protein

Recombinant Human Annexin A1

MBS964966

0.05 mg (E-Coli)

165 USD

Recombinant Protein

Recombinant Human Annexin A1

Annexin A1

Annexin I; Annexin-1; Calpactin II; Calpactin-2; Chromobindin-9; Lipocortin I; Phospholipase A2 inhibitory proteinp35

annexin A1; Annexin A1; annexin A1; annexin A1; Annexin I; Annexin-1; Calpactin II; Calpactin-2; Chromobindin-9; Lipocortin I

ANX1

LPC1

ANXA1; ANXA1; ANX1; LPC1; ANX1; LPC1

ANXA1_HUMAN

E Coli

5-346

346

SEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFN
PSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKA
AYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDAD
ELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREEL
KRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLA
DSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQ
KYTKYSKHDMNKVLDLELKGD

Greater than 90% as determined by SDS-PAGE.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Signal Transduction

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.

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)

4502101

NP_000691.1

NM_000700.2

P04083

42.4kD

Class A/1 (Rhodopsin-like Receptors) Pathway (1269545); Formyl Peptide Receptors Bind Formyl Peptides And Many Other Ligands Pathway (1269551); G Alpha (i) Signalling Events Pathway (1269576); G Alpha (q) Signalling Events Pathway (1269578); GPCR Downstream Signaling Pathway (1269574); GPCR Ligand Binding Pathway (1269544); Gastrin-CREB Signalling Pathway Via PKC And MAPK (1269592); Integrated Breast Cancer Pathway (219801); Integrated Pancreatic Cancer Pathway (711360); Muscle Contraction Pathway (1269868)

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]

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

0.05 mg (E-Coli)

165 USD

0.2 mg (E-Coli)

275

0.5 mg (E-Coli)

515

1 mg (E-Coli)

755