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Key Documents

SAB3500069

Sigma-Aldrich

Anti-SYPL2 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

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

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About This Item

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

species reactivity

rat, human, mouse

technique(s)

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

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SYPL2(284612)

Related Categories

General description

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.

Immunogen

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

Biochem/physiol Actions

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.

Features and Benefits

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.

Target description

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.

Linkage

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

Physical form

Supplied at approx. 1 mg/mL in phosphate buffered saline containing 0.02% 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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Product No.
Description
Pricing

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Exome sequencing followed by genotyping suggests SYPL2 as a susceptibility gene for morbid obesity.
Jiao H
European Journal of Human Genetics (2015)
Mitsugumin 29 is transcriptionally induced in senile plaque-associated astrocytes.
Satoh K
Brain Research (2012)
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

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