GW22560F
Anti-SH3GL1 antibody produced in chicken
affinity isolated antibody, buffered aqueous solution
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
biological source
chicken
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
rat, human, mouse
technique(s)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... SH3GL1(6455)
General description
SH3GL1 (SH3-domain GRB2-like 1), also called EA2 (endophilin A2), was initially recognized as a fusion partner of MLL (mixed-lineage leukaemia) translocation in childhood leukaemia. It is the first member of the EEN/EA SH3 domain (Src homology 3 domain)-containing family of proteins. It is found in the cells of haemopoietic, fibroblast and epithelial lineage, where it resides primarily in the nucleus. In neurons and osteoclasts, its primary localization is in cytoplasm, thus suggesting its shuttles between nucleus and cytoplasm.
Application
Anti-SH3GL1 antibody produced in chicken is suitable for western blotting analysis at a dilution of 1:500, for tissue or cell staining at a dilution of 1:200.
Biochem/physiol Actions
SH3GL1 (SH3-domain GRB2-like 1) or endophilin-A2 is involved in the formation of endocytic vesicles. The protein is a 50- to 60-amino-acid module carried by intracellular proteins involved in the transduction of signals for cell polarization, motility, enzymatic activation, and transcriptional regulation. SH3GL1 is expressed ubiquitously. It is one of the main accessory proteins involved in clathrin-mediated endocytosis and it interacts with other endocytic proteins, such as dynamin, by its SH3 domain. SH3GL1 may be one of the pathogenic genes for idiopathic scoliosis (IS) and may be associated with adolescent idiopathic scoliosis (AIS). It may have some role in the cell cycle. SH3GL1 may be involved in the oncogenic process of gliomas.
Physical form
Solution in phosphate buffered saline containing 0.02% sodium azide.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Jifeng Zhang et al.
Cellular signalling, 24(11), 2043-2050 (2012-07-04)
Endophilin, one of the main accessory proteins involved in clathrin-mediated endocytosis, interacts with other endocytic proteins, such as dynamin, by its SH3 domain. We previously reported that voltage-gated Ca(2+) channels are an integral part of the synaptic vesicle (SV) endocytosis
Ngai Cheung et al.
The Biochemical journal, 383(Pt 1), 27-35 (2004-06-25)
EEN (extra eleven nineteen), also known as EA2 (endophilin A2), a fusion partner of the MLL (mixed-lineage leukaemia) gene in human acute leukaemia, is a member of the endophilin A family, involved in the formation of endocytic vesicles. We present
Tao Yang et al.
Zhonghua wai ke za zhi [Chinese journal of surgery], 48(6), 435-438 (2010-07-16)
To identify whether SH3GL1 gene serves as a disease associated gene of adolescent idiopathic scoliosis (AIS). Positioning candidate cloning: "case-sibling or case-family control design" research scheme based on family constellation was designed. Fifty-six AIS patients (15 male and 41 female
Tomoo Matsutani et al.
Journal of experimental & clinical cancer research : CR, 31, 85-85 (2012-10-12)
Glioma is the most common primary malignant central nervous system tumor in adult, and is usually not curable in spite of various therapeutic approaches. Clarification of the oncogenic process in its early stage is important for the diagnosis and effective
C Giachino et al.
Genomics, 41(3), 427-434 (1997-05-01)
The Src-homology-3 domain (SH3) is an evolutionarily conserved, 50- to 60-amino-acid module carried by intracellular proteins involved in the transduction of signals for cell polarization, motility, enzymatic activation, and transcriptional regulation. The SH3 drives protein-protein interactions through binding to proline-rich
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