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Human AMY2A Gene cDNA Clone (full-length ORF Clone)

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AMY2AcDNA Clone Product Information
Gene Bank Ref.ID:BC007060
cDNA Size:1536
cDNA Description:ORF Clone of Homo sapiens amylase, alpha 2A (pancreatic) DNA.
Gene Synonym:PA, AMY2, AMY2B, AMY2A
Species:Human
Vector:pGEM-T Vector
Restriction Site:
Tag Sequence:
Sequence Description:Identical with the Gene Bank Ref. ID sequence.
Shipping Carrier:Each tube contains approximately 10 μg of lyophilized plasmid.
Storage:The lyophilized plasmid can be stored at ambient temperature for three months.
pGEM-T Vector Information

The pGEM-T is 3kb in length, and contains the amplicin resistance gene, conferring selection of the plasmid in E. coli, and the ori site which is the bacterial origin of replication. The plasmid has multiple cloning sites as shown below. The coding sequence was inserted by TA cloning. Many E. coli strains are suitable for the propagation of this vector including JM109, DH5α and TOP10.

pGEM-T Simple Usage Suggestion:

The coding sequence can be easily obtained by digesting the vector with proper restriction enzyme(s). The coding sequence can also be amplified by PCR with M13 primers, or primer pair SP6 and T7.

Vector Sequence Download
Human AMY2A Gene cDNA Clone (full-length ORF Clone) on other vectors
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Background

Alpha-amylase is the major form of amylase found in humans and other mammals. Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. Alpha-amylase hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. Amylases is widely expressed and is most prominent in pancreatic juice and saliva, each of which has its own isoform of human α-amylase. They behave differently on isoelectric focusing, and can also be separated in testing by using specific monoclonal antibodies.

References
  • Abe A, et al. (2005) Complexes of Thermoactinomyces vulgaris R-47 Alpha-amylase / AMY2A 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with alpha-(1,6) glycosidic linkages. FEBS J. 272(23):6145-53.
  • Aghajari, N, et al. (1998) Crystal structures of the psychrophilic Alpha-amylase / AMY2A from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Protein Sci. 7(3): 564-72.
  • Ramasubbu, N, et al. (1996) Structure of Human Salivary -Amylase at 1.6 Resolution: Implications for its Role in the Oral Cavity. Acta Crystallographica Section D Biological Crystallography. 52(3):435-46.
  • Catalog:HG13277-G
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