Interleukin-4 Recombinant Protein | IL4 recombinant protein

Recombinant Human Interleukin-4

Cat. Num. AAA955105

• Gene Names: IL4; BSF1; IL-4; BCGF1; BSF-1; BCGF-1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Interleukin-4; Recombinant Human Interleukin-4; B-cell stimulatory factor 1; BSF-1; Binetrakin; Lymphocyte stimulatory factor 1; Pitrakinra; IL4 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 25-153. Full Length of Mature Protein
• Sequence: HKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYSHHEKDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCPVKEANQSTLENFLERLKTIMREKYSKCSS

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for IL4 recombinant protein

Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes.

Product Categories/Family for IL4 recombinant protein

Immunology

References

Isolation and characterization of a human interleukin cDNA clone, homologous to mouse B-cell stimulatory factor 1, that expresses B-cell- and T-cell-stimulating activities.Yokota T., Otsuka T., Mosmann T., Banchereau J., Defrance T., Blanchard D., de Vries J.E., Lee F., Arai K.Proc. Natl. Acad. Sci. U.S.A. 83:5894-5898(1986) Complete nucleotide sequence of the chromosomal gene for human IL-4 and its expression.Arai N., Nomura D., Villaret D., Malefijt R.D., Seiki M., Yoshida M., Minoshima S., Fukuyama R., Maekawa M., Kudoh J., Shimizu N., Yokota K., Abe E., Yokota T., Takebe Y., Arai K.J. Immunol. 142:274-282(1989) An alternatively spliced interleukin 4 form in lymphoid cells.Klein S.C., Golverdingen J., Bouwens A.G.M., Tilanus M.G.J.Immunogenetics 41:57-57(1995) SeattleSNPs variation discovery resource The 5' region of the human interleukin 4 gene structure and potential regulatory elements.Eder A., Krafft-Czepa H., Krammer P.H.Nucleic Acids Res. 16:772-772(1988) Disulfide assignments in recombinant mouse and human interleukin 4.Carr C., Aykent S., Kimack N.M., Levine A.D.Biochemistry 30:1515-1523(1991) Crystal structure of recombinant human interleukin-4.Walter M.R., Cook W.J., Zhao B.G., Cameron R.P. Jr., Ealick S.E., Walter R.L. Jr., Reichert P., Nagabhushan T.L., Trotta P.P., Bugg C.E.J. Biol. Chem. 267:20371-20376(1992) Crystal structure of human recombinant interleukin-4 at 2.25-A resolution.Wlodaver A., Pavlovsky A., Gustchina A.FEBS Lett. 309:59-64(1992) Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface.Hage T., Sebald W., Reinemer P.Cell 97:271-281(1999) Secondary structure and topology of human interleukin 4 in solution.Redfield C., Smith L.J., Boyd J., Lawrence G.M.P., Edwards R.G., Smith R.A.G., Dobson C.M.Biochemistry 30:11029-11035(1991) Human interleukin 4. The solution structure of a four-helix bundle protein.Smith L.J., Redfield C., Boyd J., Lawrence G.M.P., Edwards R.G., Smith R.A.G., Dobson C.M.J. Mol. Biol. 224:899-904(1992) 1H, 15N, 13C, and 13CO assignments of human interleukin-4 using three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy.Powers R., Garret D.S., March C.J., Frieden E.A., Gronenborn A.M., Clore G.M.Biochemistry 31:4334-4346(1992) Determination of the secondary structure and folding topology of human interleukin-4 using three-dimensional heteronuclear magnetic resonance spectroscopy.Garret D.S., Powers R., March C.J., Frieden E.A., Clore G.M., Gronenborn A.M.Biochemistry 31:4347-4353(1992) Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy.Powers R., Garret D.S., March C.J., Frieden E.A., Gronenborn A.M., Clore G.M.Science 256:1673-1677(1992) Experimental and theoretical studies of the three-dimensional structure of human interleukin-4.Curtis B.M., Presnell S.R., Srinivasan S., Sassenfeld H., Klinke R., Jeffery E., Cosman D., March C.J., Cohen F.E.Proteins 11:111-119(1991) Aspects of receptor binding and signalling of interleukin-4 investigated by site-directed mutagenesis and NMR spectroscopy.Mueller T., Dieckmann T., Sebald W., Oschkinat H.J. Mol. Biol. 237:423-436(1994) Comparison of four independently determined structures of human recombinant interleukin-4.Smith L.J., Redfield C., Smith R.A.G., Dobson C.M., Clore G.M., Gronenborn A.M., Walter M.R., Naganbushan T.L., Wlodawer A.Nat. Struct. Biol. 1:301-310(1994) Polymorphism in the P-selectin and interleukin-4 genes as determinants of stroke a population-based, prospective genetic analysis.Zee R.Y.L., Cook N.R., Cheng S., Reynolds R., Erlich H.A., Lindpaintner K., Ridker P.M.Hum. Mol. Genet. 13:389-396(2004)

NCBI and Uniprot Product Information

• NCBI GI #: 4504669
• NCBI GeneID: 3565
• NCBI Accession #: NP_000580.1
• NCBI GenBank Nucleotide #: NM_000589.3
• UniProt Accession #: P05112; Q14630; Q6NZ77
• Molecular Weight: 17.0 kDa
• NCBI Official Full Name: interleukin-4 isoform 1
• NCBI Official Synonym Full Names: interleukin 4
• NCBI Official Symbol: IL4
• NCBI Official Synonym Symbols: BSF1; IL-4; BCGF1; BSF-1; BCGF-1
• NCBI Protein Information: interleukin-4
• UniProt Protein Name: Interleukin-4
• Protein Family: Interleukin
• UniProt Gene Name: IL4
• UniProt Synonym Gene Names: IL-4; BSF-1
• UniProt Entry Name: IL4_HUMAN

NCBI Description

The protein encoded by this gene is a pleiotropic cytokine produced by activated T cells. This cytokine is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. This gene, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008]

Uniprot Description

IL4: Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Genetic variations in IL4 may be a cause of susceptibility to ischemic stroke (ISCHSTR); also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. Belongs to the IL-4/IL-13 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Cell cycle regulation; Secreted, signal peptide; Cytokine; Motility/polarity/chemotaxis; Secreted

Chromosomal Location of Human Ortholog: 5q31.1

Cellular Component: external side of plasma membrane; extracellular space

Molecular Function: cytokine activity; growth factor activity; interleukin-4 receptor binding; protein binding

Biological Process: B cell costimulation; B cell differentiation; cellular defense response; chemotaxis; cholesterol metabolic process; connective tissue growth factor biosynthetic process; defense response to protozoan; female pregnancy; immune response; innate immune response in mucosa; microglial cell activation; myeloid dendritic cell differentiation; negative regulation of acute inflammatory response; negative regulation of apoptosis; negative regulation of chronic inflammatory response; negative regulation of macrophage activation; negative regulation of nitric oxide biosynthetic process; negative regulation of osteoclast differentiation; negative regulation of transcription, DNA-dependent; positive regulation of activated T cell proliferation; positive regulation of B cell proliferation; positive regulation of chemokine biosynthetic process; positive regulation of defense response to virus by host; positive regulation of interleukin-10 production; positive regulation of interleukin-13 production; positive regulation of isotype switching to IgE isotypes; positive regulation of isotype switching to IgG isotypes; positive regulation of mast cell degranulation; positive regulation of MHC class II biosynthetic process; positive regulation of T cell differentiation; positive regulation of T cell proliferation; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; positive regulation of tyrosine phosphorylation of Stat5 protein; regulation of immune response; regulation of isotype switching; regulation of phosphorylation; regulation of proton transport; response to cytokine stimulus; response to drug; response to ethanol; response to nutrient; response to organic cyclic substance; retina development in camera-type eye; T-helper 1 cell lineage commitment; T-helper 2 cell differentiation; T-helper 2 type immune response

Disease: Stroke, Ischemic