Gene ID Number
1ug per 1ul
ALEXA FLUOR® 350
Human, Mouse, Rat
Purified by Protein A.
Alexa Fluor,ALEXA FLUOR 350
Conjugated Primary Antibodies
Anti-CPN2 PAb ALEXA FLUOR 350
Rabbit (Oryctolagus cuniculus)
This is a highly specific antibody against CPN2.
CPN2 Polyclonal Antibody, ALEXA FLUOR 350 Conjugated
Due to limited amount of testing and knowledge, not every possible cross-reactivity is known.
This antibody was obtained by immunization of the host with KLH conjugated synthetic peptide derived from human CPN2
Store this antibody in aqueous buffered solution containing 1% BSA, 50% glycerol and 0.09% sodium azide. Keep refrigerated at 2 to 8 degrees Celcius for up to one year.
CPN 2; CPN2; CPN-2; ACBP; Carboxypeptidase N 83 kDa chain; Carboxypeptidase N large subunit; Carboxypeptidase N regulatory subunit; Carboxypeptidase N subunit 2 [Precursor]; carboxypeptidase N, polypeptide 2; CPN2_HUMAN.
For facs or microscopy Alexa 1 conjugate.Alexa Fluor 350 conjugates can be used in multi-color flow cytometry with FACS's equipped with a second red laser or red diode.If you buy Antibodies supplied by Bioss Primary Conjugated Antibodies. ALEXA FLUOR they should be stored frozen at - 24°C for long term storage and for short term at + 5°C.
CPN2 is a zinc metalloprotease, and cleaves carboxy-terminal arginines and lysines from peptides found in the bloodstream such as complement anaphylatoxins, kinins, and creatine kinase MM (CK-MM). By removing only one amino acid, CPN has the ability to change peptide activity and receptor binding. It is a 280 kDa tetrameric glycoprotein that is synthesized by the liver and secreted into the plasma. It consists of 2 identical 83 kDa regulatory subunits (CPN2) and 2 identical 50 kDa catalytic subunits (CPN1). CPN2, the 83 kDa subunit, binds and stabilizes the catalytic subunit at 37 degrees Celsius and keeps it in circulation. Under some circumstances it may be an allosteric modifier of the catalytic subunit. CPN is a member of a larger family of carboxypeptidases, many of which also cleave arginine and lysine. Because of the highly conserved active sites and the possible redundant functions of carboxypeptidases, it has been difficult to elucidate the role of CPN in disease processes.