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Alpha-2-macroglobulin Mouse Monoclonal Antibody [A5-A9] (M1510-22)

Price: Regular price $350.00

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Catalog# M1510-22

Mouse Monoclonal to Alpha-2-macroglobulin

Tested for

  • WB

  • IF-Cell

  • IHC-P

  • ELISA

Reacts with

  • Human

Safety datasheet

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Specifications

Product Type

Mouse monoclonal primary

Product Name

Alpha-2-macroglobulin Mouse Monoclonal Antibody [A5-A9] (M1510-22)

Immunogen

Recombinant protein within human alpha-2-macroglobulin aa 950-1200.

Host

Mouse

Positive Control

LOVO cell lysates, LO2 cell lysates, Hela, HepG2, human liver tissue, human uterus tissue.

Conjugation

Unconjugated

Clonality

Monoclonal

Clone Number

A5-A9

RRID

AB_3073134

APPLICATION DILUTION

  • WB

  • 1:500-1:1,000

  • IF-Cell

  • 1:50-1:200

  • IHC-P

  • 1:100-1:500

  • ELISA

  • 1:1,000-1:10,000

PROPERTIES

Form

Liquid

Storage Condition

Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.

Storage Buffer

1*PBS (pH7.4), 0.2% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.

Concentration

2ug/ul

Purification

Protein G affinity purified.

Molecular Weight

Predicted band size: 163 kDa

Isotype

IgG1

TARGET

UNIPROT #

P01023

PROTEIN NAME

Alpha-2-macroglobulin

SYNONYMS

A2m antibody;A2MG_HUMAN antibody;Alpha 2 M antibody;Alpha 2M antibody;Alpha-2-M antibody;Alpha-2-macroglobulin antibody;C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5 antibody;CPAMD5 antibody;DKFZp779B086 antibody;FWP007 antibody;S863 7 antibody

SEQUENCE SIMILARITIES

Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family.

TISSUE SPECIFICITY

Secreted in plasma.

DEVELOPMENTAL STAGE

Unlike the rat protein, which is an acute phase protein, this protein is always in circulation at high levels.

SUBCELLULAR LOCATION

Secreted.

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.

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