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CPA2 Protein, Rat, Recombinant (His)

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CPA2 Protein, Rat, Recombinant (His)

Catalog No. TMPY-00332

CPA2 Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 46.5 kDa and the accession number is A6IEG7.

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Pack Size	Price	Availability	Quantity
50 μg	$700	7-10 days

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Biological Description

Biological Information	Testing in progress
Description	CPA2 Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 46.5 kDa and the accession number is A6IEG7.
Species	Rat
Expression System	HEK293 Cells
Tag	C-His
Accession Number	A6IEG7
Synonyms	CPA2,Carboxypeptidase A2
Construction	The Rat Cpa2 (NP_001013101.2) (Met1-Tyr417) was expressed with a polyhistidine tag at the C-terminus.
Protein Purity	> 90 % as determined by SDS-PAGE
Molecular Weight	46.5 kDa (predicted)
Endotoxin	< 1.0 EU/μg of the protein as determined by the LAL method.
Formulation	Lyophilized from a solution filtered through a 0.22 μm filter, containing PBS, pH 7.4. Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization.
Reconstitution	A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
Stability & Storage	It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	In general, Lyophilized powders are shipping with blue ice.
Research Background	Carboxypeptidase A2 ( CPA2 ) is a secreted pancreatic procarboxy -peptidase, and 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.