"STAMBPL1" Related Products

Recombinant Human STAMBPL1, GST-tagged

Cat.No.: STAMBPL1-172H
Product Overview: Recombinant human STAMBPL1 (amino acid residues 264-436), fused with N-terminal GST, was expressed in E.coli.
Description: There are two main classes of DUB; cysteine proteases and metalloproteases. AMSH-Like Protein (AMSH-LP) is a member of the JAB1/MPN/Mov34 metalloenzyme (JAMM) family and cloning of the human gene was first described by Nagase et al. (2000). AMSH and AMSH-LP share 54% identity and 75% sequence similarity in their JAMM domain. It is known that both proteins act as regulators of free ubiquitin in the cell, bind clathrin, contain a putative nuclear localization signal and an MIT domain.
Source: E. coli
Species: Human
Tag: GST
Form: 50 mM HEPES pH 7.5, 150 mM sodium chloride, 2 mM dithiothreitol, 10% glycerol
Bio-activity: Deubiquitylase Enzyme Assay: The activity of GST-AMSH-LP was validated by determining the increase in fluorescence measured as a result of the enzyme catalysed cleavage of the fluorogenic substrate Ubiquitin-Rhodamine110-Glycine generating Ubiquitin and Rhodamine110-Glycine. Incubation of the substrate in the presence or absence of GST-AMSH-LP was compared confirming the deubiquitylating activity of GST-AMSH-LP.
Molecular Mass: ~47 kDa
Purity: >92% by SDS-PAGE
Storage: 12 months at -70°C. Avoid multiple freeze/thaw cycles.
Concentration: 0.5 mg/ml
Gene Name: STAMBPL1 STAM binding protein-like 1 [ Homo sapiens ]
Official Symbol: STAMBPL1
Synonyms: STAMBPL1; STAM binding protein-like 1; AMSH-like protease; ALMalpha; AMSH FP; AMSH LP; associated molecule with the SH3 domain of STAM (AMSH) Family Protein; associated molecule with the SH3 domain of STAM (AMSH) like protein; bA399O19.2; FLJ31524; KIAA1373; associated molecule with the SH3 domain of STAM (AMSH) - Family Protein; AMSH-FP; AMSH-LP;
Gene ID: 57559
mRNA Refseq: NM_020799
Protein Refseq: NP_065850
MIM: 612352
UniProt ID: Q96FJ0
Chromosome Location: 10q23.32
Pathway: TGF-beta Receptor Signaling Pathway, organism-specific biosystem;
Function: metal ion binding; metallopeptidase activity; peptidase activity; protein binding;

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