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Key Documents

SAB4200146

Sigma-Aldrich

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

~1 mg/mL, affinity isolated antibody

Synonyma:

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

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~50 kDa

species reactivity

monkey, canine, human, rat, bovine, mouse

packaging

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

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

Biochem/physiol Actions

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).

Physical form

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

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

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


Osvědčení o analýze (COA)

Vyhledejte osvědčení Osvědčení o analýze (COA) zadáním čísla šarže/dávky těchto produktů. Čísla šarže a dávky lze nalézt na štítku produktu za slovy „Lot“ nebo „Batch“.

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Dokumenty související s produkty, které jste v minulosti zakoupili, byly za účelem usnadnění shromážděny ve vaší Knihovně dokumentů.

Navštívit knihovnu dokumentů

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)
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)
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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