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- Table of Contents
2 Citations 8 Q&As
Facts about Alpha-2-macroglobulin.
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).
Human | |
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Gene Name: | A2M |
Uniprot: | P01023 |
Entrez: | 2 |
Belongs to: |
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protease inhibitor I39 (alpha-2-macroglobulin) family |
A2M; alpha 2Macroglobulin; alpha 2-Macroglobulin; alpha-2-M; alpha-2-macroglobulin; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5; CPAMD5; CPAMD5DKFZp779B086; FWP007; S863-7
Mass (kDA):
163.291 kDA
Human | |
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Location: | 12p13.31 |
Sequence: | 12; NC_000012.12 (9067708..9116229, complement) |
Secreted in plasma.
Secreted.
The Alpha-2-macroglobulin (A2M) marker is used in many biological assays. These antibodies, which can be monoclonal or polyclonal, recognize Alpha-2-macroglobulin in many animal samples. Boster Bio developed antibodies to recognize A2M using rabbit and mouse as models. The antibodies have an area of bait that has specific cleavage sites for multiple proteinases. It keeps the proteinase or enzyme active against high and low molecular-weight substrates by capturing it.
Biotinylatedlectins offer many advantages. Biotinylation of a cell's outer protein can result in an increase in cell adhesion as well as migration. These results are particularly useful for assessing the effects of biotin on adhesion of cancerous cells. Boster Bio's biotinylated and lectin-based biotins are especially effective in cell adhesion, invasion and migration tests. Biotinylation also increases the strength of binding.
These findings suggest that simultaneous binding of a lectin can be achieved. It is possible to enhance the affinity of a lectin's binding by clustering it with multiple glycans. The question is , how? WGA and CEA had the highest binding affinity of all the lectins in Boster Bio's series. Their binding affinity is less than those monomer counterparts.
The lectin screening kit includes seven biotinylated Linctins. The linctins used were selected due to their specificity to sugars. The lectins in the kit were of the same quality as those in the individual lectin reagent kits. These findings must be confirmed and biotinylatedlectins could help in this process.
Glycan-binding proteins are crucial to understand the changes in cell surface glycosyls in different diseases and tissues. A sugar-binding microarray containing over 100 lectins may be used to determine the totality of cell Glycans. Moreover, the arrays can detect small differences between cells. Specific lectins may also be used to create diagnostic tests.
This anti-calreticulin/CALR antibody from Boster Bio has been tested using both ELISA and Flow Cytometry. It is able to bind to both Human and Mouse the calreticulin protein and then reacts with them. This anti-calreticulin antibody is extremely specific to a variety applications and is suitable for researchers working with cancer cells. The boster bio antibody is extremely specific to the human calreticulin/CALR.
CALR is a calcium-binding chaperone which promotes folding, oligomeric assembly and quality control of proteins within the ER's endoplasmic reticulum. It also interacts with monoglucosylated glycoproteins in the ER and mediates nuclear export. It may also play an important role during the maturation of oocytes. There are numerous antibodies to this protein in different forms that can be used for analyzing different processes within the human body.
In a recent study CALR inhibited p53 and pJNK. ZsGreen-expressing cells could be identified after 72 hours following lentiviral transfection. After a western blot analysis, the expression of CALR mRNA and levels of the protein were measured using the RTQPCR method and western blot. GAPDH was used as an internal reference protein. Specific phosphorylated-to-total protein ratios are shown to indicate CALR-containing proteins.
A2M-specific antibody can be used in a variety biological tests. These antibodies, both monoclonal and polyclonal, recognize Alpha-2-macroglobulin in many animal samples. Boster Bio developed antibodies by using mouse and rabbit as models. The antibodies include bait regions with specific cleavage locations for different proteinases. The proteins trapped in these regions retain activity against low or high-molecular-weight substrates.
PMID: 2581245 by Kan C.-C., et al. Nucleotide sequence of cDNA encoding human alpha 2-macroglobulin and assignment of the chromosomal locus.
PMID: 15611997 by Lin V.K., et al. Alpha(2) macroglobulin, a PSA-binding protein, is expressed in human prostate stroma.
*More publications can be found for each product on its corresponding product page