Recombinant Human Carboxypeptidase A2/CPA2

Instruction Manual!

Product name:	Recombinant Human Carboxypeptidase A2/CPA2
Source:	Human Cells
Purity:	Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:	Lyophilized from a 0.2 μm filtered solution of 20mM TrisHCl, 150mm NaCl, pH 7.5.
Applications:	Applications:SDS-PAGE; WB; ELISA; IP.
Storage:	Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:	100ug/50ug/200ug/1mg/1g

Source	Human Cells
Description	Recombinant Human Carboxypeptidase A2 is produced by our Mammalian expression system and the target gene encoding Leu17-Tyr417 is expressed with a 6His tag at the C-terminus.
Names	Carboxypeptidase A2, CPA2
Accession #	P48052
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM TrisHCl, 150mm NaCl, pH 7.5.
Shipping	The product is shipped at ambient temperature.
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 μg/ml. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
Purity	Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin	Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Amino Acid Sequence	LETFVGDQVLEIVPSNEEQIKNLLQLEAQEHLQLDFWKSPTTPGETAHVRVPFVNVQAVKVFLGS QGIAYSIMIEDVQVLLDKENEEMLFNRRRERSGNFNFGAYHTLEEISQEMDNLVAEHPGLVSKVN IGSSFENRPMNVLKFSTGGDKPAIWLDAGIHAREWVTQATALWTANKIVSDYGKDPSITSILDAL DIFLLPVTNPDGYVFSQTKNRMWRKTRSKVSGSLCVGVDPNRNWDAGFGGPGASSNPCSDSYHGP SANSEVEVKSIVDFIKSHGKVKAFITLHSYSQLLMFPYGYKCTKLDDFDELSEVAQKAAQSLRSL HGTKYKVGPICSVIYQASGGSIDWSYDYGIKYSFAFELRDTGRYGFLLPARQILPTAEETWLGLK AIMEHVRDHPYVDHHHHHH
Background	Carboxypeptidase A2 (CPA) is a secreted pancreatic procarboxy-peptidase that cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan. CPA2 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. Three different forms of human pancreatic procarboxypeptidase A have been isolated, and the A1 and A2 forms are always secreted as monomeric proteins with different biochemical properties. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E, and is involved in zymogen inhibition.