SAA Canine

Serum Amyloid A (APO-SAA) Canine Recombinant

SAA Canine, produced in E. coli, is a single, non-glycosylated polypeptide chain (amino acids 1-111) containing 121 amino acids. It has a molecular mass of 13,766 Daltons. The SAA is fused with a 10 amino acid affinity tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21790
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

SAA Equine

Serum Amyloid A (APO-SAA) Equine Recombinant

SAA Equine, produced in E. coli, is a single, non-glycosylated polypeptide chain (amino acids 1-110) containing 120 amino acids and having a molecular mass of 13,580 Daltons. SAA is fused with a 10 amino acid affinity tag at the N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21853
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

SAA Feline

Serum Amyloid A (APO-SAA) Feline Recombinant

SAA Feline, produced in E.coli, is a single, non-glycosylated polypeptide chain (amino acids 1-111) containing 121 amino acids. It has a molecular mass of 13,838 Daltons. The SAA is fused with a 10 amino acid His tag at the N-terminus and purified using 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

Recombinant Human APO-SAA, produced in E. coli, is a single-chain polypeptide. This non-glycosylated protein comprises 104 amino acids with a molecular weight of 11.7 kDa. It is important to note that while this Recombinant Apo-SAA represents a consensus SAA molecule corresponding to human Apo-SAA1a, there are slight variations. These include an N-terminal methionine residue, an asparagine substitution for aspartic acid at position 60, and arginine replacing histidine at position 71. It's worth noting that the latter two substitutions are naturally found in the Apo-SAA2b isoform. The purification of Human APO-SAA is achieved using proprietary chromatographic techniques, ensuring a high degree of purity.
Shipped with Ice Packs
Cat. No.
BT21979
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

SAA1 Human

Serum Amyloid A (APO-SAA1) Human Recombinant

Recombinant human SAA1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 104 amino acids. With a molecular weight of 11.7 kDa, it undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22033
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

SAA1 Human, His

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

Recombinant human SAA1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 125 amino acids (residues 19-122). It has a molecular weight of 13.9 kDa. The protein is engineered with a 20-amino acid His-tag at the N-terminus to facilitate purification, which is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT22144
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

SAA1 Monkey

Serum Amyloid A (APO-SAA1) Rhesus Macaque Recombinant

This product consists of recombinant SAA1 protein derived from monkey and produced in E. coli. It is a single, non-glycosylated polypeptide chain with 104 amino acids, resulting in a molecular mass of 11.8 kDa. The protein undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT22211
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

SAA2 Human

Serum Amyloid A2 Human Recombinant

Recombinant human SAA2, produced in E. coli, is a single, non-glycosylated polypeptide chain containing an N-terminal methionine. It has a molecular mass of 11.76 kDa. SAA2 Human is purified using 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

Recombinant human SAA4, expressed in E. coli, is fused with a 21 amino acid His tag at its N-terminus. This non-glycosylated polypeptide chain comprises 131 amino acids (21-130 a.a.) and has a molecular weight of 14.9 kDa. Purification of SAA4 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT22353
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.
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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