Datasheet

Biological Description

Specificity	SorLA/SORL1 Antibody [G6C20] detects endogenous levels of total SorLA/SORL1 protein.
Background	SorLA, also known as SORL1 or sortilin-related receptor 1, is a large (~250 kDa) multi-domain type I transmembrane protein belonging to the vacuolar protein sorting 10 protein (Vps10p) domain receptor family. Its extracellular region is composed of a VPS10p domain responsible for ligand binding, a YWTD β-propeller domain, a cluster of 11 complement-type repeat (CR) domains crucial for interacting with ligands such as amyloid precursor protein (APP), and a cassette of fibronectin type-III domains. The cytoplasmic tail contains motifs essential for binding cytosolic adaptor proteins involved in intracellular trafficking. SorLA acts as a sorting receptor that regulates the intracellular trafficking and processing of proteins, cycling between the trans-Golgi network (TGN), endosomes, and the cell surface. While predominantly expressed in neurons, SorLA is also present in other tissues such as the heart and kidney. It plays a critical role in mediating the trafficking and processing of APP, reducing amyloid-beta peptide production by retaining APP in the Golgi and influencing its post-translational modifications, such as O-linked glycosylation, thereby impacting Alzheimer’s disease pathology. SorLA also interacts with lipoprotein receptors like LRP1 and apolipoproteins, linking it to lipoprotein metabolism and cardiovascular disease. Its recycling and endocytosis depend on cytoplasmic tail motifs that engage adaptor proteins such as AP2 and PACS1, enabling efficient retrograde trafficking from endosomes to the Golgi.

Specificity

SorLA/SORL1 Antibody [G6C20] detects endogenous levels of total SorLA/SORL1 protein.

Background

SorLA, also known as SORL1 or sortilin-related receptor 1, is a large (~250 kDa) multi-domain type I transmembrane protein belonging to the vacuolar protein sorting 10 protein (Vps10p) domain receptor family. Its extracellular region is composed of a VPS10p domain responsible for ligand binding, a YWTD β-propeller domain, a cluster of 11 complement-type repeat (CR) domains crucial for interacting with ligands such as amyloid precursor protein (APP), and a cassette of fibronectin type-III domains. The cytoplasmic tail contains motifs essential for binding cytosolic adaptor proteins involved in intracellular trafficking. SorLA acts as a sorting receptor that regulates the intracellular trafficking and processing of proteins, cycling between the trans-Golgi network (TGN), endosomes, and the cell surface. While predominantly expressed in neurons, SorLA is also present in other tissues such as the heart and kidney. It plays a critical role in mediating the trafficking and processing of APP, reducing amyloid-beta peptide production by retaining APP in the Golgi and influencing its post-translational modifications, such as O-linked glycosylation, thereby impacting Alzheimer’s disease pathology. SorLA also interacts with lipoprotein receptors like LRP1 and apolipoproteins, linking it to lipoprotein metabolism and cardiovascular disease. Its recycling and endocytosis depend on cytoplasmic tail motifs that engage adaptor proteins such as AP2 and PACS1, enabling efficient retrograde trafficking from endosomes to the Golgi.

Usage Information

Application

WB, IHC

Dilution

WB	IHC
1:1000 - 1:10000	1:500 - 1:1000

Reactivity

Rat, Human

Source

Rabbit Monoclonal Antibody

MW

248 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/25525276/
https://pubmed.ncbi.nlm.nih.gov/27832290/

SorLA/SORL1 Antibody [G6C20]

Biological Description

Usage Information

References

Application Data