SAB4200145
Anti-AMSH-LP/STAMBPL1 antibody produced in rabbit
~1.0 mg/mL, affinity isolated antibody
别名:
Anti-ALMalpha, Anti-AMSH-FP, Anti-AMSH-like protease, Anti-STAM binding protein-like 1, Anti-associated molecule with the SH3 domain of STAM (AMSH) like protein
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关于此项目
NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IF, WB
Citations:
5
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
~50 kDa
species reactivity
human
packaging
antibody small pack of 25 μL
concentration
~1.0 mg/mL
technique(s)
indirect immunofluorescence: 2-5 μg/mL using human HeLa cells, western blot: 1-2 μg/mL using whole extracts of human PMC2 cells
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... STAMBPL1(57559)
General description
STAM binding protein like 1 (STAMBPL1) or AMSH-LP (AMSH-like protein), is a close homolog of AMSH (Associated Molecule with the SH3 domain of STAM). AMSH and AMSH-LP belong to the Joseph disease protease and JAB1/MPN/Mov34 metalloenzyme (JAMM) domain metalloprotease family of Zn2+-dependent deubiquitinating enzymes (DUBs). STAMBPL1 is mapped to human chromosome 10q23.31.
Application
Anti-AMSH-LP/STAMBPL1 antibody produced in rabbit has been used in immunoblotting and immunofluorescence.
Biochem/physiol Actions
Anti-AMSH-LP/STAMBPL1 recognizes human AMSH-LP/STAMBPL1.
STAM binding protein like 1 (STAMBPL1), along with Associated Molecule with the SRC homology 3 domain (SH3) of STAM (AMSH proteins) mediate the deubiquitination of endosomal proteins and specifically cleave lysine-63-linked polyubiquitin chains. AMSH-LP, like AMSH, interacts with clathrin heavy chain and this interaction is essential for its endosomal localization. However, AMSH-LP, unlike AMSH, fails to bind to the SH3 domain of STAM, suggesting that they are not functionally redundant. AMSH-LP positively regulates transforming growth factor (TGF-β) signaling through interaction with inhibitory I-SMADs.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide
Preparation Note
Store at –20 °C. For continuous use, store at 2–8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.
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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存储类别
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
Cloning of a novel signaling molecule, AMSH-2, that potentiates transforming growth factor beta signaling
Ibarrola N, et al.
BMC Cell Biology, 5(1), 2-2 (2004)
Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains
Sato Y, et al.
Nature, 455(7211), 358-362 (2008)
Clathrin anchors deubiquitinating enzymes, AMSH and AMSH-like protein, on early endosomes
Nakamura M, et al.
Genes Cells, 11(6), 593-606 (2006)
Chinyere Ibeawuchi et al.
International journal of molecular sciences, 16(2), 3856-3869 (2015-02-14)
The multifocal nature of prostate cancer (PCa) creates a challenge to patients' outcome prediction and their clinical management. An approach that scrutinizes every cancer focus is needed in order to generate a comprehensive evaluation of the disease, and by correlating
Xi Chen et al.
Cancer letters, 456, 49-58 (2019-04-21)
The zinc metalloprotease STAM-binding protein-like 1 (STAMBPL1) has been identified as a deubiquitinase by specifically cleaving Lys-63-linked polyubiquitin chains, but its cellular function remains unclear. Here we described the potential role of STAMBPL1 in suppression of the intrinsic apoptosis. We
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