Mouse SorCS2 Antibody

R&D Systems | Catalog # AF4237

R&D Systems

Key Product Details

Species Reactivity

Validated:

Mouse

Cited:

Mouse, Transgenic Mouse

Applications

Validated:

Immunohistochemistry, Western Blot

Cited:

Immunohistochemistry, Immunohistochemistry-Frozen, Western Blot, Immunocytochemistry, Immunoprecipitation

Label

Unconjugated

Antibody Source

Polyclonal Sheep IgG
View all SorCS2 Primary Antibodies »

Product Specifications

Immunogen

Mouse myeloma cell line NS0-derived recombinant mouse SorCS2
Ala118-Gly1078
Accession # Q9EPR5

Specificity

Detects mouse SorCS2 in direct ELISAs and Western blots. In direct ELISAs, approximately 10% cross-reactivity with recombinant human (rh) SorCS2 and less than 5% cross-reactivity with rhSorCS1 and recombinant mouse SorCS1 is observed.

Clonality

Polyclonal

Host

Sheep

Isotype

IgG

Scientific Data Images for Mouse SorCS2 Antibody

SorCS2 antibody in Mouse Brain by Immunohistochemistry (IHC-Fr).

SorCS2 in Mouse Brain.

SorCS2 was detected in perfusion fixed frozen sections of mouse brain using Sheep Anti-Mouse SorCS2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4237) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Sheep HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS019) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.
SorCS2 antibody in Mouse Brain by Immunohistochemistry (IHC-Fr).

SorCS2 in Mouse Brain.

SorCS2 was detected in perfusion fixed frozen sections of mouse brain using Sheep Anti-Mouse SorCS2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4237) at 15 µg/mL overnight at 4 °C. Tissue was stained using the NorthernLights™ 557-conjugated Anti-Sheep IgG Secondary Antibody (red; Catalog # NL010) and counterstained with DAPI (blue). View our protocol for Fluorescent IHC Staining of Frozen Tissue Sections.
Detection of SorCS2 by Immunocytochemistry/ Immunofluorescence

Detection of SorCS2 by Immunocytochemistry/ Immunofluorescence

DRD2 activation with sumanirole removes TrkB from the peripheral dendrites in iSPNs. (A) TrkB and SORCS-2 immunoreactivity in purified DRD2-SPNs. Neurons were stimulated with sumanirole for 10 min or bafilomycin for 10 min or 4 h and compared with untreated controls. DRD2 activation with sumanirole reduces surface TrkB expression in iSPNs. Prolonged treatment with bafilomycin leads to an accumulation of SORCS-2- and Lamp-1-positive structures in the soma but not in the dendrites of iSPNs. Scale bar: 10 µm. (B) TrkB immunoreactivity in the peripheral dendrites of DRD2 neurons. Sumanirole treatment leads to a retraction of TrkB from the peripheral dendrites and less association with the cargo receptor SORCS-2. The bafilomycin treatment also decreased TrkB/SORCS-2 association. Scale bar: 2 µm. (C) Quantification of TrkB/SORCS-2 colocalization in peripheral dendrites stimulated with sumanirole (Sum) or bafilomycin (Baf). Data are shown as the mean ± SEM in % of TrkB/SORCS-2 colocalization. n = 3 for every condition. One-way ANOVA with Tukey’s multiple comparisons test. * p < 0.05. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/37887070), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of SorCS2 by Immunocytochemistry/ Immunofluorescence

Detection of SorCS2 by Immunocytochemistry/ Immunofluorescence

DRD2 activation with sumanirole removes TrkB from the peripheral dendrites in iSPNs. (A) TrkB and SORCS-2 immunoreactivity in purified DRD2-SPNs. Neurons were stimulated with sumanirole for 10 min or bafilomycin for 10 min or 4 h and compared with untreated controls. DRD2 activation with sumanirole reduces surface TrkB expression in iSPNs. Prolonged treatment with bafilomycin leads to an accumulation of SORCS-2- and Lamp-1-positive structures in the soma but not in the dendrites of iSPNs. Scale bar: 10 µm. (B) TrkB immunoreactivity in the peripheral dendrites of DRD2 neurons. Sumanirole treatment leads to a retraction of TrkB from the peripheral dendrites and less association with the cargo receptor SORCS-2. The bafilomycin treatment also decreased TrkB/SORCS-2 association. Scale bar: 2 µm. (C) Quantification of TrkB/SORCS-2 colocalization in peripheral dendrites stimulated with sumanirole (Sum) or bafilomycin (Baf). Data are shown as the mean ± SEM in % of TrkB/SORCS-2 colocalization. n = 3 for every condition. One-way ANOVA with Tukey’s multiple comparisons test. * p < 0.05. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/37887070), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of SorCS2 by Immunocytochemistry/ Immunofluorescence

Detection of SorCS2 by Immunocytochemistry/ Immunofluorescence

SorCS2 splice variants display different trafficking.A, SorCS2-immunostained HEK293 cells transfected with SorCS2A and SorCS2C show a more paranuclear staining pattern compared to cells transfected with SorCS2B and SorCS2D for which staining is distributed in vesicular structures throughout the cell. B, surface SorCS2 was labeled with an antibody directed against its extracellular domain on ice. Trafficking was subsequently monitored by incubation at 37 °C, followed by fixation, permeabilization, and staining with a secondary antibody at indicated time points. C, after 30 min, more SorCS2A and SorCS2C accumulate in paranuclear structures positive for the trans-Golgi marker TGN46 compared to SorCS2B, and D. D, quantification of C. The data in the graph is shown as mean ± SD and comparisons between groups conducted using a t test. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/37507021), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of SorCS2 by Western Blot

Detection of SorCS2 by Western Blot

Cellular stress regulates SorCS2 alternative splicing.A, RT-PCR of SORCS2 mRNA from HEK293 cells subjected to cellular stress as indicated. Cellular stress increases the expression of SorCS2 long and decreases the expression of SorCS2 short. B, densitometric quantification of A. C, quantification of SORCS2 mRNA isoforms in HEK293 cells subjected to stress. D and G, RT-PCR of SORCS2 mRNA from HepG2 (D) or SH-SY5Y (G) cells were subjected to hypoosmotic conditions. E and H, densitometric quantification of D and G, respectively. F and I, quantification of SORCS2A, SORCS2B, SORCS2C, and SORCS2D mRNA in HepG2 (F) and SH-SY5Y (I) cells were subjected to hypoosmotic stress. J, six DIV hippocampal cultures were treated with hypoosmotic medium as indicated for 24 h and Sorcs2 mRNA was assessed by RT-PCR. K, densitometric quantification of J. L, representative Western blot showing increased SorCS2 levels after hypoosmotic shock. M and N, normalized expression of SORCS2 transcripts in prefrontal cortex of autism patients (M) and amygdala of schizophrenia patients (N) compared to healthy control groups. Data in B, C, E, F, H, I, and K represents mean ± SD of three experiments. Relative stress-induced mRNA expression of SORCS2 isoforms was compared to the corresponding isoform from nontreated cells using a t test. Variances in SorCS2 mRNA levels in patients suffering from autism or schizophrenia and control groups were compared using an F-test. HEK, human embryonic kidney. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/37507021), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of SorCS2 by Western Blot

Detection of SorCS2 by Western Blot

Cellular stress regulates SorCS2 alternative splicing.A, RT-PCR of SORCS2 mRNA from HEK293 cells subjected to cellular stress as indicated. Cellular stress increases the expression of SorCS2 long and decreases the expression of SorCS2 short. B, densitometric quantification of A. C, quantification of SORCS2 mRNA isoforms in HEK293 cells subjected to stress. D and G, RT-PCR of SORCS2 mRNA from HepG2 (D) or SH-SY5Y (G) cells were subjected to hypoosmotic conditions. E and H, densitometric quantification of D and G, respectively. F and I, quantification of SORCS2A, SORCS2B, SORCS2C, and SORCS2D mRNA in HepG2 (F) and SH-SY5Y (I) cells were subjected to hypoosmotic stress. J, six DIV hippocampal cultures were treated with hypoosmotic medium as indicated for 24 h and Sorcs2 mRNA was assessed by RT-PCR. K, densitometric quantification of J. L, representative Western blot showing increased SorCS2 levels after hypoosmotic shock. M and N, normalized expression of SORCS2 transcripts in prefrontal cortex of autism patients (M) and amygdala of schizophrenia patients (N) compared to healthy control groups. Data in B, C, E, F, H, I, and K represents mean ± SD of three experiments. Relative stress-induced mRNA expression of SORCS2 isoforms was compared to the corresponding isoform from nontreated cells using a t test. Variances in SorCS2 mRNA levels in patients suffering from autism or schizophrenia and control groups were compared using an F-test. HEK, human embryonic kidney. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/37507021), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of SorCS2 by Western Blot

Detection of SorCS2 by Western Blot

Cellular stress regulates SorCS2 alternative splicing.A, RT-PCR of SORCS2 mRNA from HEK293 cells subjected to cellular stress as indicated. Cellular stress increases the expression of SorCS2 long and decreases the expression of SorCS2 short. B, densitometric quantification of A. C, quantification of SORCS2 mRNA isoforms in HEK293 cells subjected to stress. D and G, RT-PCR of SORCS2 mRNA from HepG2 (D) or SH-SY5Y (G) cells were subjected to hypoosmotic conditions. E and H, densitometric quantification of D and G, respectively. F and I, quantification of SORCS2A, SORCS2B, SORCS2C, and SORCS2D mRNA in HepG2 (F) and SH-SY5Y (I) cells were subjected to hypoosmotic stress. J, six DIV hippocampal cultures were treated with hypoosmotic medium as indicated for 24 h and Sorcs2 mRNA was assessed by RT-PCR. K, densitometric quantification of J. L, representative Western blot showing increased SorCS2 levels after hypoosmotic shock. M and N, normalized expression of SORCS2 transcripts in prefrontal cortex of autism patients (M) and amygdala of schizophrenia patients (N) compared to healthy control groups. Data in B, C, E, F, H, I, and K represents mean ± SD of three experiments. Relative stress-induced mRNA expression of SORCS2 isoforms was compared to the corresponding isoform from nontreated cells using a t test. Variances in SorCS2 mRNA levels in patients suffering from autism or schizophrenia and control groups were compared using an F-test. HEK, human embryonic kidney. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/37507021), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of SorCS2 by Western Blot

Detection of SorCS2 by Western Blot

Cellular stress regulates SorCS2 alternative splicing.A, RT-PCR of SORCS2 mRNA from HEK293 cells subjected to cellular stress as indicated. Cellular stress increases the expression of SorCS2 long and decreases the expression of SorCS2 short. B, densitometric quantification of A. C, quantification of SORCS2 mRNA isoforms in HEK293 cells subjected to stress. D and G, RT-PCR of SORCS2 mRNA from HepG2 (D) or SH-SY5Y (G) cells were subjected to hypoosmotic conditions. E and H, densitometric quantification of D and G, respectively. F and I, quantification of SORCS2A, SORCS2B, SORCS2C, and SORCS2D mRNA in HepG2 (F) and SH-SY5Y (I) cells were subjected to hypoosmotic stress. J, six DIV hippocampal cultures were treated with hypoosmotic medium as indicated for 24 h and Sorcs2 mRNA was assessed by RT-PCR. K, densitometric quantification of J. L, representative Western blot showing increased SorCS2 levels after hypoosmotic shock. M and N, normalized expression of SORCS2 transcripts in prefrontal cortex of autism patients (M) and amygdala of schizophrenia patients (N) compared to healthy control groups. Data in B, C, E, F, H, I, and K represents mean ± SD of three experiments. Relative stress-induced mRNA expression of SORCS2 isoforms was compared to the corresponding isoform from nontreated cells using a t test. Variances in SorCS2 mRNA levels in patients suffering from autism or schizophrenia and control groups were compared using an F-test. HEK, human embryonic kidney. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/37507021), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of SorCS2 by Immunocytochemistry/ Immunofluorescence

Detection of SorCS2 by Immunocytochemistry/ Immunofluorescence

Insertion of S1104 in SorCS2 hampers BDNF-induced neuronal branching. SorCS2 KO hippocampal neurons were cotransfected with GFP and indicated SorCS2 constructs and treated with 1 nM BDNF for 72 h. A, representative images of neurons transfected with SorCS2A or SorCS2 tailless in the presence or absence of BDNF. Images have been reconstructed using Imaris software (https://imaris.oxinst.com/). B, quantification of neuronal branching for neurons transfected with SorCS2A, SorCS2B, SorCS2C, or SorCS2D in the presence or absence of BDNF. Data in graphs represent mean ± SD of three or four experiments. Treatment responses in different groups were compared by two-way ANOVA. If the analysis of variance revealed significant differences, a t test was carried out to elucidate the pattern of differences. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/37507021), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of SorCS2 by Western Blot

Detection of SorCS2 by Western Blot

Cellular stress regulates SorCS2 alternative splicing.A, RT-PCR of SORCS2 mRNA from HEK293 cells subjected to cellular stress as indicated. Cellular stress increases the expression of SorCS2 long and decreases the expression of SorCS2 short. B, densitometric quantification of A. C, quantification of SORCS2 mRNA isoforms in HEK293 cells subjected to stress. D and G, RT-PCR of SORCS2 mRNA from HepG2 (D) or SH-SY5Y (G) cells were subjected to hypoosmotic conditions. E and H, densitometric quantification of D and G, respectively. F and I, quantification of SORCS2A, SORCS2B, SORCS2C, and SORCS2D mRNA in HepG2 (F) and SH-SY5Y (I) cells were subjected to hypoosmotic stress. J, six DIV hippocampal cultures were treated with hypoosmotic medium as indicated for 24 h and Sorcs2 mRNA was assessed by RT-PCR. K, densitometric quantification of J. L, representative Western blot showing increased SorCS2 levels after hypoosmotic shock. M and N, normalized expression of SORCS2 transcripts in prefrontal cortex of autism patients (M) and amygdala of schizophrenia patients (N) compared to healthy control groups. Data in B, C, E, F, H, I, and K represents mean ± SD of three experiments. Relative stress-induced mRNA expression of SORCS2 isoforms was compared to the corresponding isoform from nontreated cells using a t test. Variances in SorCS2 mRNA levels in patients suffering from autism or schizophrenia and control groups were compared using an F-test. HEK, human embryonic kidney. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/37507021), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of SorCS2 by Immunocytochemistry/ Immunofluorescence

Detection of SorCS2 by Immunocytochemistry/ Immunofluorescence

Interactions with KLC1 and DYNLT3 regulate SorCS2 isoform anterograde and retrograde trafficking. Trafficking of cell surface SorCS2 variants were followed by antibody uptake experiments. Data represent SorCS2 subcellular distribution after 30 min at 37 °C. A, mutation of the DYNLT3-binding site of SorCS2A reduces its accumulation in TGN46-positive paranuclear compartments. B, mutation of the KLC1-binding site of SorCS2B increases its accumulation in TGN46-positive paranuclear compartments. The data in the graphs are shown as mean ± SD and comparisons between groups conducted using a t test. DYNLT3, dynein light chain Tctex-type 3; KLC, kinesin light chain. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/37507021), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of SorCS2 by Western Blot

Detection of SorCS2 by Western Blot

SorCS2 variants selectively interacts with KLC1 and DYNLT3.A, illustration of yeast two-hybrid screen used for identification of SorCS2D ICD–binding partners. SorCS2D ICD fused to the DNA-binding protein LexA constitutes the bait, which binds upstream of a histidine reporter gene. Protein fragments from an adult human brain library fused to the activation domain (AD) of the Gal4 transcription factor is referred to as the prey. Only a physical interaction between bait and prey allows transcription of the histidine reporter gene and growth in the absence of histidine. Aside from fragments covering KLC1 and DYNLT3, the remaining eight fragments covering five proteins reached a score of 3 or less. B, representative yeast two-hybrid assay showing an interaction between SorCS2B and SorCS2D ICD with KLC1 and between ICD of all four isoforms with DYNLT3. C, SorCS2B and SorCS2D ICD fused to GST pull-down endogenous KLC1 from HEK293 cell lysate. D, DYNLT3-GST pulls down all SorCS2 isoforms from transfected HEK293 cell lysate. E, mapping by yeast two-hybrid shows that deletion of the C-terminal 20 amino acids of SorCS2D ICD compromises interactions with KLC1 and DYNLT3. F, representative yeast two-hybrid assay showing that substitutions with alanine mainly within the acidic cluster of SorCS2D ICD abrogates interactions with KLC1. In contrast, only substitutions outside the acidic cluster abrogates interactions with DYNLT3. DYNLT3, dynein light chain Tctex-type 3; ICD, intracellular domain; KLC, kinesin light chain; PD, pull down. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/37507021), licensed under a CC-BY license. Not internally tested by R&D Systems.

Applications for Mouse SorCS2 Antibody

Application
Recommended Usage

Immunohistochemistry

5-15 µg/mL
Sample: Perfusion fixed frozen sections of mouse brain (cortex)

Western Blot

0.1 µg/mL
Sample: Recombinant Mouse SorCS2 (Catalog # 4237-SR)

Reviewed Applications

Read 5 reviews rated 4.4 using AF4237 in the following applications:

Formulation, Preparation, and Storage

Purification

Antigen Affinity-purified

Reconstitution

Reconstitute at 0.2 mg/mL in sterile PBS. For liquid material, refer to CoA for concentration.

Formulation

Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Shipping

Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: SorCS2

Mouse SorCS2 is a 110‑130 kDa member of the Vps10p (vacuolar protein sorting 10 protein)-D family of sorting receptors. It is synthesized as a 1159 amino acid (aa) preproprecursor that undergoes proteolytic processing to generate a 1042 aa mature type I transmembrane receptor. The extracellular domain shows an imperfect LRR and a Vps10p domain. SorCS2 is plasma membrane expressed and may undergo proteolytic cleavage. Over aa 118-1078, mouse SorCS2 is 88% and 98% aa identical to human and rat SorCs2, respectively.

Long Name

Sortilin-related VPS10 Domain Containing Receptor 2

Alternate Names

KIAA1329VPS10 domain receptor protein, sortilin-related VPS10 domain containing receptor 2, VPS10 domain-containing receptor SorCS2

Entrez Gene IDs

57537 (Human); 81840 (Mouse)

Gene Symbol

SORCS2

UniProt

Q9EPR5

Additional SorCS2 Products

Product Documents for Mouse SorCS2 Antibody

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

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Product Specific Notices for Mouse SorCS2 Antibody

For research use only

Citations for Mouse SorCS2 Antibody

Customer Reviews for Mouse SorCS2 Antibody (5)

4.4 out of 5
5 Customer Ratings
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Showing  1 - 5 的 5 reviews Showing All
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  • Name: Anonymous
    Application: Western Blot
    Sample Tested: Hippocampal lysates from p20 mice
    Species: Mouse
    Verified Customer | Posted 12/17/2014
  • Name: Anonymous
    Application: Western Blot
    Sample Tested: Primary rat Schwann cells
    Species: Rat
    Verified Customer | Posted 12/17/2014
  • Name: Anonymous
    Application: Immunoprecipitation
    Sample Tested: IP of endogenous SorCS2 in mouse tissues as well as SorCS2 knockout mouse
    Species: Mouse
    Verified Customer | Posted 12/17/2014
  • Mouse SorCS2 Antibody
    Name: Anonymous
    Application: Immunocytochemistry
    Sample Tested: Mouse Tissues
    Species: Mouse
    Verified Customer | Posted 12/16/2014
  • Mouse SorCS2 Antibody
    Name: Anonymous
    Application: Western Blot
    Sample Tested: mouse tissue homogenates
    Species: Other
    Verified Customer | Posted 12/16/2014

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Protocols

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