Recombinant Mouse Serum Amyloid A-3 Protein (SAA3) Protein (His)

Beta LifeScience SKU/CAT #: BLC-03242P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Serum Amyloid A-3 Protein (SAA3) Protein (His)

Beta LifeScience SKU/CAT #: BLC-03242P
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Product Overview

Description Recombinant Mouse Serum Amyloid A-3 Protein (SAA3) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P04918
Target Symbol SAA3
Synonyms Saa3; Serum amyloid A-3 protein
Species Mus musculus (Mouse)
Expression System Yeast
Tag N-6His
Target Protein Sequence RWVQFMKEAGQGSRDMWRAYSDMKKANWKNSDKYFHARGNYDAARRGPGGAWAAKVISDAREAVQKFTGHGAEDSRADQFANEWGRSGKDPNHFRPAGLPKRY
Expression Range 20-122aa
Protein Length Full Length of Mature Protein
Mol. Weight 13.8kDa
Research Area Others
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 reactant. Apolipoprotein of the HDL complex.
Subcellular Location Secreted.
Protein Families SAA family
Database References

KEGG: mmu:20210

STRING: 10090.ENSMUSP00000006956

UniGene: PMID: 29351990

  • This study suggests that the level of expression of the Saa3 gene could be utilized for the number of infiltrated macrophages in obese adipose tissue. PMID: 27929048
  • BMDC lacking SAA3 demonstrate an impaired endotoxin tolerance response and inhibited responses to retinoic acid. Our findings indicate that endogenous SAA3 modulates metabolic and immune homeostasis PMID: 29390039
  • The induction of Saa3 by PTH may explain the suppression of bone formation when PTH is applied continuously and may be a new therapeutic target for osteoporosis. PMID: 26703472
  • results also suggest that Saa3 influences liver-specific SAA1/2 expression, and that SAA3 could play a larger role in the acute phase response than previously thought PMID: 25251243
  • Expression of Saa3 in osteoblasts positively correlates with increased cellular maturation toward the osteocyte phenotype. PMID: 25491310
  • Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection. PMID: 25073702
  • these data suggest a novel mechanism by which Mo MDSCs mediate inflammation through SAA3-TLR2 signaling and thus exacerbate cancer progression by a STAT3-dependent mechanism. PMID: 24659444
  • Hypoxia leads to a substantial increase in SAA3 mRNA and protein level, apparently in a time-dependent manner (threefold in 48 h), in fully differentiated 3T3-L1, followed by reestablishment of gene expression to basal levels after 24 h of reoxygenation. PMID: 23605472
  • Using various synthetic peptide fragments, it was shown that SAA3 directly binds MD-2 and activates the MyD88-dependent TLR4/MD-2 pathway, induced IL-6 and TNF-alpha, and recruited CD11b(+)Gr-1(+) cells to the lung. PMID: 23858030
  • HSV-1 induces and activate TLR2 and TLR4 receptors directly through interaction of astrocytes with the pathogen and also indirectly by endogenous ligands produced locally, such as serum amyloid A, potentiating the neuroinflammatory response. PMID: 22622619
  • Saa3 is expressed in the lungs of mice exposed to several mixed T helper (Th) type 2/Th17-polarizing allergic sensitization regimen and is implicated in the pathogenesis of experimental allergic asthma. PMID: 21622869
  • cAMP in combination with TNF specifically induced C/EBPbeta protein, leading to enhanced SAA3 expression but requiring NF-kappaB in mouse granulose cells. The data indicate SAA may play a role in events occurring during the ovulation process. PMID: 20444945
  • A 210-bp fragment of the mouse SAA3 promoter when placed in front of the LacZ gene was sufficient to confer basal and inflammation-induced reporter gene expression. PMID: 11791617
  • tumor necrosis factor-alpha likely increased serum amyloid A 3 promoter activity and protein by activating nuclear factor-kappaB signaling via tumor necrosis factor receptor 1 in mouse granulosa cells PMID: 14749357
  • Adipocyte hypertrophy leads to increased production of SAA and hyaluronan, which srecruit and retains monocytes, thereby leading to local inflammation in adipose tissue. PMID: 17563062
  • These data show a potent upregulation of SAA3 by IL-1beta. PMID: 18452164
  • In adipose tissue Saa3 was the predominant isoform and the earliest inflammatory marker induced, suggesting it is important for initiation of adipose tissue inflammation. PMID: 18584041
  • Results indicate that the expression of SAA3 in adipose tissue is upregulated by obesity, but it does not contribute to the circulating pool of SAA in mice. PMID: 19286646
  • serum amyloid A3 (SAA3) is regulated in mouse colonic epithelium and adipose tissue by the intestinal microbiota PMID: 19513118
  • 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.

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