SAA Canine

Serum Amyloid A (APO-SAA) Canine Recombinant

SAA Canine produced in E.coli is a single, non-glycosylated polypeptide chain (1-111 a.a) containing 121 a.a and having a molecular mass of 13,766 Dalton. SAA s fused with a 10 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT21790
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

SAA Equine

Serum Amyloid A (APO-SAA) Equine Recombinant

SAA Equine produced in E.coli is a single, non-glycosylated polypeptide chain (1-110 a.a) containing 120 a.a and having a molecular mass of 13,580 Dalton. SAA s fused with a 10 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT21853
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

SAA Feline

Serum Amyloid A (APO-SAA) Feline Recombinant

SAA Feline produced in E.coli is a single, non-glycosylated polypeptide chain (1-111 a.a) containing 121 a.a and having a molecular mass of 13,838 Dalton. SAA s fused with a 10 amino acids His tag at N-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT21901
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

SAA Human

Serum Amyloid A (APO-SAA) Human Recombinant

APO-SAA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 104 amino acids and having a molecular mass of 11.7kDa. Recombinant Apo-SAA is a consensus SAA molecule corresponding to human Apo-SAA1a, 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-SAA2b).
The Human APO-SAA is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21979
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

SAA1 Human

Serum Amyloid A (APO-SAA1) Human Recombinant

SAA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 104 amino acids and having a molecular mass of 11.7kDa.
The SAA1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22033
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

SAA1 Human, His

Serum Amyloid A Human Recombinant (APO-SAA1), His Tag

SAA1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (19-122 a.a.) and having a total molecular mass of 13.9 kDa.
SAA1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22144
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

SAA1 Monkey

Serum Amyloid A (APO-SAA1) Rhesus Macaque Recombinant

SAA1 monkey Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 104 amino acids and having a total molecular mass of 11.8 kDa. SAA1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22211
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

SAA2 Human

Serum Amyloid A2 Human Recombinant

SAA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing N-terminal Met and having a molecular mass of 11.76kDa. SAA2Human is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT22289
Source

Escherichia Coli.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

SAA4 Human

Serum Amyloid A4 Human Recombinant

SAA4 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 131 amino acids (21-130 a.a.) and having a molecular mass of 14.9kDa. The SAA4 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22353
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
Definition and Classification

Serum Amyloid A (SAA) proteins are a family of apolipoproteins associated with high-density lipoprotein (HDL) in plasma. They are classified into two main types: constitutive SAAs and acute-phase SAAs. Constitutive SAAs are expressed at stable levels, while acute-phase SAAs are produced in response to inflammatory stimuli .

Biological Properties

Key Biological Properties: SAA proteins are small, with approximately 104 amino acids. They are highly conserved across vertebrate evolution .

Expression Patterns: Acute-phase SAAs, such as SAA1 and SAA2, are rapidly synthesized in the liver in response to inflammatory cytokines like IL-1, IL-6, and TNF-α . Constitutive SAAs, like SAA4, are expressed at lower levels and are not significantly induced by inflammation .

Tissue Distribution: While the liver is the primary site of SAA production, these proteins can also be produced by adipocytes and other tissues .

Biological Functions

Primary Biological Functions: SAAs play a crucial role in lipid metabolism, particularly in the transport of cholesterol to the liver for secretion into bile . They also recruit immune cells to sites of inflammation and induce enzymes that degrade the extracellular matrix .

Role in Immune Responses: SAAs act as cytokine-like proteins, facilitating cell-cell communication and feedback in inflammatory and immunologic pathways . They are involved in pathogen recognition and the acute-phase response to infection .

Modes of Action

Mechanisms with Other Molecules and Cells: SAAs interact with multiple receptors, including FPR2, TLR2, TLR4, SR-BI, and P2X7 . These interactions activate transcription factors like NF-κB and play a role in epigenetic regulation through pathways such as MyD88-IRF4-Jmjd3 .

Binding Partners and Downstream Signaling Cascades: SAAs bind to HDL, glycosaminoglycans, cystatin C, and retinoic acid . These interactions trigger downstream signaling cascades that modulate inflammatory responses and lipid metabolism .

Regulatory Mechanisms

Expression and Activity Control: The expression of acute-phase SAAs is regulated by pro-inflammatory cytokines (IL-1, IL-6, TNF-α) and can be induced up to 1000-fold during acute inflammation .

Transcriptional Regulation: SAA genes are regulated at the transcriptional level by cytokines and other inflammatory mediators .

Post-Translational Modifications: Post-translational modifications of SAAs, such as phosphorylation, can influence their activity and interactions with other proteins .

Applications

Biomedical Research: SAAs are used as biomarkers for inflammation and infection due to their rapid and significant response to inflammatory stimuli .

Diagnostic Tools: SAA levels are measured in clinical settings to assess disease activity in conditions like rheumatoid arthritis, atherosclerosis, and amyloidosis .

Therapeutic Strategies: Targeting SAA pathways is being explored as a potential therapeutic approach for inflammatory diseases and amyloidosis .

Role in the Life Cycle

Development to Aging and Disease: SAAs play a role throughout the life cycle, from development to aging. They are involved in the acute-phase response during infections and injuries, and their dysregulation is associated with chronic inflammatory diseases and amyloidosis .

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