Human Annexin A5 Protein, His Tag

Proteins and Peptides

貨號 Cat. No.
AN5-H5123
規格 Size
100ug
品牌 Brand
ACROBiosystems
Species
Human
Conjugate
Unconjugated
Expression System
E. coli
Tag
His Tag

Description




Source : 


Human Annexin A5, His Tag (AN5-H5123) is expressed from E.coli cells. It contains AA Met 1 - Asp 320 (Accession # P08758-1).


 

Molecule : Annexin A5


 

Synonyms : ANXA5,ANX5,ENX2,PP4,Annexin V,Annexin A5


 

Format : Powder


 

Category : Other Recombinant Proteins


 

Accession : AAH01429


 

Storage : -20℃


 

Shipping condition : Powder,RT


 

Molecular Weight : 36.8 kDa


 

Characteristics :


This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 36.8 kDa. The protein migrates as 35 kDa under reducing (R) condition (SDS-PAGE).


 

Endotoxin Level : Less than 1.0 EU per μg by the LAL method.


 

Buffer : PBS, pH7.4


 

Description :


Anexin A5 is a phospholipid binding protein, which binds with high affinity and selectivity to PS in the presence of calcium. PS is predominantly located in membrane leaflets, which face the cytosol. However, recent findings show that each cell type has the molecular machinery to expose PS at its cell surface. This machinery is activated during the execution of apoptosis. Once PS is exposed at the cell surface it exhibits procoagulant and proinflammatory activities. Anexin A5 will bind to the PS-exposing apoptotic cell and can inhibit the procoagulant and proinflammatory activities of the dying cell. Anexin A5 has also been identified as an anticoagulant protein in the blood coagulation cascade, by acting as an inhibitor of prothrombin activation. The presence of antibodies to Anexin A5 is associated with systemic lupus erythematosus (SLE), recurrent spontaneous abortions and systemic sclerosis (SSc).


 

References :


(1) Adekunle I. Elegbede a, D.K. Srivastava,et al. 2006, Protein Expression and PuriWcation 50: 157–162.
(2) Bent Brachvogela, Heike Welzel, et al. 2001, Mechanisms of Development 109: 389–393.





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