Recombinant Mouse Serum Amyloid A-1 Protein (SAA1) Protein (His)

Name: Recombinant Mouse Serum Amyloid A-1 Protein (SAA1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00016P
Price: 549.6 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Serum Amyloid A-1 Protein (SAA1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P05366
Target Symbol	SAA1
Synonyms	Saa1; Serum amyloid A-1 protein
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GFFSFVHEAFQGAGDMWRAYTDMKEANWKNSDKYFHARGNYDAAQRGPGGVWAAEKISDGREAFQEFFGRGHEDTIADQEANRHGRSGKDPNYYRPPGLPDKY
Expression Range	20-122aa
Protein Length	Full Length of Mature Protein
Mol. Weight	17 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Major acute phase protein.
Subcellular Location	Secreted.
Protein Families	SAA family
Database References	KEGG: mmu:20208 STRING: 10090.ENSMUSP00000119150 UniGene: Mm.148800
Tissue Specificity	Detected in blood plasma (at protein level). Detected in liver.

Gene Functions References

Study concludes that the transfer of serum amyloid A1 protein depends on direct cell-to-cell contacts or tunneling nanotubes. PMID: 28361953
High SAA1 expression in the stromal component is associated with pancreatic tumors. PMID: 29351990
findings show that high-density lipoprotein binding blocks fibril formation from soluble SAA1 protein, whereas internalization into mononuclear phagocytes leads to formation of amyloid; SAA1 aggregation in the cell model disturbs the integrity of vesicular membranes and leads to lysosomal leakage and apoptotic death PMID: 28637682
These findings suggest that A-SAA is functionally linked to pulmonary inflammation in this O3 exposure model and that A-SAA could be an important systemic signal of O3 exposure to the CNS.- PMID: 28533327
SAA and TLR4 have a role in skin inflammation PMID: 27502577
Data indicate that SAA1 overexpressing mice (TG) show significant deficits in social behaviors, including impaired social recognition and reduced social interaction. Study detected exogenous SAA1 expression in the brain of TG mice, implying that liver-derived SAA1 migrates to the brain. Results show an increase in the accumulation of the 87kDa form of Abeta in TG mice compared to wild type mice. PMID: 27608955
Sustained, elevated levels of SAA1 were correlated with metabolic parameters and local cytokine expression in the liver following 16 weeks on the high-fat diet. We suggest that SAA1-derived amyloid deposition under long-term high-fat diet exposure may be associated with the complications of high-fat diet-induced obesity and metabolic disorders. PMID: 27218680
Serum Amyloid A induces inflammation, proliferation and cell death in activated hepatic stellate cells. PMID: 26937641
Thermal transitions in serum amyloid A in solution and on the lipid: implications for structure and stability of acute-phase HDL PMID: 26022803
Serum amyloid A1alpha induces paracrine IL-8/CXCL8 via TLR2 and directly synergizes with this chemokine via CXCR2 and formyl peptide receptor 2 to recruit neutrophils. PMID: 26297794
Robust IL-17A production was restricted to the ileum, where SFB makes direct contact with the epithelium and induces serum amyloid A proteins 1 and 2 (SAA1/2), which promote local IL-17A expression in RORgammat(+) T17 cells. PMID: 26411290
SAA protein levels increased in both serum and lung within 2-24h after mice were exposed to Aspergillus spores. SAA mRNA levels increased within the first hour after mice were exposed to A. fumigatus. PMID: 23603100
Saa1 might be a novel inflammatory factor that acts as a chemokine modulator in hepatitis. PMID: 25847238
GAGs may have an intrinsic and divergent influence on the aggregation and fibrillation of HDL-free SAA1.1 in vivo PMID: 24878279
CE/J mice possess functional Saa1 and Saa2 genes with identical amino acid sequence. PMID: 24228751
we find no evidence that adipose tissue-derived hSAA1 influences the development of insulin resistance or obesity-related inflammation. PMID: 23967285
Its gene hold broader diversity and greater complexity and these characteristics were likely attained through gene duplication and repeated gene conversion events in the Mus lineage. PMID: 24521869
The absence of endogenous SAA1.1 and 2.1 does not affect atherosclerotic lipid deposition in apolipoprotein E-deficient mice fed either normal or Western diets. PMID: 24265416
SAA up-regulates Lp-PLA2 production significantly via a FPRL1/MAPKs./PPAR-gamma signaling pathway. PMID: 23623642
Pathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2 PMID: 23223242
An increase in plasma SAA directly accelerates the progression of atherosclerosis in ApoE-/- mice. PMID: 21953420
SAA does not impact High Density Lipoprotein levels, apoA-I clearance, or High Density Lipoprotein size PMID: 20667817
Infusions of SAA-positive cells promote renal recovery after acute renal failure and offer a potentially powerful and novel therapy of renal failure. PMID: 20534870
Serum amyloid A has a role in promoting cholesterol efflux mediated by scavenger receptor B-I PMID: 16120612
Plasma A-SAA elevation was due to induction of Saa1 and Saa2 expression in liver but not in adipose tissue. PMID: 18584041

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.