Anti-Alpha Amylase 1/AMY1A Antibody Picoband® Fluoro488 Conjugated
Product Specifications
Background
Amylase is an enzyme that catalyses the breakdown of starch into sugars. Amylase is present in human saliva, where it begins the chemical process of digestion. By in situ hybridization combined with high resolution cytogenetics, the amylase gene is mapped to 1p21.Amylase enzymes find use in bread making and to break down complex sugars such as starch (found in flour) into simple sugars. Yeast then feeds on these simple sugars and converts it into the waste products of alcohol and CO2.
Synonyms
Alpha-amylase 1;3.2.1.1;1,4-alpha-D-glucan glucanohydrolase 1; Salivary alpha-amylase; AMY1A; AMY1; AMY1B; AMY1; AMY1C; AMY1
Gene Name
AMY1A
Gene ID
276/277/278
UniProt
P04745
Host
Rabbit
Reactivity
Human, Mouse, Rat
Cross Reactivity
No cross-reactivity with other proteins
Immunogen
A synthetic peptide corresponding to a sequence at the N-terminus of human Alpha Amylase 1, different from the related rat and mouse sequences by one amino acid.
Clonality
Polyclonal
Tissue Specificity
Expressed in vascular smooth muscle cells.
Applications
Flow Cytometry
Field of Research
Alzheimer's Disease, Cell Biology, Chromatin Modifying Enzymes, Epigenetics and Nuclear Signaling, Neurodegenerative Disease, Neurology Process, Neuroscience, Proteasome / Ubiquitin, Proteolysis/Ubiquitin
Purification
Immunogen affinity purified.
Form
Liquid
Function
Ubiquitin: Exists either covalently attached to another protein, or free (unanchored) . When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains) . Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. .
References & Citations
1. Dracopoli, N. C., Meisler, M. H.Mapping the human amylase gene cluster on the proximal short arm of chromosome 1 using a highly informative (CA) n repeat.Genomics 7: 97-102, 1990. 2. Gumucio, D. L., Wiebauer, K., Caldwell, R. M., Samuelson, L. C., Meisler, M. H.Concerted evolution of human amylase genes.Molec. Cell. Biol. 8: 1197-1205, 1988. 3. Kamaryt, J., Laxova, R.Amylase heterogeneity: some genetic and clinical aspects.Humangenetik 1: 579-586, 1965.
Storage Conditions
At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.
Calculated Molecular Weight
57768 MW
Specificity
No cross reactivity with other proteins.
Applications Notes
6
Gene Name Synonym
Alpha-amylase 1
Subcellular Location
Secreted.
Sequence Similarities
Belongs to the glycosyl hydrolase 13 family.
Protein Name
Alpha-amylase 1
Isotype
Rabbit IgG
Contents
Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.
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