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SAB4200146

Sigma-Aldrich

Anti-AMSH-LP / STAMBPL1 (C-terminal) antibody produced in rabbit

~1 mg/mL, affinity isolated antibody

Sinônimo(s):

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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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

rabbit

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous solution

peso molecular

antigen ~50 kDa

reatividade de espécies

monkey, canine, human, rat, bovine, mouse

embalagem

antibody small pack of 25 μL

concentração

~1 mg/mL

técnica(s)

indirect immunofluorescence: 5-10 μg/mL using human HeLa cells
western blot: 2.5-5.0 μg/mL using whole extracts of mouse NIH-3T3 cells
western blot: 5-10 μg/mL using using whole extracts of rat NRK cells

nº de adesão UniProt

Q96FJ0

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... STAMBPL1(57559)
mouse ... Stambpl1(76630)

Categorias relacionadas

Descrição geral

AMSH-like protein (AMSH-LP), also known as STAM-binding protein-like 1 (STAMBPL1), is a close homolog of AMSH (Associated Molecule with the SH3 domain of STAM). AMSH and AMSH-LP belong to the JAMM (JAB1/MPN/Mov34 metalloenzyme) domain metalloprotease family of Zn2+-dependent deubiquitinating enzymes (DUBs). AMSH-LP contains a nuclear localization signal (NLS), an Mpr/Pad1/N-terminal (MPN) domain, and a Jab1/MPN domain metalloenzyme (JAMM) motif.

Aplicação

Anti-AMSH-LP / STAMBPL1 (C-terminal) antibody has been used in
  • immunoblotting
  • immunofluorescence
  • western blotting

Ações bioquímicas/fisiológicas

AMSH-like protein (AMSH-LP) and Associated Molecule with the SH3 domain of STAM (AMSH) proteins are involved in the deubiquitination of endosomal proteins and specifically cleave K-63-linked (Lys-63) polyubiquitin chains. AMSH-LP, interacts with clathrin heavy chain and this interaction is essential for its endosomal localization. AMSH-LP, interacts with clathrin heavy chain and this interaction is essential for its endosomal localization. It also positively regulatestransforming growth factor beta (TGF-β) signaling through interaction with inhibitory I-SMADs (inhibitory-Mothers against decapentaplegic).

forma física

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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Visite a Biblioteca de Documentos

Identification of AMSH-LP containing a Jab1/MPN domain metalloenzyme motif
Kikuchi K, et al.
Biochemical and Biophysical Research Communications, 306(3), 637-643 (2003)
In vivo identification of GTPase interactors by mitochondrial relocalization and proximity biotinylation
Gillingham A, et al.
eLife, 8 (2019)
AMSH is an endosome-associated ubiquitin isopeptidase
McCullough J, et al.
The Journal of cell biology, 166(4), 487-492 (2004)
Clathrin anchors deubiquitinating enzymes, AMSH and AMSH-like protein, on early endosomes
Nakamura M, et al.
Genes Cells, 11(6), 593-606 (2006)
Alison K Gillingham et al.
eLife, 8 (2019-07-12)
The GTPases of the Ras superfamily regulate cell growth, membrane traffic and the cytoskeleton, and a wide range of diseases are caused by mutations in particular members. They function as switchable landmarks with the active GTP-bound form recruiting to the

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