ARG41453

anti-alpha 2 Macroglobulin antibody

anti-alpha 2 Macroglobulin antibody for Western blot,IHC-Formalin-fixed paraffin-embedded sections and Human

Overview

Product Description Rabbit Polyclonal antibody recognizes alpha 2 Macroglobulin
Tested Reactivity Hu
Tested Application IHC-P, WB
Host Rabbit
Clonality Polyclonal
Isotype IgG
Target Name alpha 2 Macroglobulin
Antigen Species Human
Immunogen Synthetic peptide of Human alpha 2 Macroglobulin.
Conjugation Un-conjugated
Alternate Names CPAMD5; Alpha-2-macroglobulin; S863-7; FWP007; Alpha-2-M; A2MD; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5

Application Instructions

Application Suggestion
Tested Application Dilution
IHC-P1:50 - 1:200
WB1:500 - 1:2000
Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.
Positive Control Human plasma

Properties

Form Liquid
Purification Affinity purified.
Buffer PBS (pH 7.4), 150 mM NaCl, 0.02% Sodium azide and 50% Glycerol.
Preservative 0.02% Sodium azide
Stabilizer 50% Glycerol
Storage Instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.
Note For laboratory research only, not for drug, diagnostic or other use.

Bioinformation

Database Links

GeneID: 2 Human A2M

Swiss-port # P01023 Human Alpha-2-macroglobulin

Gene Symbol A2M
Gene Full Name alpha-2-macroglobulin
Background Alpha-2-macroglobulin is a protease inhibitor and cytokine transporter. It inhibits many proteases, including trypsin, thrombin and collagenase. A2M is implicated in Alzheimer disease (AD) due to its ability to mediate the clearance and degradation of A-beta, the major component of beta-amyloid deposits. [provided by RefSeq, Jul 2008]
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. [UniProt]
Cellular Localization Secreted. [UniProt]
Calculated MW 163 kDa