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A2ML1 blocking peptide

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Catalog # MBS9225342
Unit / Price
  0.1 mg  /  $155 +1 FREE 8GB USB
A2ML1 blocking peptide
Product Name

A2ML1, Blocking Peptide

Also Known As

A2ML1 Antibody (N-term) Blocking Peptide

Product Synonym Names
Alpha-2-macroglobulin-like protein 1; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 9; A2ML1
Antibody/Peptide Pairs
A2ML1 peptide (MBS9225342) is used for blocking the activity of A2ML1 antibody (MBS9209002)
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Length
1454
OMIM
610627
3D Structure
ModBase 3D Structure for A8K2U0
Form/Format
Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
Cellular Location
Secreted.
Tissue Location
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
Preparation and Storage
Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.
Other Notes
Small volumes of A2ML1 blocking peptide vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
A2ML1 blocking peptide
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.
NCBI/Uniprot data below describe general gene information for A2ML1. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
105,968 Da
NCBI Official Full Name
Alpha-2-macroglobulin-like protein 1
NCBI Official Synonym Full Names
alpha-2-macroglobulin like 1
NCBI Official Symbol
A2ML1  [Similar Products]
NCBI Official Synonym Symbols
CPAMD9
  [Similar Products]
NCBI Protein Information
alpha-2-macroglobulin-like protein 1
UniProt Protein Name
Alpha-2-macroglobulin-like protein 1
UniProt Synonym Protein Names
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 9
UniProt Gene Name
A2ML1  [Similar Products]
UniProt Entry Name
A2ML1_HUMAN
NCBI Summary for A2ML1
This gene encodes a member of the alpha-macroglobulin superfamily. The encoded protein is thought to be an N-glycosylated monomeric protein that acts as an inhibitor of several proteases. It has been shown to form covalent interactions with proteases, and has been reported as the p170 antigen recognized by autoantibodies in the autoimmune disease paraneoplastic pemphigus (PNP; PMID:20805888). Mutations in these gene have also been associated with some cases of Noonan syndrome (NS; PMID:24939586) as well as some cases of otitis media (PMID:26121085). Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Aug 2015]
UniProt Comments for A2ML1
A2ML1: 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. Belongs to the protease inhibitor I39 (alpha-2- macroglobulin) family.

Protein type: Secreted, signal peptide; Secreted; Inhibitor

Chromosomal Location of Human Ortholog: 12p13.31

Cellular Component: extracellular space

Molecular Function: protease inhibitor activity

Biological Process: regulation of endopeptidase activity
Precautions
All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
Disclaimer
While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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