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T1075

Sigma-Aldrich

Anti-Tal (CS-15) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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Synonym(s):
Anti-Tsg101-associated ligase
MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 84 kDa

species reactivity

rat, canine, human, mouse

technique(s)

immunoprecipitation (IP): 5-10 μg using mouse brain S1 cytosolic fraction
microarray: suitable
western blot: 0.1-0.2 μg/mL using whole extract of human epitheloid carcinoma HeLa cell line and also canine kidney MDCK cell line
western blot: 0.2-0.4 μg/mL using whole extract of rat brain S1 cytosolic fraction

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... LRSAM1(90678)
mouse ... Lrsam1(227738)

General description

Tsg101-associated ligase (TAL), contains an N-terminal leucine-rich repeat (LRR), followed by an ezrin-radixin-moesin (ERM) domain, a coiled-coil (CC) region, a sterile alpha motif (SAM) domain and a C-terminal C3HC4-type RING finger domain. Also called leucine-rich repeat and sterile alpha motif-containing protein 1 (LRSAM1), TAL is an E3 ubiquitin ligase. TAL gene is mapped to human chromosome 9.

Specificity

Anti-Tal (CS-15) recognizes human, dog, rat, and mouse Tal (84 kDa, may appear as doublet).

Immunogen

synthetic peptide encoding amino acids 709-723 located near the C-terminus of human Tal, conjugated to KLH. This sequence is highly conserved in mouse and rat Tal (two amino acids substitution).

Application

Anti-Tal (CS-15) antibody produced in rabbit may be used in immunoblotting and immunoprecipitation.

Biochem/physiol Actions

Tsg101-associated ligase (TAL) plays a key role in cell signaling, cell adhesion and regulates cargo sorting. Reduced expression of Tsg101 shunts active epidermal growth factor receptor (EGFRs) from the normal degradative pathway to a recycling route. Tal, which interacts with Tsg101 associates with and ubiquitylates Tsg101 in a manner that regulates receptor trafficking and budding of viral particles. Tal binds to Tsg101 in a bimodal mode, through an interaction of its CC domain with the steadiness box (SB) of Tsg101, and also via binding of the UEV domain of Tsg101 with two PTAP motifs just upstream of the C-terminal RING domain. Tal interaction with Tsg101 promotes multiple monoubiquitination of Tsg101, rather than polyubiquitination, which leads to the release of Tsg101 from membrane complexes and its inactivation. Mutations in the TAL gene is implicated in Charcot-Marie-Tooth (CMT) syndrome.

Physical form

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

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. Storage in frost-free freezers is also 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, 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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The self-association and activity regulation of LRSAM1 E3 ligase
Bian W, et al.
Biochemical and biophysical research communications, 485(1), 95-101 (2017)
Familial 9q33q34 microduplication in siblings with developmental disorders and macrocephaly
Shimojima K, et al.
European Journal of Medical Genetics, 60(12), 650-654 (2017)
LRSAM1 E3 ubiquitin ligase: molecular neurobiological perspectives linked with brain diseases
Mishra R, et al.
Cellular and Molecular Life Sciences, 76(11), 2093-2110 (2019)
Marissa Mock et al.
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Changes in the level of cellular proteins in cells inoculated with equine influenza virus H7N7 and H3N8 were studied with microarray technique. H3N8 induced pro-apoptotic proteins while H7N7 induced both pro- as well as anti-apoptotic factors. The higher level of

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