Other Proteins

Recombinant Human Apo-SAA

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Product Details

Catalogue Number: 300-13
Description:


Recombinant Human Apo-SAA

Human Apo-SAA is a 104 amino acid polypeptide that circulates primarily in association with high-density lipoproteins (HDL). The level of Apo-SAA, normally 1-5 μg/ml in plasma, increases 500-1000 fold within 24 hours of an inflammatory stimulus and, under these conditions, is the most abundant HDL apolipoprotein. The human SAA gene codes for a 122 amino acid polypeptide, which contains an 18 amino acid N-terminal signal sequence. Recombinant Apo-SAA is a consensus SAA molecule corresponding to human Apo-SAA1α, except for the presence of an N-terminal methionine, the substitution of asparagine for aspartic acid at position 60, and arginine for histidine at position 71 (the latter two substituted residues are present in Apo-SAA2β).  The calculated molecular weight of Recombinant Human Apo-SAA is 11.7 kDa.

Source: E.coli

Synonyms: Serum amyloid A protein (SAA), Serum amyloid A apolipoprotein, Amyloid fibril protein AA, TP53I4, PIG4

AA Sequence: MRSFFSFLGE AFDGARDMWR AYSDMREANY IGSDKYFHAR GNYDAAKRGP GGVWAAEAIS NARENIQRFF GRGAEDSLAD QAANEWGRSG KDPNHFRPAG LPEKY

Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Tested by its ability to down-regulate lipid biosynthesis in aortic smooth muscle cells. The effective concentration was found to be 4 μM.*

* Schreiber, BM. et al. Biochem J. 1999 Nov 15; 344 Pt 1:7-13

Calculated Molecular Weight: 11.7 kDa

Accession Number: P0DJI8

Gene ID: 6288

crossreactivity:
Country Of Origin: USA

Not for human use.

Research Interest

product.subtitle.recentcitations

First Author
Li, W
Title
Connexin 43 Hemichannel as a Novel Mediator of Sterile and Infectious Inflammatory Diseases.
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Scientific Reports; 8(1) pg166
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First Author
He, R L
Title
Serum amyloid A induces G-CSF expression and neutrophilia via Toll-like receptor 2.
Citation
Blood; 113(2) pg429-37
PubMed Id
First Author
Lu, J
Title
Structural mechanism of serum amyloid A-mediated inflammatory amyloidosis.
Citation
Proceedings of the National Academy of Sciences of the United States of America; 111(14) pg5189-94
PubMed Id