Human Alpha amylase / AMY2A Gene ORF cDNA clone expression plasmid,C terminal GFP tag

Catalog Number:HGA359-CG

Gene
Species
Human
NCBI Ref Seq
RefSeq ORF Size
1536bp
Gene Synonym
PA, AMY2, AMY2B, AMY2A
Sequence Description
Identical with the Gene Bank Ref. ID sequence.
Description
Full length Clone DNA of Human amylase, alpha 2A (pancreatic) Gene ORF cDNA clone expression plasmid,C terminal GFP tag
Plasmid
Promoter
Enhanced CMV mammalian cell promoter
Vector
pCMV3-C-GFPSpark
Restriction Site
Protein Tag
GFPSpark
Tag Sequence
GTGAGCAAGGGC……GAGCTGTACAAG
Sequencing Primers
Forward:T7(TAATACGACTCACTATAGGG) Reverse:BGH(TAGAAGGCACAGTCGAGG)
Quality Control
The plasmid is confirmed by full-length sequencing.
GFPSpark Tag Information
GFPSpark is an improved variant of the green fluorescent protein GFP. It possesses bright green fluorescence (excitation/ emission max = 487 / 508 nm) that is visible earlier than fluorescence of other green fluorescent proteins. GFPSpark is mainly intended for applications where fast appearance of bright fluorescence is crucial. It is specially recommended for cell and organelle labeling and tracking the promoter activity.
Screening
Antibiotic in E.coli
Kanamycin
Antibiotic in Mammalian cell
Hygromycin
Application
Stable or Transient mammalian expression
Storage & Shipping
Shipping
Each tube contains lyophilized plasmid.
Storage
The lyophilized plasmid can be stored at ambient temperature for three months.
Background Information
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.
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