Annexin A1 Recombinant Protein | ANX1 recombinant protein

Recombinant Human Annexin A1

Cat. Num. AAA964966

• Gene Names: ANXA1; ANX1; LPC1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Annexin A1; Recombinant Human Annexin A1; Annexin I; Annexin-1; Calpactin II; Calpactin-2; Chromobindin-9; Lipocortin I; Phospholipase A2 inhibitory proteinp35; ANX1 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 5-346aa; Partial
• Sequence: SEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN
• Sequence Length: 346

• 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 ANX1 recombinant protein

Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It ses to bind from two to four calcium ions with high affinity.

Product Categories/Family for ANX1 recombinant protein

Signal Transduction

References

Cloning and expression of human lipocortin, a phospholipase A2 inhibitor with potential anti-inflammatory activity.Wallner B.P., Mattaliano R.J., Hession C., Cate R.L., Tizard R., Sinclair L.K., Foeller C., Chow E.P., Browning J.L., Ramachandran K.L., Pepinsky R.B.Nature 320:77-81(1986) Correlation of gene and protein structure of rat and human lipocortin I.Kovacic R.T., Tizard R., Cate R.L., Frey A.Z., Wallner B.P.Biochemistry 30:9015-9021(1991) Structural characterization of a biologically active human lipocortin 1 expressed in Escherichia coli.Arcone R., Arpaia G., Ruoppolo M., Malorni A., Pucci P., Marino G., Ialenti A., di Rosa M., Ciliberto G.Eur. J. Biochem. 211:347-355(1993) Location of sites in human lipocortin I that are phosphorylated by protein tyrosine kinases and protein kinases A and C.Varticovski L., Chahwala S.B., Whitman M., Cantley L., Schindler D., Chow E.P., Sinclair L.K., Pepinsky R.B.Biochemistry 27:3682-3690(1988) Characterization by tandem mass spectrometry of structural modifications in proteins.Biemann K., Scoble H.A.Science 237:992-998(1987) A dimeric form of lipocortin-1 in human placenta.Pepinsky R.B., Sinclair L.K., Chow E.P., O'Brine-Greco B.Biochem. J. 263:97-103(1989) Phosphorylation of annexin I by TRPM7 channel-kinase.Dorovkov M.V., Ryazanov A.G.J. Biol. Chem. 279:50643-50646(2004) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Crystal structure of human annexin I at 2.5-A resolution.Weng X., Luecke H., Song I.S., Kang D.S., Kim S.-H., Huber R.Protein Sci. 2:448-458(1993) NMR solution structure of domain 1 of human annexin I shows an autonomous folding unit.Gao J., Li Y., Yan H.J. Biol. Chem. 274:2971-2977(1999)

NCBI and Uniprot Product Information

• NCBI GI #: 4502101
• NCBI GeneID: 301
• NCBI Accession #: NP_000691.1
• NCBI GenBank Nucleotide #: NM_000700.2
• UniProt Accession #: P04083
• Molecular Weight: 42.3 kDa
• NCBI Official Full Name: annexin A1
• NCBI Official Synonym Full Names: annexin A1
• NCBI Official Symbol: ANXA1
• NCBI Official Synonym Symbols: ANX1; LPC1
• NCBI Protein Information: annexin A1
• UniProt Protein Name: Annexin A1
• Protein Family: Annexin
• UniProt Gene Name: ANXA1
• UniProt Synonym Gene Names: ANX1; LPC1
• UniProt Entry Name: ANXA1_HUMAN

NCBI Description

This gene encodes a membrane-localized protein that binds phospholipids. This protein inhibits phospholipase A2 and has anti-inflammatory activity. Loss of function or expression of this gene has been detected in multiple tumors. [provided by RefSeq, Dec 2014]

Uniprot Description

ANXA1: a calcium/phospholipid-binding protein with which promotes membrane fusion and is involved in endocytosis. Has anti-inflammatory properties and inhibits phospholipase A2 activity. Accumulates on internalized vesicles after EGF-stimulated endocytosis, suggesting that it may be required for a late stage in inward vesiculation. Phosphorylated by PKC, EGFR and Chak1. Phosphorylation results in loss of the inhibitory activity. Annexins are a family of structurally related proteins whose common property is calcium-dependent binding to phospholipids. There are at least ten different annexins in mammalian species. Annexins do not contain signal peptides, yet some annexins (A1, A2 and A5) appear to be secreted in a physiologically regulated fashion.

Protein type: Calcium-binding; Lipid-binding

Chromosomal Location of Human Ortholog: 9q21.13

Cellular Component: apical plasma membrane; basolateral plasma membrane; cell surface; cornified envelope; cytoplasm; cytoplasmic vesicle membrane; early endosome membrane; endosome; extracellular region; extracellular space; extrinsic to external side of plasma membrane; extrinsic to membrane; focal adhesion; lateral plasma membrane; mast cell granule; mitochondrial membrane; nucleoplasm; nucleus; phagocytic cup; plasma membrane; protein complex; sarcolemma; vesicle

Molecular Function: calcium ion binding; calcium-dependent phospholipid binding; calcium-dependent protein binding; double-stranded DNA-dependent ATPase activity; helicase activity; phospholipase A2 inhibitor activity; phospholipid binding; protein binding; protein binding, bridging; protein homodimerization activity; receptor binding; single-stranded DNA binding; single-stranded RNA binding; structural molecule activity

Biological Process: actin cytoskeleton reorganization; adaptive immune response; alpha-beta T cell differentiation; arachidonic acid secretion; cell surface receptor linked signal transduction; DNA duplex unwinding; DNA strand renaturation; endocrine pancreas development; G-protein signaling, coupled to cyclic nucleotide second messenger; gliogenesis; inflammatory response; innate immune response; insulin secretion; keratinocyte differentiation; monocyte chemotaxis; muscle contraction; myoblast migration involved in skeletal muscle regeneration; negative regulation of apoptosis; negative regulation of exocytosis; negative regulation of T-helper 2 cell differentiation; neutrophil homeostasis; peptide cross-linking; phagocytosis; positive regulation of interleukin-2 production; positive regulation of neutrophil apoptosis; positive regulation of prostaglandin biosynthetic process; positive regulation of T cell proliferation; positive regulation of T-helper 1 cell differentiation; positive regulation of vesicle fusion; prostate gland development; regulation of cell shape; regulation of hormone secretion; regulation of inflammatory response; regulation of interleukin-1 production; regulation of leukocyte migration; response to drug; response to estradiol stimulus; response to peptide hormone stimulus; response to X-ray; signal transduction