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SAB4200146

Sigma-Aldrich

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

~1 mg/mL, affinity isolated antibody

Synonyme(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

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~50 kDa

Espèces réactives

monkey, canine, human, rat, bovine, mouse

Conditionnement

antibody small pack of 25 μL

Concentration

~1 mg/mL

Technique(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

Numéro d'accès UniProt

Q96FJ0

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

Description générale

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.

Application

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

Actions biochimiques/physiologiques

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).

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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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