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SAB3500069

Sigma-Aldrich

Anti-SYPL2 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-MG29, Anti-Mitsugumin 29, Anti-Synaptophysin-like protein 2

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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

Espèces réactives

rat, human, mouse

Technique(s)

immunofluorescence: suitable
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... SYPL2(284612)

Catégories apparentées

Description générale

Synaptophysin-like 2 (SYPL2) is part of the synaptophysin family and is localized to synaptic vesicles. It is expressed in the heart, brain and kidneys. The gene encoding this protein is localized on human chromosome 1.

Immunogène

SYPL2 antibody was raised against a 15 amino acid peptide near the carboxy terminus of human SYPL.

Actions biochimiques/physiologiques

Synaptophysin-like 2 (SYPL2) may be a Ca2+-dependent transporter involved in exocytosis. It has been shown to be expressed in activated astrocytes which are linked to senile plaques in individuals with Alzheimer′s disease. Thus, it has been speculated as a protein leading to enhanced neurodegeneration. SYPL2 has been linked to morbid obesity.

Caractéristiques et avantages

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Description de la cible

SYPL2, also known as Mitsugumin 29, was initially identified as a transmembrane protein from the triad junction in skeletal muscle that had significant homology with members of the synaptophysin family. SYPL2 is thought to participate in the excitation-contraction coupling process of skeletal muscle as SYPL2-null mice showed reduced muscle contractile force and altered triad junction structure and increased susceptibility to fatigue of the skeletal muscle. SYPL2 plays a critical role in muscle Ca2+ signaling by regulating the process of store-operated Ca2+ entry and interacts with ryanodine receptor (RyR), thereby influencing intracellular Ca2+ homeostasis through changes in the RyR/Ca2+ release function. Co-expression of SYPL2 and RyR in cultured cells leads to apoptotic cell death resulting from the depletion of Ca2+ from the intracellular stores. At least two isoforms of SYPL2 are known to exist. SYPL2 antibody will not cross-react with SYPL1.

Liaison

The action of this antibody can be blocked using blocking peptide SBP3500069.

Forme physique

Supplied at approx. 1 mg/mL in phosphate buffered saline containing 0.02% 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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Produit(s) apparenté(s)

Réf. du produit
Description
Tarif

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Exome sequencing followed by genotyping suggests SYPL2 as a susceptibility gene for morbid obesity.
Jiao H
European Journal of Human Genetics (2015)
Elena Conte et al.
Frontiers in pharmacology, 15, 1393746-1393746 (2024-07-04)
Introduction: During aging, sarcopenia and decline in physiological processes lead to partial loss of muscle strength, atrophy, and increased fatigability. Muscle changes may be related to a reduced intake of essential amino acids playing a role in proteostasis. We have
Mitsugumin 29 is transcriptionally induced in senile plaque-associated astrocytes.
Satoh K
Brain Research (2012)

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