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Interleukin-21 (IL21) is a pleiotropic cytokine produced by CD4+ T-cells in response to antigenic stimulation. Its action generally enhances antigen-specific responses of immune cells. The biological effects of IL21 include induction of differentiation of T-cells-stimulated B-cells into plasma cells and memory B-cells, stimulation of IgG production with IL4, and induction of apoptotic effects in naive B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL21 promotes the anti-tumorigenic activity of CD8+ T-cells and natural killer (NK) cells. IL21 exerts its effect through binding to a specific type I cytokine receptor, IL21R, which also contains the gamma chain (γc) found in other cytokine receptors, including IL2, IL4, IL7, IL9 and IL15. The IL21/IL21R interaction triggers a cascade of events which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3.

IL22 belongs to IL10 family of regulatory cytokines, which includes IL10, IL19, IL20, IL22, IL24 and IL26. Members of this family share partial homology in their amino acid sequences, but are dissimilar in their biological functions. Produced by T-lymphocytes and dendritic cells, IL10 contributes to the inflammatory response in vivo, and signals through CRF2-4 and IL22. Along with IL17, it is rapidly produced by splenic LTi-like cells and can be also produced by Th17 cells. It is likely that IL22 plays a role in the coordinated response of both the adaptive and innate immune systems.

Interleukin-3 beta (IL3B) and IL3A are two variants of IL3. IL3A and IL3B are identical aside from the fact that IL3A has three extra amino acids inserted at position 56. IL3 is a hematopoietic growth factor that promotes the survival, differentiation and proliferation of committed progenitor cells of the megakaryocyte, granulocyte-macrophage, erythroid, eosinophil, basophil and mast cell lineages. Produced by T-cells, mast cells and eosinophils, IL3 enhances thrombopoieses, phagocytosis and antibody-mediated cellular cytotoxicity. Its ability to activate monocytes suggests that IL3 may have additional immunoregulatory roles. Many of the IL3 activities depend upon co-stimulation with other cytokines. IL3 is a species-specific, variably glycosylated cytokine.

Interleukin-3 (IL3) is an interleukin which is a type of biological signal (cytokine) encoded by the IL3 gene located on chromosome 5, and produced primarily by activated T-cells, human thymic epithelial cells, activated murine mast cells, murine keratinocytes and murine neurons/astrocytes. The protein acts in hematopoiesis by controlling the production, differentiation and function of two related white cell populations in the blood: the granulocytes and the monocytes/macrophages. The rhesus macaque IL3 reported to be a monomer, as it is known, contains 124 amino acid residues, which make up a single nonglycosylated polypeptide. However, recombinant rhesus macaque, human and murine IL3 share low homology.

Interleukin-33 (IL33), also known as NF-HEV and DVS 27, is a cytokine belonging to the IL1 superfamily. IL33 is a pro-inflammatory protein that may regulate gene transcription and induce helper T-cells, mast cells, eosinophils and basophils to produce type 2 cytokines. The induction of type 2 cytokines by IL33 in vivo is believed to induce the severe pathological changes observed in mucosal organs following administration of IL33. IL33 is constitutively expressed in smooth muscle and airway epithelia, and it binds to a high-affinity receptor family member ST2. In vivo administration of mature IL33 promotes increased production of IL5, IL13, IgE and IgA, as well as splenomegaly and inflammatory infiltration of mucosal tissues.

Interleukin-4 (IL4) is a pleiotropic cytokine that induces differentiation of naive helper T-cells (Th0 cells) to Th2-cells, and is produced by mast cells, activated T-cells and bone marrow stromal cells. It has many biological roles, including the stimulation of activated B-cell and T-cell proliferation, and the differentiation of CD4+ T-cells into Th2-cells. IL4 can enhance both the secretion and cell surface expression of IgE and IgG1. IL4 also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. The rat IL4 shares about 40-45% amino acid sequence identity with human, mouse, rhesus macaque IL4, and they are species-specific in their activities.

Interleukin-4 (IL4) is a pleiotropic cytokine mainly produced by mast cells, activated T-cells and bone marrow stromal cells. It has many biological roles, including the stimulation of activated B-cell and T-cell proliferation, and the differentiation of CD4+ T-cells into Th2 cells. Additionally, IL4 enhances both the secretion and expression of cell surface IgE and IgG1. IL4 also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. The rhesus macaque IL4 shares about 40-45% amino acid sequence identity with human, mouse, and rat IL4 and is species-specific in its activities.

The IL5 gene is located on chromosome 11 in rats, in close proximity to the genes encoding IL3, IL4, and granulocyte-macrophage colony-stimulating factor (CSF2), which are often co-expressed in TH2 cells. Through binding to the IL5 receptor, IL5 stimulates B cell growth and increases immunoglobulin secretion and is also a key mediator in eosinophil activation. Interleukin 5 has long been associated with the cause of several allergic diseases including allergic rhinitis and asthma. Rat IL5 is a TH2 cytokine that is part of the hematopoietic family. Unlike other members of this cytokine family (namely IL3 and CSF2), this glycoprotein is a homodimer in its active form.

Interleukin-6 (IL6) is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T-cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL6 has diverse biological functions. It stimulates B-cell differentiation and antibody production, synergizes with IL3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins, and regulates bone metabolism. IL6 signals through the IL6 receptor system that consists of two chains, IL6R alpha and gp130.

Interleukin-6 (IL6) is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T-cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL6 has diverse biological functions. It stimulates B-cell differentiation and antibody production, synergizes with IL3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins and regulates bone metabolism. IL6 signals through the IL6 receptor system that consists of two chains: IL6Rα and gp130.

Interleukin-7 (IL7) is encoded by the IL7 gene and secreted by stromal cells in the red marrow and thymus. It binds to the IL7 receptor, a heterodimer consisting of an IL7 receptor alpha chain and an IL2 receptor gamma chain. IL7 stimulates the differentiation of hematopoietic stem cells into lymphoid progenitor cells and also stimulates the proliferation of B-cells, T-cells and natural killer (NK) cells. Furthermore, IL7 as an immunotherapy agent has been examined in many human clinical trials for various malignancies including during HIV infection. Rat IL7 contains 129 amino acid residues and has three disulfide bonds. In addition, it has approximately 63% and 88% amino acid sequence identity with human and murine IL7 respectively.

Interleukin-8 (C-X-C motif chemokine 8) is coded by the interleukin 8 gene on chromosome 5 in Rhesus macaque (Macaca mulatta), which is not only 94% identical to human IL8, but also structurally and functionally similar with human IL8. IL8 also provides a valuable resource for a model of inflammation in primates.

Interleukin-9 (IL9) is encoded by the IL9 gene and is produced by T-cells and specifically by CD4+ helper cells. IL9 was originally identified as a cytokine found in the conditioned medium of a human T-cell leukemia virus type I (HTLVI) transformed T-cell line. IL9 functions through the IL-9 receptor, which activates different signal transducer and activator (STAT) proteins and thus connects this pleiotropic cytokine to various biological processes. IL9 can support the growth of IL2 independent and IL4 independent helper T-cells. The gene encoding this cytokine has been identified as a candidate gene for asthma. Genetic studies on a mouse model of asthma demonstrated that this cytokine is a determining factor in the pathogenesis of bronchial hyperresponsiveness.

Ficin is a cysteine protease enzyme which is derived from the latex of fig trees with activity similar to other cysteine protease enzymes including endopeptidases, aminopeptidases, and dipeptidyl peptidases. Ficin cleaves mouse immunoglobulin G molecules (IgG1) in the hinge region. The concentration of cysteine changes how ficin cleaves IgG1. A F(ab’)2 fragment is formed in the presence of 1mM cysteine. The F(ab’)2 fragments are smaller than whole IgG molecules and better penetrate tissue for antigen recognition while avoiding unspecific binding to Fc receptors. In the presence of 10mM cysteine, two 2 Fab fragments are produced instead. F(ab) fragments block background from primary antibody binding, and block endogenous and exposed immunoglobulins and tissues in labeling experiments.

Immobilized Ficin Agarose Resin offers a convenient solution to the production of F(ab’)2 and Fab fragments while eliminating autolysis and protease contamination and the need to remove the enzymes following digestion. Fab and F(ab’)2 can be further separated from whole IgG with either Protein A Agarose Resin (GoldBio Product # P-400) or ion exchange chromatography.

Activity:1-1.5 mg ficin/ml of resin

Support: 6% Cross-linked Agarose

Storage/Handling: Shipped at ambient temperature. Upon receipt, store at 4°C, do NOT freeze.

Papain is a cysteine protease enzyme from papaya latex that has a wide variety of activities including endopeptidases, aminopeptidases, dipeptidyl peptidases and enzymes with both exo- and endo-peptidase activity. In particular, papain cleaves immunoglobulin G (IgG) molecules near the hinge region of the antibody, resulting in three similar, ~50 kDa, fragments; an Fc domain and two monovalent Fab domains. This papain-digested antibody is therefore unable to promote agglutination, precipitation, opsonization or lysis. The Fc fragment can then be used to determine the specificity of the Fc receptors without any typical antigen binging interference while the Fab fragments can be used in immunohistochemical studies.

Pepsin, one of the principal digestion enzymes, breaks down proteins in to smaller peptides. It is most efficient in cleaving the peptide bonds between hydrophobic and aromatic amino acids such as phenylalanine, tryptophan and tyrosine. Pepsin readily cleaves immunoglobulin G (IgG) molecules, generating F(ab’)2 fragments and small Fc peptide fragments. The smaller Fc fragments can be easily removed via gel filtration while the F(ab’)2 fragments can then be purified from any remaining, undigested IgG. The F(ab’)2 fragments are highly useful for research interests, being able to penetrate tissue better than standard IgG antibodies and facilitate better antigen recognition while avoiding unspecific binding to Fc receptors.

Immobilized Pepsin Agarose Resin is an efficient method for producing F(ab’)2 fragments from IgG molecules for antibody mimetic. Undigested IgG can be quickly removed with our Protein A Agarose Resin (GoldBio Catalog # P-400). Fc fragments can also be removed using a gel filtration system.

Resin: 6% Cross-linked Agarose

Shipping/Handling: Shipped at ambient temperature. Upon receipt, store at 4°C, do NOT freeze.

Pepstatin A is a competitive, reversible aspartic protease inhibitor which inhibits proteases such as pepsin, chymosin, renin, HIV proteases, and cathepsins D and E. Peptstatin A is highly selective and is often used in a mixture with other enzyme inhibitors. In vitro studies have shown pepstatin A is the only aspartic acid inhibitor that exhibits inhibitory effects on HIV proteases.

Trypsin is a serine protease that hydrolyses proteins which can be found in the digestive system. Trypsin cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues with very little or no cleavage at lysyl-proline and arginyl-proline bonds. This special cleaving activity yields peptides that are easily identified by mass spectrometry. Additionally, our Immobilized Trypsin is TPCK treated to deactivate interfering chymotrypsin, which can interfere with sequence analysis.

KIT Ligand (KITLG), also called Stem Cell Factor (SCF) which binds to the c-Kit receptor is produced by fibroblasts and endothelial cells. The soluble and transmembrane forms of the protein are formed by alternative splicing of the same RNA transcript and the presence of both soluble and transmembrane SCF is required for normal hematopoietic function. SCF plays an important role in hematopoiesis, spermatogenesis and melanogenesis and it promotes mast cell adhesion, migration, proliferation, and survival. Rat KITLG shares 75­-90% amino acid sequence identity with canine, feline, mouse, and human KITLG. Furthermore, rat KITLG is active on mouse and human cells, but human KITLG is only weakly active on mouse cells.

L-Rhamnose monohydrate is a deoxy sugar in plants and bacteria. It is a component of plant cell walls that helps maintain structure.