A2M / CPAMD5 / Alpha-2-macroglobulin Recombinant Protein | A2M recombinant protein

Recombinant Human A2M / CPAMD5 / Alpha-2-macroglobulin Protein (His tag)

Cat. Num. AAA2545995

• Gene Names: A2M; A2MD; CPAMD5; FWP007; S863-7
• Purity: > 92 % as determined by SDS-PAGE
• Synonyms: A2M / CPAMD5 / Alpha-2-macroglobulin; Recombinant Human A2M / CPAMD5 / Alpha-2-macroglobulin Protein (His tag); A2mp; A2M recombinant protein

• Host: Baculovirus-Insect Cells
• Purity/Purification: > 92 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4
• Sequence Length: 1474

• Application Notes: The recombinant human A2M consists of 1461 amino acids and predicts a molecular mass of 164 kDa. The apparent molecular mass of rhA2M is approximately 160-170 kDa in SDS-PAGE under reducing conditions.
• Predicted N Terminal: Ser 24
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

Related Product Information for A2M recombinant protein

Background: alpha-2-macroglobulin, also known as alpha2-macroglobulin (alpha2M and A2M), is an abundant protein of the plasma of vertebrates and members of several invertebrate phyla and functions as a broad-spectrum protease-binding protein. alpha-2-macroglobulin is produced by the liver, and is a major component of the alpha-2 band in protein electrophoresis. alpha-2-macroglobulin is a large plasma glycoprotein that has long been known as an irreversible inhibitor of a variety of proteinases. More recently, it has been reported that numerous growth factors, cytokines and hormones bind to alpha 2M through diverse mechanisms. A2M is also produced in the brain where it binds multiple extracellular ligands and is internalized by neurons and astrocytes. In the brain of Alzheimer's disease (AD) patients, A2M has been localized to diffuse amyloid plaques. A2M also binds soluble beta-amyloid, of which it mediates degradation. Protease-conjugated alpha2-macroglobulin is selectively bound by cells contacting the body fluids and alpha2-macroglobulin and its protease cargo are then internalized and degraded in secondary lysosomes of those cells. In addition to this function as an agent for protease clearance, alpha2-macroglobulin binds a variety of other ligands, including several peptide growth factors and modulates the activity of a lectin-dependent cytolytic pathway in arthropods.

Description: A DNA sequence encoding the human A2M (NP_000005.2) (Met 1-Ala 1474) was expressed, fused with a polyhistidine tag at the C-terminus.

NCBI and Uniprot Product Information

• NCBI GI #: 66932947
• NCBI GeneID: 2
• NCBI Accession #: NP_000005.2
• NCBI GenBank Nucleotide #: NM_000014.5
• UniProt Accession #: P01023; Q13677; Q59F47; Q5QTS0; Q68DN2; Q6PIY3; Q6PN97
• Molecular Weight: 163,291 Da
• NCBI Official Full Name: alpha-2-macroglobulin isoform a
• NCBI Official Synonym Full Names: alpha-2-macroglobulin
• NCBI Official Symbol: A2M
• NCBI Official Synonym Symbols: A2MD; CPAMD5; FWP007; S863-7
• NCBI Protein Information: alpha-2-macroglobulin
• UniProt Protein Name: Alpha-2-macroglobulin
• Protein Family: Alpha-2-macroglobulin
• UniProt Gene Name: A2M
• UniProt Synonym Gene Names: CPAMD5; Alpha-2-M

NCBI Description

The protein encoded by this gene is a protease inhibitor and cytokine transporter. It uses a bait-and-trap mechanism to inhibit a broad spectrum of proteases, including trypsin, thrombin and collagenase. It can also inhibit inflammatory cytokines, and it thus disrupts inflammatory cascades. Mutations in this gene are a cause of alpha-2-macroglobulin deficiency. This gene is implicated in Alzheimer's disease (AD) due to its ability to mediate the clearance and degradation of A-beta, the major component of beta-amyloid deposits. A related pseudogene, which is also located on the p arm of chromosome 12, has been identified. [provided by RefSeq, Nov 2016]

Uniprot Description

Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.