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Glucagon Antibody

Mouse Monoclonal Antibody (Mab)

     
  • 1 - Glucagon Antibody AM1940B
    All lanes : Anti-Glucagon Antibody (C-term) at 1:1000 dilution Lane 1: HepG2 whole cell lysate Lane 2: HT-29 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-mouse IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 21 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession P01275
Other Accession NP_002045.1
Reactivity Human
Host Mouse
Clonality Monoclonal
Isotype IgG1,k
Clone Names 329CT36.10.10
Calculated MW 20909 Da
Additional info
Gene ID 2641
Other Names Glucagon, Glicentin, Glicentin-related polypeptide, GRPP, Oxyntomodulin, OXM, OXY, Glucagon, Glucagon-like peptide 1, GLP-1, Incretin hormone, Glucagon-like peptide 1(7-37), GLP-1(7-37), Glucagon-like peptide 1(7-36), GLP-1(7-36), Glucagon-like peptide 2, GLP-2, GCG
Target/Specificity This Glucagon antibody is generated from mice immunized with a KLH conjugated synthetic peptide between 119-148 amino acids from human Glucagon.
Dilution WB~~1:1000
Format Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsGlucagon Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name GCG
Function Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes. GLP-2 stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability. Glicentin may modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life.
Cellular Location Secreted.
Tissue Location Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract. GLP-1 and GLP-2 are also secreted in selected neurons in the brain
Research Areas

BACKGROUND

The protein encoded by this gene is actually a preproprotein that is cleaved into four distinct mature peptides. One of these, glucagon, is a pancreatic hormone that counteracts the glucose-lowering action of insulin by stimulating glycogenolysis and gluconeogenesis. Glucagon is a ligand for a specific G-protein linked receptor whose signalling pathway controls cell proliferation. Two of the other peptides are secreted from gut endocrine cells and promote nutrient absorption through distinct mechanisms. Finally, the fourth peptide is similar to glicentin, an active enteroglucagon.

REFERENCES

Jablonski, K.A., et al. Diabetes 59(10):2672-2681(2010)
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Hare, K.J. Dan Med Bull 57 (9), B4181 (2010) :
Yamaoka-Tojo, M., et al. Cardiovasc Diabetol 9, 17 (2010) :
Bertenshaw, G.P., et al. J. Biol. Chem. 276(16):13248-13255(2001)

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