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About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IF, WB
Citations:
1
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
~150 kDa
species reactivity
human
concentration
1 mg/mL
technique(s)
indirect immunofluorescence: 1:100-1:200, western blot: 1:500-1:1000
isotype
IgG
immunogen sequence
(K-E-G-E-G)
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... FAM129A(116496)
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General description
Regulates phosphorylation of a number of proteins involved in translation regulation including EIF2A, EIF4EBP1 and RPS6KB1. May be involved in the endoplasmic reticulum stress response.
Immunogen
peptide Corresponding to the 908-920 amino-acid sequence from human niban protein , according to the protein FAM129A.
Features and Benefits
Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.
Physical form
Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Soma Samanta et al.
Cancer research, 81(7), 1883-1895 (2021-02-04)
GRP78 (glucose-regulated protein, 78 kDa) is a key regulator of endoplasmic reticulum (ER) stress signaling. Cancer cells are highly proliferative and have high demand for protein synthesis and folding, which results in significant stress on the ER. To respond to
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