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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity purified immunoglobulin
antibody product type
primary antibodies
clone
polyclonal
species reactivity
human
technique(s)
immunohistochemistry: 1:2,000-1:10,000
immunoprecipitation (IP): 2-5 μg/mg
western blot: 1:2,000- 1:10,000
accession no.
NP_006133.1
shipped in
wet ice
storage temp.
2-8°C
target post-translational modification
unmodified
Gene Information
human ... SFN(2810)
General description
Rabbit anti-14-3-3 Sigma or stratifin is mapped to human chromosome 1p36.11. 14-3-3σ protein is expressed as seven isoforms and has molecular weight in the range of 25 to 30 kDa. It is an acidic homodimeric protein and harbors pleckstrin homology (PH) domain. 14-3-3σ is highly expressed in epidermis.
Immunogen
The epitope recognized by PLA0201 maps to a region between residue 198 and 248 of human 14-3-3 sigma using the numbering given in entry NP_006133.1 (GeneID 2810).
Application
Rabbit anti-14-3-3 Sigma Antibody, Affinity Purified has been used in the pull down assay for Rho associated coiled-coil containing protein kinase 1 (ROCK1) proteins and heat shock 70 kDa 4 protein (Hsp74) in HCT116 cancer cells.
Biochem/physiol Actions
Rabbit anti-14-3-3 or stratifin participates in several biological events including apoptosis and cell differentiation. It regulates the transcription matrix metallopeptidases (MMPs) in fibroblasts and may serve as therapeutic potential in wound healing. 14-3-3σ is less expressed and is hyper methylated in breast cancer cells. It plays a key role in linking signalling proteins and in the enhancing of protein kinase C functionality. A mutation in the stratifin gene is implicated in epilation phenotype in mice. It interacts with ubiquitin-specific protease 8 (USP8) and is highly expressed in human lung adenocarcinoma.
Physical form
Tris-citrate/phosphate buffer, pH 7 to 8 containing 0.09% Sodium Azide
Other Notes
14-3-3 sigma was identified as an epithelial cell marker. It is part of the 14-3-3 family of proteins in which seven isoforms have been identified: beta, zeta, gamma, eta, epsilon, tau, and sigma. 14-3-3 proteins function as adaptors that bind with a number of partners to mediate various signaling pathways. 14-3-3 sigma is also called stratifin or HME1 and appears to function as a tumor suppressor whose expression can be downregulated via methylation. Loss of 14-3-3 sigma expression results in a defective G2/M phase checkpoint and appears to contribute to both epithelial and non-epithelial tumorigenesis.
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 Code
12 - Non Combustible Liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Stratifin regulates stabilization of receptor tyrosine kinases via interaction with ubiquitin-specific protease 8 in lung adenocarcinoma
Kim Y, et al.
Oncogene, 37(40), 5387-5387 (2018)
A mutation in stratifin is responsible for the repeated epilation (Er) phenotype in mice
Herron BJ, et al.
Nature Genetics, 37(11), 1210-1210 (2005)
The role of stratifin in fibroblast-keratinocyte interaction
Medina A, et al.
Molecular and Cellular Biochemistry, 305(1-2), 255-264 (2007)
Hsp74/14-3-3σ Complex Mediates Centrosome Amplification by High Glucose, Insulin, and Palmitic Acid.
Yu Cheng Lu et al.
Proteomics, 19(7), e1800197-e1800197 (2019-01-29)
It has been reported recently that type 2 diabetes promotes centrosome amplification via 14-3-3σ/ROCK1 complex. In the present study, 14-3-3σ interacting proteins are characterized and their roles in the centrosome amplification by high glucose, insulin, and palmitic acid are investigated.
Hsp74/14-3-3sigma Complex Mediates Centrosome Amplification by High Glucose, Insulin, and Palmitic Acid
Lu YC, et al.
Proteomics, 1800197-1800197 (2019)
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