beta Amylase cDNA ORF Clone in Cloning Vector, Human

Cat: HG13575-G
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beta Amylase cDNA ORF Clone in Cloning Vector, Human General Information
Gene
Species
Human
NCBI Ref Seq
RefSeq ORF Size
1536 bp
Sequence Description
Identical with the Gene Bank Ref. ID sequence except for the point mutation 1510 G/C and 1512 A/T resulting in the amino acid Ala substitution by Pro.
Description
Full length Clone DNA of Human amylase, alpha 2B (pancreatic).
Plasmid
Vector
pGEM-T Vector
Sequencing Primers
SP6 and T7 or M13-47 and RV-M
Quality Control
The plasmid is confirmed by full-length sequencing.
Screening
Antibiotic in E.coli
Ampicillin
Storage & Shipping
Shipping
Each tube contains lyophilized plasmid.
Storage
The lyophilized plasmid can be stored at ambient temperature for three months.
beta Amylase cDNA ORF Neucleotide Sequence and Amino Acid Sequence Information

**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**

beta Amylase cDNA ORF Clone in Cloning Vector, Human Alternative Names
AMY2 cDNA ORF Clone, Human;AMY3 cDNA ORF Clone, Human;HXA cDNA ORF Clone, Human
beta Amylase Background Information

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 is the major form of amylase found in humans and other mammals. 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.

Full Name
amylase, alpha 2B (pancreatic)
References
  • Abe A. et al., 2005, FEBS J. 272 (23): 6145-53.
  • Aghajari N. et al., 1998, Protein Sci. 7 (3): 564-72.
  • Ramasubbu N. et al., 1996, Acta Crystallographica Section D Biological Crystallography. 52 (3): 435-46.
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