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Bovine IL-4 (Yeast-derived Recombinant Protein) - 100 micrograms

RP0001B-100
$900.00
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Bulk quantities of Bovine IL-4 protein are available.
Please contact us for pricing.

Bovine IL-4 Specifications

Molecular Weight (calculated) - 12.6kDa

Amino Acid Sequence - GHKCDIT LAEIIKTLNI LTTRKNSCME LPVADVFAAP KNTTEKETFC RVGIELRRIY RSHTCLNKFL GGLDRNLNSL ASKTCSVNEA KTSTSTLKDL LERLKTIMKE KYSKC (115)

Gene ID - 280824

Purity - >98% as visualized by SDS-PAGE analysis.

Homology Across Species
Bos taurus (cattle) IL-4 - 100%
Bison bison (bison) IL-4 - 100%
Bubalus bubalis (water buffalo) IL-4 - 100%
Bos mutus (wild yak) IL-4 - 100%
Syncerus caffer (African buffalo) IL-4 - 100%
Bos indicus (zebu) IL-4 – 99%
More - https://blast.ncbi.nlm.nih.gov/

Endotoxin - Naturally endotoxin-free

Applications

Cell Culture, ELISA Standard, Western Blot Control

IL-4 Background

Interleukin-4 (IL-4) induces differentiation of naive helper T cells (Th0 cells) to Th2 cells. Upon activation by IL-4, Th2 cells subsequently produce additional IL-4. IL-4 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. It is a key regulator in humoral and adaptive immunity. IL-4 induces B-cell class switching to IgE, and up-regulates MHC class II production. Overproduction of IL-4 is associated with allergies.

Alternate Names - IL4, BCGF-1, BCGF1, BSF-1, BSF1, IL-4, interleukin 4

Bovine IL-4 (Yeast-derived Recombinant Protein) - 100 micrograms
Catalog No.:
RP0001B-100
Quantity:
100 ug
Source:
The Bovine IL-4 recombinant protein was produced in yeast and therefore does not have endotoxin, is naturally folded, and post-translationally modified.
MW:
The Bovine IL-4 recombinant protein has a predicted molecular weight of 12.6 kDa.
Protein Sequence:
GHKCDIT LAEIIKTLNI LTTRKNSCME LPVADVFAAP KNTTEKETFC RVGIELRRIY RSHTCLNKFL GGLDRNLNSL ASKTCSVNEA KTSTSTLKDL LERLKTIMKE KYSKC (115)
Country of Origin:
USA
Applications:
The Bovine IL-4 endotoxin-free recombinant protein can be used in cell culture, as an ELISA Standard, and as a Western Blot Control.

28878771

Coordinated Role of Toll-Like Receptor-3 and Retinoic Acid-Inducible Gene-I in the Innate Response of Bovine Endometrial Cells to Virus.

Carneiro LC, Bedford C, Jacca S, Rosamilia A, de Lima VF, Donofrio G, Sheldon IM, Cronin JG.

Front Immunol. 2017 Aug 23;8:996. doi: 10.3389/fimmu.2017.00996. eCollection 2017.

Applications: Stimulation of bovine dendritic cells using bovine IL-4 and bovine GM-CSF to produce monocyte-derived dendritic cells in culture.


26163935

Monocyte-derived dendritic cells from late gestation cows have an impaired ability to mature in response to E. coli stimulation in a receptor and cytokine-mediated fashion.

Pomeroy B, Sipka A, Klaessig S, Schukken Y.

Vet Immunol Immunopathol. 2015 Sep 15;167(1-2):22-9. doi: 10.1016/j.vetimm.2015.06.016. Epub 2015 Jul 2.

Applications: IL-10 and IL-12 were used as ELISA standards. IL-4 and GM-CSF were used to stimulate monocytes in culture. MHC II, CD14, and CD80 antibodies were used to look at cell surface receptors by flow cytometry.


22627785

Classically or alternatively activated bovine monocyte-derived macrophages in vitro do not resemble CD163/Calprotectin biased macrophage populations in the teat.

Düvel A, Frank C, Schnapper A, Schuberth HJ, Sipka A

Innate Immun. 2012 May 23.

Applications: Stimulation of bovine MDM cells.

Abstract
The functional phenotype of resident macrophages significantly determines the character of an inflammatory response. In this study we identified two phenotypes of tissue macrophages in bovine teat tissue based on expression of Calprotectin and CD163. To investigate a possible link between the dichotomy in phenotype and functional properties of cells in association with different host mediators we set up an in vitro model with bovine monocyte-derived macrophages (MdM). In vitro differentiated MdM invariably and uniformly expressed both antigens. Classically activated MdM (IFN-γ priming and LPS stimulation) showed a decreased CD163 expression while alternative activation (IL-4/IL-13 priming) did not change expression of CD163 and Calprotectin. Differently activated MdM showed a clearly distinct expression of genes related to classical (IL-12, inducible NO synthase) or alternative activation (IL-10, arginase I). The presence of the inflammatory host mediator prostaglandin E(2) (PGE(2)) neither influenced expression of Calprotectin and CD163 nor gene expression profiles in MdM generated in the presence of PGE(2) (PGE(2)-MdM). Supernatants of PGE(2-)MdM, however, significantly dampened the migration of neutrophilic granulocytes. The results of this study highlight the discrepancy between in vivo and in vitro obtained macrophages and point to the necessity to analyze the functional capacities of bovine tissue macrophages in situ.


22129622

Effects of interleukin-8 on estradiol and progesterone production by bovine granulosa cells from large follicles and progesterone production by luteinizing granulosa cells in culture.

Shimizu T, Kaji A, Murayama C, Magata F, Shirasuna K, Wakamiya K, Okuda K, Miyamoto A.

Cytokine. 2012 Jan;57(1):175-81.

Applications: Non-specific ELISA Standard

Abstract
Interleukin 8 (IL-8) is a chemoattractant involved in the recruitment and activation of neutrophils and is associated with the ovulate process. We examined the possible role of IL-8 in steroid production by bovine granulosa cells before and after ovulation. The concentration of IL-8 in the follicular fluid of estrogen-active dominant (EAD) and pre-ovulatory follicles (POF) was higher than that of small follicles (SF). CXCR1 mRNA expression was higher in the granulosa cells of EAD and POF than that of SF. In contrast, CXCR2 mRNA expression was lower in granulosa cells of EAD and POF than in SF. IL-8 inhibited estradiol (E2) production in follicle-stimulating hormone (FSH)-treated granulosa cells at 48 h of culture. IL-8 also suppressed CYP19A1 mRNA expression in FSH-treated granulosa cells. IL-8 stimulated progesterone (P4) production in luteinizing hormone (LH)-treated granulosa cells at 48 h of culture. Although IL-8 did not alter the expression of genes associated with P4 production, it induced StAR protein expression in LH-treated granulosa cells. The expression of CXCR1 mRNA in corpus luteum (CL) did not change during the luteal phase. In contrast, the expression of CXCR2 mRNA in middle CL was significantly higher than in early and regression CL during the luteal phase. In luteinizing granulosa cells, an in vitro model of granulosa cell luteinization, CXCR2 mRNA expression was downregulated, whereas CXCR1 mRNA expression was unchanged. IL-8 also stimulated P4 production in luteinizing granulosa cells. These data provide evidence that IL-8 functions not only as a chemokine, but also act as a regulator of steroid synthesis in granulosa cells to promote luteinization after ovulation.


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