annexin a

We have previously shown that Annexin A8 (ANXA8) is strongly associated with the basal-like subgroup of breast cancers, including BRCA1-associated breast cancers, and poor prognosis; while in the mouse mammary gland AnxA8 mRNA is expressed in low-proliferative isolated pubertal mouse mammary ductal epithelium and after enforced involution, but not in isolated highly proliferative terminal end buds (TEB) or during pregnancy. ANXA8 as a potential mediator of quiescence in the normal mouse mammary ductal epithelium, while its expression in basal-like breast cancers may be linked to ANXA8's association with their specific cells of origin. Annexin A8 (ANXA8), a member of a superfamily of calcium and phospholipid binding proteins, is physiologically expressed in a tissue-specific manner, recent microarray studies reported that ANXA8 was also ectopically expressed in pancreatic cancers. We investigated the molecular mechanism of expression of ANXA8 in cancer cells and its functional role in pancreatic cancer cells. ANXA8 was diversely expressed in human cancer cell lines. Ectopic ANXA8 expression in cancer cells might involve an epigenetic mechanism. ANXA8 might play an important role in calcium fluctuation-mediated HIF-1α transcriptional activation and cell viability. The retinoic acid derivative fenretinide (FR) is capable of transdifferentiating cultured retinal pigment epithelial (RPE) cells towards a neuronal-like phenotype, down-regulation of AnxA8 is both necessary and sufficient for neuronal transdifferentiation of RPE cells and reveal an essential role for AnxA8 as a key regulator of RPE phenotype.

Annexin A7 (ANXA7) is a member of the annexin family of calcium-dependent phospholipid binding proteins. Annexin A7 has a unique, highly hydrophobic N-terminal domain and a conserved C-terminal region. The C-terminal region is composed of alternating hydrophobic and hydrophilic segments. Annexin A7 is a calcium phospholipid-binding protein with diverse properties including voltage-sensitive calcium channel activity and promotes membrane fusion and is also involved in exocytosis.

Annexin A3(ANXA3)contains 4 annexin repeats and belongs to the annexin family. Members of this calcium-dependent phospholipid-binding protein family play a role in the regulation of cellular growth and in signal transduction pathways. It is abnormally expressed in fetuses of both IVF and ICSI, which may contribute to the increase risk of birth defects in these ART. ANXA3 is Inhibitor of phospholipase A2 and cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. it also also play a role in anti-coagulant properties.

Annexin A8 (ANXA8) belongs to a family of calcium-dependent membrane and phospholipid binding proteins. Annexin A8 contains 4 annexin repeats separated by linking sequences of variable lengths. A pair of annexin repeats may form one binding site for calcium and phospholipid. ANXA8 is preferentially expressed in acute promyelocytic leukemia (APL) cells, which suggests its participation in hematopoietic cell differentiation. In addition, ANXA8 is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.

Expression system: E. coli
Length: 2-319, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-235, Full Length
Activity: Not Tested

The placental anticoagulant protein Annexin A5 (ANXA5) is a multifunctional protein that is highly expressed on the apical surfaces of syncytiotrophoblasts, and plays an important role in haemostatic regulations, maintaining blood fluidity of the placenta. Annexin A5 (ANXA5) is a protein abundantly expressed in normal placenta where it contributes to the healthy outcome of a pregnancy. Lower ANXA5 levels have been observed in M2 ANXA5 haplotype carrying chorion. The association found between the maternal carriage of the M2 ANXA5 haplotype and an elevated risk of IUGR and or PE supports the hypothesis that carrier status of this haplotype and the consequently reduced placental ANXA5 expression might be responsible, at least partially, for the onset of these gestational vascular complications. ANXA5 could be used as a biomarker for the early detection of PE and for the prediction of its severity. ANXA5 as an embryonic anticoagulant that appears deficient in contiguous specter of thrombophilia-related pregnancy complications culminating more frequently in miscarriage in a maternal M2 carrier background. As a potential indicator for malignancy and lymphatic metastasis, ANXA5 overexpression increases in vitro migration and invasion of Hca-P cell, promotes in vivo malignancy, LNM rate and level of Hca-P-transplanted mice. Hereditary thrombophilias can impair vascular placental functions and predispose to the birth of small-for-gestational age (SGA) babies. The placental anticoagulant protein annexin A5 (ANXA5) may contribute to this process. A functional haplotype (M2) within the ANXA5 gene is associated with fetal loss and venous thrombosis.

Annexin A13 (ANXA13) belongs to the annexin family which plays a role in phospholipase inhibition, cytoskeletal interactions, intracellular signal transduction pathways and regulation of cellular growth. ANXA13 contains four annexin repeats and a pair of annexin repeats may form one binding site for calcium and phospholipid. ANXA13 is highly expressed in intestinal and kidney epithelial cells. The specific function of ANXA13 has not yet been determined; however it is associated with the plasma membrane of undifferentiated, proliferating crypt epithelial cells as well as differentiated villus enterocytes.

Annexin A6, also known as ANXA6 or ANXAⅥ, belongs to a family of Ca2+-dependent membrane and phospholipid binding proteins. Members of this family have been implicated in membrane-related events along exocytotic and endocytotic pathways. Annexin 6 is phosphorylated in vivo associated with cell growth. Annexin 6 was not phosphorylated in quiescent cells, but was phosphorylated on serine and to a lesser extent threonine, several hours following cell stimulation. Experiment has revealed the presence of annexin A6 on the cell surface of variety cells as putative receptors and or binding proteins for chondroitin sulfate proteoglycans, helping cells to bind with this extracellular matrix glycosaminoglycan chondroitin sulfate which is related to the cell-substratum adhesion. A post-tranlational modification other than direct protein phosphorylation may influence the activity of annexin6 and provide evidence linking cell growth with regulation of annexin 6 function.

Expression system: P. pastoris (Yeast)
Length: 2-320, Full Length of Mature Protein
Activity: Not Tested

S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from the neural crest, chondrocytes, macrophages, dendritic cells, etc. S1 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A10, also known as Calpactin I light chain, Cellular ligand of annexin II, S100 calcium-binding protein A10, p10 protein, p11, ANX2LG and S100A10, is a member of the S100 family of small, dimeric EF hand-type Ca(2+)-binding proteins that generally modulate cellular target proteins in response to intracellular Ca(2+) signals. In contrast to all other S100 proteins, S100A10 is Ca(2+) insensitive because of amino acid replacements in its Ca(2+)-binding loops that lock the protein in a permanently active state. S100A10 forms a heterotetramer with annexin IIH and promotes carcinoma invasion and metastasis by plasminogen activation. S100A10 and annexin II contribute to the aggressive characteristics of anaplastic carcinoma, while playing a constitutive role in papillary carcinoma. S100A10 induces the dimerization of ANXA2 p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target of tyrosine-specific kinase. S100A10 functions as a linker tethering certain transmembrane proteins to annexin A2 thereby assisting their traffic to the plasma membrane and or their firm anchorage at certain membrane sites.

Expression system: E. coli
Length: 1-324, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 2-346, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 5-322, Partial
Activity: Not Tested

Expression system: E. coli
Length: 2-339, Full Length of Mature Protein
Activity: Not Tested