Bovine Leukemia Inhibitory Factor (LIF) Polyclonal Antibody Testing

Using our bovine LIF recombinant protein as the antigen, polyclonal antibodies were produced in chickens and screened for recognition of both the glycosylated and deglycosylated forms of bovine, canine, rabbit and swine LIF recombinant proteins. (Previously it was demonstrated that the Kingfisher Biotech LIF recombinant proteins were glycosylated.) The Kingfisher Biotech LIF recombinant proteins were either treated with deglycosylation enzymes or left untreated and were subsequently screened using a Western Blot. The Western Blot showed that the anti-bovine LIF polyclonal antibody recognized both the glycosylated and the deglycosylated forms of bovine (lanes 2 & 3), canine (lanes 4 & 5), rabbit (lanes 6 & 7), and swine (lanes 7 & 8) LIF recombinant proteins.

Glycosylation of Bovine, Canine, Rabbit, and Swine Leukemia Inhibitory Factor

Kingfisher Biotech expresses recombinant proteins in yeast so they are potentially post-translationally modified. Bovine, canine, rabbit and swine Leukemia Inhibitory Factor (LIF) have calculated molecular weights of  19.8, 19.7, 19.7, and 19.7 kDa, respectively. The Kingfisher Biotech LIF recombinant proteins were treated with deglycosylation enzymes using NEB kit Protein Deglycosylation Mix  (NEB Catalog No. P6039S) to determine if the protein produced in yeast is glycosylated. The results show that all four LIF recombinant proteins shifts in molecular weight when treated with the deglycosylation enzymes; the smear of higher MW material appears to be reduced to a single band migrating with the 22/28 kDa doublet standards. The bands showing the molecular weight of the deglycosylation enzymes are also visible. This data suggests Kingfisher Biotech's bovine, canine, rabbit and swine LIF recombinant protein produced in yeast are glycosylated.

Lane	Sample	Treatment
1	Stds-PAGEgel Two-Color SDS Protein Ladder
2	Bovine LIF	Untreated
3	Bovine LIF	Denatured/Deglycosylated
4	Canine LIF	Untreated
5	Canine LIF	Denatured/Deglycosylated
6	Stds-PAGEgel Two-Color SDS Protein Ladder
7	Rabbit LIF	Untreated
8	Rabbit LIF	Denatured/Deglycosylated
9	Swine LIF	Untreated
10	Swine LIF	Denatured/Deglycosylated
11	Stds-PAGEgel Two-Color SDS Protein Ladder
12

MW of Standards: 7.6, 12, 22/28 doublet, 33, 48, 71, 96, 142, 195 kDa. 
16% Acrylamide SDS-PAGE Gel (Expedeon)

LIF Homology Across Species

Bovine, Canine Rabbit, and Swine Leukemia Inhibitory Factor Recombinant Proteins are available from Kingfisher Biotech. Leukemia inhibitory factor, or LIF, is a member of the IL-6 family. LIF affects cell growth by inhibiting differentiation. When LIF levels drop, the cells differentiate. 

Rabbit and Canine Leukemia Inhibitory Factor (LIF) Recombinant Proteins

Kingfisher Biotech's Rabbit and Canine Leukemia Inhibitory Factor (LIF) recombinant proteins can be used in cell culture, as an LIF ELISA Standard, and as a Western Blot Control. Leukemia inhibitory factor, or LIF, is a member of the IL-6 family. LIF affects cell growth by inhibiting differentiation. When LIF levels drop, the cells differentiate. Leukemia inhibitory factor derives its name from its ability to induce the terminal differentiation of myeloid leukemic cells, thus preventing their continued growth. Other properties attributed to LIF include: the growth promotion and cell differentiation of different types of target cells, influence on bone metabolism, cachexia, neural development, embryogenesis and inflammation. p53 regulated LIF has been shown to facilitate implantation in the mouse model and possibly in humans. Removal of LIF pushes stem cells toward differentiation, but they retain their proliferative potential or pluripotency. LIF is typically added to stem cell culture medium to reduce spontaneous differentiation.

Kingfisher Biotech's LIF recombinant proteins are intended for use in animal model and animal health research. Our portfolio includes bovine, canine, and rabbit Leukemia Inhibitory Factor (LIF) recombinant proteins. We will be adding Swine Leukemia Inhibitory Factor (LIF) recombinant protein soon.

IFN gamma Recombinant Proteins - Bovine, Canine, Chicken, Dolphin, Equine, Feline, Human, Mouse, Ovine, Rabbit, and Swine

Bovine, Canine, Chicken, Dolphin, Equine, Feline, Human, Mouse, Ovine, Rabbit, and Swine IFN gamma Recombinant Proteins

IFN-gamma, or type II interferon, is a cytokine that is critical for innate and adaptive immunity against viral and intracellular bacterial infections and for tumor control. Aberrant IFN-gamma expression is associated with a number of autoinflammatory and autoimmune diseases. The importance of IFN-gamma in the immune system stems in part from its ability to inhibit viral replication directly, but, most important, derives from its immunostimulatory and immunomodulatory effects. IFN-gamma is produced predominantly by natural killer (NK) and natural killer T (NKT) cells as part of the innate immune response, and by CD4 and CD8 cytotoxic T lymphocyte (CTL) effector T cells once antigen-specific immunity develops.

Kingfisher Biotech offers bovine, canine, chicken, dolphin, equine, feline, human, mouse, ovine, rabbit, and swine IFN gamma recombinant proteins. Our proteins are produced in yeast, making them naturally endotoxin-free - perfect for cell culture applications. 

IFN gamma Homology Across Species

Deglycosylation of Bovine IL-6 (RP0014B)

Kingfisher Biotech expresses recombinant proteins in yeast so they are potentially post-translationally modified. Bovine IL-6 has a calculated molecular weight of 20.6 kDa. The Kingfisher Biotech Bovine IL-6 (RP0014B) recombinant protein was treated with deglycosylation enzymes using NEB kit Protein Deglycosylation Mix  (NEB Catalog No. P6039S) to determine if the protein produced in yeast is glycosylated. The results show that Bovine IL-6 shifts in molecular weight when treated with the deglycosylation enzymes; the smear of higher MW material appears to be reduced to a single band migrating with the 22/28 kDa doublet standards. The bands showing the molecular weight of the deglycosylation enzymes are also visible. This data suggests Kingfisher Biotech's Bovine IL-6 recombinant protein produced in yeast is glycosylated.

Lane	Sample
1	Standards-PAGE gel Two-Color SDS Protein Ladder
2	Bovine IL-6 KFB RP0014B-025 - untreated
3	Bovine IL-6 KFB RP0014B-025 - denatured
4	Bovine IL-6 KFB RP0014B-025 - denatured and deglycosylated
5	Standards-PAGE gel Two-Color SDS Protein Ladder

MW of Standards: 7.6, 12, 22/28 doublet, 33, 48, 71, 96, 142, 195 kDa. 
16% Acrylamide SDS-PAGE Gel (Expedeon)

Bovine Leukemia Inhibitory Factor (LIF) Recombinant Protein

Kingfisher Biotech's Bovine Leukemia Inhibitory Factor (LIF) recombinant protein can be used in cell culture, as an LIF ELISA Standard, and as a Western Blot Control. Leukemia inhibitory factor, or LIF, is a member of the IL-6 family. LIF affects cell growth by inhibiting differentiation. When LIF levels drop, the cells differentiate. Leukemia inhibitory factor derives its name from its ability to induce the terminal differentiation of myeloid leukemic cells, thus preventing their continued growth. Other properties attributed to LIF include: the growth promotion and cell differentiation of different types of target cells, influence on bone metabolism, cachexia, neural development, embryogenesis and inflammation. p53 regulated LIF has been shown to facilitate implantation in the mouse model and possibly in humans. Removal of LIF pushes stem cells toward differentiation, but they retain their proliferative potential or pluripotency. LIF is typically added to stem cell culture medium to reduce spontaneous differentiation.Kingfisher Biotech's Bovine Leukemia Inhibitory Factor (LIF) recombinant protein is intended for use in animal model and animal health research.

CCL5 Recombinant Proteins - Bovine, Canine, Chicken, Equne, Guinea Pig, Human, Mouse, Swine

RANTES/CCL5 recombinant proteins can be used in cell culture, as an RANTES/CCL5 ELISA Standard, and as a Western Blot Control. CCL5, also know as RANTES (regulated and normal T cell expressed and secreted) is a member of the C-C Chemokine Family. There are at least 27 distinct members of the C-C subgroup reported for mammals. RANTES (CCL5) is chemotactic for T cells, eosinophils, and basophils, and plays an active role in recruiting leukocytes into inflammatory sites. CCL5 plays a role in many disease states, including rheumatoid arthritis, HIV, and cancer. CCL5/RANTES recombinant proteins are intended for use in animal model and animal health research.

Bovine CCL5 (RANTES) Recombinant Protein - 25 micrograms	RP0062B-025	25 ug
Bovine CCL5 (RANTES) Recombinant Protein - 5 micrograms	RP0062B-005	5 ug
Canine CCL5 (RANTES) Recombinant Protein - 25 micrograms	RP0454D-025	25 ug
Canine CCL5 (RANTES) Recombinant Protein - 5 micrograms	RP0454D-005	5 ug
Chicken CCL5 (RANTES) Recombinant Protein - 25 micrograms	RP0982C-025	25 ug
Chicken CCL5 (RANTES) Recombinant Protein - 5 micrograms	RP0982C-005	5 ug
Equine CCL5 (RANTES) Recombinant Protein - 25 micrograms	RP0070E-025	25 ug
Equine CCL5 (RANTES) Recombinant Protein - 5 micrograms	RP0070E-005	5 ug
Guinea Pig CCL5 (RANTES) Recombinant Protein - 25 micrograms	RP0348GP-025	25 ug
Guinea Pig CCL5 (RANTES) Recombinant Protein - 5 micrograms	RP0348GP-005	5 ug
Human CCL5 (RANTES) Recombinant Protein - 25 micrograms	RP0983H-025	25 ug
Human CCL5 (RANTES) Recombinant Protein - 5 micrograms	RP0983H-005	5 ug
Mouse CCL5 (RANTES) Recombinant Protein - 25 micrograms	RP0984M-025	25 ug
Mouse CCL5 (RANTES) Recombinant Protein - 5 micrograms	RP0984M-005	5 ug
Swine CCL5 (RANTES) Recombinant Protein - 100 micrograms	RP0059S-100	100 ug
Swine CCL5 (RANTES) Recombinant Protein - 25 micrograms	RP0059S-025	25 ug
Swine CCL5 (RANTES) Recombinant Protein - 5 micrograms	RP0059S-005	5 ug

Canine, Equine, and Swine Erythropoietin Recombinant Proteins

Erythropoietin (EPO) is an essential hormone for red blood cell production. Without it, definitive erythropoiesis does not take place. Erythropoietin has its primary effect on red blood cell progenitors and precursors by promoting their survival through protecting these cells from apoptosis. It is the primary erythropoietic factor that cooperates with various other growth factors (e.g., IL-3, IL-6, glucocorticoids, and SCF) involved in the development of erythroid lineage from multipotent progenitors. Erythropoietin has a range of actions including vasoconstriction-dependent hypertension, stimulating angiogenesis, and inducing proliferation of smooth muscle fibers. It can increase iron absorption by suppressing the hormone hepcidin. EPO is highly glycosylated, with half-life in blood around five hours. The half-life of EPO may vary between endogenous and various recombinant versions. Additional glycosylation or other alterations of EPO via recombinant technology have led to increased stability in blood. EPO binds to the erythropoietin receptor on the red cell progenitor surface and activates a JAK2 signaling cascade. Erythropoietin receptor expression is found in a number of tissues, such as bone marrow and peripheral/central nervous tissue. In the bloodstream, red cells themselves do not express erythropoietin receptor, so cannot respond to EPO. However, indirect dependence of red cell longevity in the blood on plasma erythropoietin levels has been reported, a process termed neocytolysis. Kigfisher Biotech's recombinant Erythropoietin proteins are intended for use in animal model and animal health research and can be used in cell culture, as an EPO ELISA Standard, and as a Western Blot Control. Canine, equine, and swine EPO recombinant proteins are now available from Kingfisher Biotech.

Kingfisher Biotech, Inc. is committed to accelerating basic veterinary research and human disease research done in animal models by developing and commercializing research reagents specific for a variety of species, including bovine, canine, caprine, chicken, dolphin, equine, feline, guinea pig, hamster, human, mouse, ovine, rabbit, rat, swine, and turkey. We will continue to add species as our customer request specific reagents for their research. Currently, we offer over 1200 recombinant proteins, polyclonal antibodies, monoclonal antibodies and ELISA kits for animal health and animal model research. Our products are primarily cytokines, chemokines, interferons, and growth factors. Our product development queue is filled mainly by customer requests. If there is a product that you are looking for and can't find, please send us an email.

Kingfisher Biotech Announces the Launch of Bovine GM-CSF Protein

Bovine GM-CSF is glycosylated in nature; Kingfisher Biotech’s bovine GM-CSF is produced in yeast so it is glycosylated, making it more likely to mimic natural bovine GM-CSF.

Kingfisher Biotech’s bovine GM-CSF protein has been shown to be a superior product for use in cell culture. The biological activity of recombinant bovine GM-CSF was confirmed by an independent lab in a cell proliferation assay using the human TF-1 cell line. The ED50 for this effect was determined to be 2.5 – 4.0 ng/mL.

Granulocyte-macrophage colony-stimulating factor (GM-CSF) is a protein secreted by macrophages, T cells, mast cells, NK cells, endothelial cells and fibroblasts. GM-CSF stimulates stem cells to produce granulocytes (neutrophils, eosinophils, and basophils) and monocytes. Granulocyte macrophage–colony stimulating factor (GM-CSF) is secreted in response to inflammatory stimuli such as LPS, IL-1, and TNF-α by a variety of different cells, including endothelium, fibroblasts, muscle cells, and macrophages, and by activated T cells. GM-CSF is glycosylated in its mature form.

Bovine GM-CSF protein was produced in yeast without the use of tags. Proteins produced in yeast are naturally endotoxin free, properly folded, biologically active, and may be post-translationally modified. Many scientists find that these properties make proteins produced in yeast preferable over E. coli-produced proteins.

Bovine GM-CSF is lyophilized, available in convenient sizes (5, 25, and 100 micrograms) and in-stock ready to ship. Additional information, including product specifications and ordering information can be found at http://www.kingfisherbiotech.com.

Kingfisher Biotech is focused on providing kits and reagents to the animal health and animal model research community. Currently, the Kingfisher Biotech product portfolio contains over 750 products. Kingfisher Biotech products are supplied for research applications. They are not intended for medicinal, diagnostic or therapeutic use.

Kingfisher Biotech’s Mouse GM-CSF Protein Found to be 40% More Active Than Competitor’s Mouse GM-CSF Protein

Granulocyte-macrophage colony-stimulating factor (GM-CSF) is a protein secreted by macrophages, T cells, mast cells, NK cells, endothelial cells and fibroblasts. GM-CSF stimulates stem cells to produce granulocytes (neutrophils, eosinophils, and basophils) and monocytes. Granulocyte macrophage–colony stimulating factor (GM-CSF) is secreted in response to inflammatory stimuli such as LPS, IL-1, and TNF-α by a variety of different cells, including endothelium, fibroblasts, muscle cells, and macrophages, and by activated T cells. GM-CSF is glycosylated in its mature form.

Kingfisher Biotech’s mouse GM-CSF protein has been shown to be a superior product for use in cell culture. It is 40% more active than another commercially available mouse GM-CSF as measured by an independent testing laboratory. The biological activity of recombinant mouse GM-CSF was measured in a cell proliferation assay using the mouse FDC-P1 cell line. The ED50 for this effect was determined to be 0.0015-0.0023 ng/mL as compared to 0.0021-0.0035 ng/mL for the competitor’s mouse GM-CSF protein.

Mouse GM-CSF protein was produced in yeast without the use of tags. Proteins produced in yeast are naturally endotoxin free, properly folded, biologically active, and may be post-translationally modified. Many scientists find that these properties make proteins produced in yeast preferable over E. coli-produced proteins.

Mouse GM-CSF is lyophilized, available in convenient sizes (5, 25, and 100 micrograms) and in-stock ready to ship. Additional information, including product specifications and ordering information can be found at http://www.kingfisherbiotech.com.