Thermo Fisher Scientific Human Apo-SAA Recombinant Protein, PeproTech

Applications

Tested Dilution

Publications

Western Blot (WB)

-

View 2 publications 2 publications

ELISA (ELISA)

-

View 1 publication 1 publication

Functional Assay (Functional)

Assay-dependent

-

Immunoelectrophoresis (IE)

-

View 1 publication 1 publication

In vitro Assay (IV)

-

View 35 publications 35 publications

Miscellaneous PubMed (Misc)

-

View 10 publications 10 publications

Product Specifications

Species

Human

Published species

Bacteria, Hamster, Human, Mouse, Rat

Expression System

E. coli

Amino acid sequence

MRSFFSFLGE AFDGARDMWR AYSDMREANY IGSDKYFHAR GNYDAAKRGP GGVWAAEAIS NARENIQRFF GRGAEDSLAD QAANEWGRSG KDPNHFRPAG LPEKY

Molecular weight

11.7 kDa

Class

Recombinant

Type

Protein

Purity

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

Endotoxin concentration

<1 EU/µg

Activity

Tested by its ability to down-regulate lipid biosynthesis in aortic smooth muscle cells. The effective concentration was found to be 4 uM. * Schreiber, BM. et al. Biochem J. 1999 Nov 15; 344 Pt 1:7-13

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Purification

purified

Contains

no preservative

Storage conditions

-20°C

Shipping conditions

Ambient

Product Specific Information

Recombinant Apo-SAA is a consensus SAA molecule corresponding to human Apo-SAA1alpha, 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-SAA2beta). The calculated molecular weight of Recombinant Human Apo-SAA is 11.7 kDa.

This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis

Target Information

The serum amyloid A family comprises a number of differentially expressed apolipoproteins, acute-phase SAA1 and SAA2, the former being the major component in plasma and constitutive SAAs. Although the liver is the primary site of synthesis of both SAA types extrahepatic production has been reported. The in vivo concentrations increase by as much as 1000 fold during inflammation. Several studies have expressed its importance in the diagnosis and monitoring of various diseases. Pathological SAA values are often detected in association with normal CRP concentrations; SAA rises earlier and more sharply than CRP. Recently, a broader view of SAA expression and function has been emerging.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.