Rabbit anti-Human A2ML1 Polyclonal Antibody | anti-A2ML1 antibody

A2ML1 Antibody

Cat. Num. AAA9629692

• Gene Names: A2ML1; CPAMD9
• Reactivity: Human
• Applications: ELISA
• Purity: The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin (Thermo Fisher Scientific).
• Synonyms: A2ML1; Polyclonal Antibody; A2ML1 Antibody; A2ML 1; Alpha 2 macroglobulin like 1; Alpha 2 macroglobulin like protein 1; C3 and PZP like alpha 2 macroglobulin domain containing protein 9; CPAMD9; DKFZp686C1729; DKFZp686D2011; DKFZp686G1812; DKFZp686L1821; DKFZp686O1010; FLJ16045; FLJ25179; FLJ39129; FLJ41597; FLJ41598; FLJ41607; anti-A2ML1 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: Rabbit IgG
• Specificity: A2ML1 Antibody detects endogenous levels of total A2ML1.
• Purity/Purification: The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin (Thermo Fisher Scientific).
• Form/Format: Liquid. Rabbit IgG in phosphate buffered saline, pH7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
• Concentration: 1mg/ml (varies by lot)

• Applicable Applications for anti-A2ML1 antibody: ELISA (EIA)(peptide)
• Application Notes: ELISA(peptide): 1:20000-1:40000
• Immunogen: A synthesized peptide derived from Human MYOCD.
• Conjugation: Unconjugated
• Similarity: Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family.
• Subunit Structure: Monomer.
• Tissue Specificity: In the epidermis, expressed predominantly in the granular layer at the apical edge of keratinocytes (at protein level). Also detected in placenta, testis and thymus but not in epithelia of kidney, lung, small intestine or colon.
• Function: 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 (By similarity). Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases.
• Preparation and Storage: Store at -20 degree C. Stable for 12 months from date of receipt.

Product Categories/Family for anti-A2ML1 antibody

Secreted; Primary

NCBI and Uniprot Product Information

• NCBI GI #: 539846446
• NCBI GeneID: 144568
• NCBI Accession #: NP_001269353.1
• NCBI GenBank Nucleotide #: NM_001282424.1
• UniProt Accession #: A8K2U0; Q2M224; Q6ZW52; Q6ZW53; Q8N1M4; Q96LQ8; B5MDD1
• Molecular Weight: 161,107 Da
• NCBI Official Full Name: alpha-2-macroglobulin-like protein 1 isoform 2
• NCBI Official Synonym Full Names: alpha-2-macroglobulin-like 1
• NCBI Official Symbol: A2ML1
• NCBI Official Synonym Symbols: CPAMD9
• NCBI Protein Information: alpha-2-macroglobulin-like protein 1; A2ML1 {ECO:0000312|EMBL:AAI12132.1}; C3 and PZP-like, alpha-2-macroglobulin domain containing 9
• UniProt Protein Name: Alpha-2-macroglobulin-like protein 1
• Protein Family: Alpha-2-macroglobulin-like protein
• UniProt Gene Name: A2ML1

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 (). Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases.