Serum amyloid A-1 protein (SAA1)
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BackgroundFunction Serum amyloid A (SAA) proteins function as cytokine-like proteins with roles in the acute phase response, lipid transport and metabolism, cell-cell communication, atherosclerosis, and feedback in inflammatory, neoplastic, immunologic, and protective pathways1. SAA proteins are normally found at low levels in healthy individuals, but after the onset of the acute phase response, SAA levels can increase by 1000-fold within 24 hours, with levels decreasing back to normal when the event resolves. However, elevated levels of SAA can persist when inflammation is chronic. Acute-phase SAA is tightly bound to high-density lipoprotein (HDL) and functions as an apolipoprotein. Mechanism and pathways The human genome encodes four major variants of SAA (SAA1-4), with Saa3 being a transcribed pseudogene1. SAA1 and SAA2 are involved in the classic acute phase response and are synthesized and secreted by the liver (hepatocytes), macrophages, adipocytes, kidney, lung, and mammary gland cells. Transcription of Saa1 and Saa2 is also observed in synovial and brain cells. During the acute phase response, SAA1 expression is regulated by many transcription factors (NF-κB, C/EBP, YY1, AP-2, SAF, Sp1, STAT3), proinflammatory cytokines (IL-1β, IL-6, TNF-α), and glucocorticoids2. SAA4 is constitutively expressed1. SAA1 is a major precursor of amyloid A and is known to form pathogenic amyloid fibrils when over-produced or aberrantly processed2. Additionally, SAA1 is used as a clinical biomarker for inflammatory disorders2 and may be useful as a prognostic marker in the tumor microenvironment3 or for metastasis of hepatocellular4 and renal cell5carcinomas. Additionally, SAA1 has been suggested as a novel therapeutic target of pancreatic cancer6. Structure Mature SAA1 protein consists of 104 amino acids and is a hexamer stabilized by its C-terminal tail2. SAA proteins are poorly soluble in aqueous solutions, and concentrations needed to characterize their 3D structure are difficult to acquire1. Heparin sulfate disrupts SAA binding to HDL. Protein DetailsSpecies Human Format Purified No Carrier Protein Protein Accession No. P0DJI8 Amino Acid Sequence MRSFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY State of Matter Lyophilized SDS-Page Molecular Weight ~15k Predicted Molecular Mass ~12k Reconstitution Reconstitute at 0.1-1 mg/ml using filtered deionized water. Gently mix by vortexing and/or inversion until fully dissolved. Centrifuge if necessary. Storage and Stability This lyophilized protein is stable for twelve months when stored at -20°C to -70°C. After aseptic reconstitution, this protein may be stored for one month at 2°C to 8°C or for three months at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. Country of Origin USA Shipping Frozen Dry Ice Species Human Regulatory Status Research Use Only NCBI Gene Bank UniProt.org Applications and Recommended Usage ? (Quality Tested by Leinco) SDS-Page, WB, Elisa, FA References & Citations1 Sack GH Jr. Mol Med. 24(1):46. 2018. 2 Sun L, Ye RD. Gene. 583(1):48-57. 2016. 3 Xu Z, Wu Y, Fu G, et al. Int J Mol Sci. 24(8):7505. 2023. 4 Li G, Shen Q, Xu H, et al. Front Oncol. 13:1138995. 2023. 5 Li S, Cheng Y, Cheng G, et al. Front Oncol. 11:649761. 2021. 6 Takehara M, Sato Y, Kimura T, et al. Cancer Sci. 111(8):2883-2894. 2020. 7 Jiang B, Wang D, Hu Y, et al. Mol Metab. 59:101462. 2022. 8 Cao K, Jiang X, Wang B, et al. Front Neurol. 13:905561. 2022. 9 Bang YJ, Hu Z, Li Y, et al. Science. 373(6561):eabf9232. 2021. 10 Lee JY, Hall JA, Kroehling L, et al. Cell. 180(1):79-91. 2020. Technical ProtocolsCertificate of AnalysisIMPORTANT Use lot specific datasheet for all technical information pertaining to this recombinant protein. |
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