Recombinant Rat Carboxypeptidase A protein (rFc Tag)

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• Recombinant Rat Carboxypeptidase A protein (rFc Tag) (Eg3276)

Species

Rat

Purity

>90 %, SDS-PAGE

Tag

rFc Tag

Activity

not tested

Cat no : Eg3276

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Validation Data Gallery

• 

  Purity of Recombinant Rat Carboxypeptidase A was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

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Product Information

• Purity: >90 %, SDS-PAGE
• Endotoxin: <0.1 EU/μg protein, LAL method
• Activity:

  Not tested

• Expression: HEK293-derived Rat Carboxypeptidase A protein Asn17-Tyr419 (Accession# P00731) with a rabbit IgG Fc tag at the C-terminus.
• GeneID: 24269
• Accession: P00731
• PredictedSize: 71.7 kDa
• SDS-PAGE: 65-75 kDa, reducing (R) conditions
• Formulation: Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
• Reconstitution: Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
• Storage Conditions:
  It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
• Shipping: The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

Carboxypeptidase A (CPA) is a well-studied enzyme in rats, with significant implications in various biological processes.A novel rat carboxypeptidase, CPA2, was identified from the predicted amino acid sequence of a rat pancreatic cDNA clone. Evolutionary trees built from the amino acid sequences of known pancreatic carboxypeptidases show that CPA2 and carboxypeptidase A1 (CPA1) are products of genes that duplicated before themammalian radiation. Carboxypeptidases have been implicated in various diseases.

References:

1.	Uratani Y, Takiguchi-Hayashi K, et al. (2000) Biochem J. 346 Pt 3(Pt 3):817-26. 
2.	Bodwell JE, Meyer WL. (1981) Biochemistry. 20(10):2767-77.
3.	Lützelschwab C, et al. (1997) J Exp Med. 185(1):13-29.