. Preincubation of cells with antibodies against β1-integrin, as well as α1-integrin, greatly enhanced amyloid beta-induced apoptosis, indicating a protective role for integrins in apoptosis. The monoclonal antibody BV7 does not recognize α5β1 complex and not the cytoplasmic part of the β1-subunit. Monoclonal antibody BV7 is active on HT-29 colon carcinoma cells and on HCCP-2998 tumor cells. BV7 binds to several other tumor cells (MG3 osteosarcoma, A375 melanoma, MHCC- 1410 and Lovo colon carcinoma) but does not affect adhesion to endothelial cells.
Host
Human
Reactivity
Applications
Conjugation
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