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Monoclonal Antibody Endoplasmic Reticulum

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The ATP2A2 (SERCA2) calcium pump is one of several sarcoplasmic and endoplasmic reticulum Ca2+-ATPases responsible for regulating calcium transport across intracellular membranes (1). Multiple isoforms have been isolated, with ATP2A2a (SERCA2a) found predominantly in the sarcoplasmic reticulum of muscle cells and ATP2A2b (SERCA2b) more ubiquitously expressed in the endoplasmic reticulum of most cell types (2). An isoform containing a truncated carboxy region (ATP2A2c) is expressed in epithelial and hematopoietic cell lines and may be involved in monocyte differentiation (3). Post-translational modification of ATP2A2 (SERCA2), including phosphorylation and tyrosine nitration, modify Ca2+ -ATPase activity and calcium transport (4,5). Mutation in the corresponding ATP2A2 (SERCA2) gene results in Darier disease, a skin disorder characterized by the presence of dark, keratotic papules or rash found on the head and torso (6).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated BiP (C50B12) Rabbit mAb #3177.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: Secretory and transmembrane proteins are synthesized on polysomes and translocated into the endoplasmic reticulum (ER). Inside the ER, these proteins are often modified by disulfide bond formation, amino-linked glycosylation and folding. To help proteins fold properly, the ER contains a pool of molecular chaperones including BiP. BiP was identified as an immunoglobulin heavy chain binding protein in pre-B cells (1,2). It was also found to be induced at the protein level by glucose starvation (3). When protein folding is disturbed inside ER, BiP synthesis is increased. Subsequently, BiP binds to misfolded proteins to prevent them from forming aggregates and assists in proper refolding (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Sarcoplasmic and endoplasmic reticulum Ca2+ ATPases (SERCA) are members of a highly conserved family of Ca2+ pumps (1). SERCA pumps transport Ca2+ from the cytosol to the sarcoplasmic and endoplasmic reticulum lumen against a large concentration gradient (1). ATP2A1 (SERCA1) is a fast-twitch, skeletal muscle sarcoplasmic reticulum Ca2+ ATPase (2). Research studies have shown that mutations in the ATP2A1 gene cause an autosomal recessive muscle disorder known as Brody myopathy, which is characterized by muscle cramping and impaired muscle relaxation associated with exercise (1-3).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Calreticulin (D3E6) XP® Rabbit mAb #12238.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Calcium is a universal signaling molecule involved in many cellular functions such as cell motility, metabolism, protein modification, protein folding, and apoptosis. Calcium is stored in the endoplasmic reticulum (ER), where it is buffered by calcium binding chaperones such as calnexin and calreticulin, and is released via the IP3 Receptor channel (1). Calreticulin also functions as an ER chaperone that ensures proper folding and quality control of newly synthesized glycoproteins. As such, calreticulin presumably does not alter protein folding but regulates proper timing for efficient folding and subunit assembly. Furthermore, calreticulin retains proteins in non-native conformation within the ER and targets them for degradation (2,3).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells and for immunofluorescent analysis in human and mouse cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Calreticulin (D3E6) XP® Rabbit mAb #12238.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Calcium is a universal signaling molecule involved in many cellular functions such as cell motility, metabolism, protein modification, protein folding, and apoptosis. Calcium is stored in the endoplasmic reticulum (ER), where it is buffered by calcium binding chaperones such as calnexin and calreticulin, and is released via the IP3 Receptor channel (1). Calreticulin also functions as an ER chaperone that ensures proper folding and quality control of newly synthesized glycoproteins. As such, calreticulin presumably does not alter protein folding but regulates proper timing for efficient folding and subunit assembly. Furthermore, calreticulin retains proteins in non-native conformation within the ER and targets them for degradation (2,3).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells and immunofluorescent analysis in mouse and human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Calreticulin (D3E6) XP® Rabbit mAb #12238.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Calcium is a universal signaling molecule involved in many cellular functions such as cell motility, metabolism, protein modification, protein folding, and apoptosis. Calcium is stored in the endoplasmic reticulum (ER), where it is buffered by calcium binding chaperones such as calnexin and calreticulin, and is released via the IP3 Receptor channel (1). Calreticulin also functions as an ER chaperone that ensures proper folding and quality control of newly synthesized glycoproteins. As such, calreticulin presumably does not alter protein folding but regulates proper timing for efficient folding and subunit assembly. Furthermore, calreticulin retains proteins in non-native conformation within the ER and targets them for degradation (2,3).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: Secretory and transmembrane proteins are synthesized on polysomes and translocate into the endoplasmic reticulum (ER) where they are often modified by the formation of disulfide bonds, amino-linked glycosylation and folding. To help proteins fold properly, the ER contains a pool of molecular chaperones including calnexin. Calnexin was first identified as being involved in the assembly of murine class I histocompatibility molecules (1,2). Calnexin is a calcium-binding protein embedded in the ER membrane that retains the newly synthesized glycoproteins inside the ER to ensure proper folding and quality control (3-5). The specificity of calnexin for a subset of glycoproteins is defined by a lectin site, which binds an early oligosaccharide intermediate on the folding glycoprotein (5).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Secretory proteins translocate into the endoplasmic reticulum (ER) after their synthesis where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Disulfide isomerase (PDI) has two thioredoxin homology domains and catalyzes the formation and isomerization of these disulfide bonds (2). Other ER resident proteins that possess the thioredoxin homology domains, including endoplasmic reticulum resident protein 44 (ERp44), constitute the PDI family (2). ERp44 is induced upon ER stress and is linked to Ero1-Lα and Ero1-Lβ through mixed disulfide bonds (3). ERp44 was shown to mediate the ER localization of Ero1-Lα (4).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Protein kinase-like endoplasmic reticulum kinase (PERK) is an eIF2α kinase and transmembrane protein resident in the endoplasmic reticulum (ER) membrane that couples ER stress signals to translation inhibition (1-3). ER stress increases the activity of PERK, which then phosphorylates eIF2α to promote reduced translation. Research studies have demonstrated that PERK-deficient mice have defects in pancreatic β cells several weeks after birth, suggesting a role for PERK-mediated translational control in protecting secretory cells from ER stress (4). PERK activation during ER stress correlates with autophosphorylation of its cytoplasmic kinase domain (1-3). Phosphorylation of PERK at Thr980 serves as a marker for its activation status.

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin), Western Blotting

Background: Secretory and transmembrane proteins are synthesized on polysomes and translocated into the endoplasmic reticulum (ER). Inside the ER, these proteins are often modified by disulfide bond formation, amino-linked glycosylation and folding. To help proteins fold properly, the ER contains a pool of molecular chaperones including BiP. BiP was identified as an immunoglobulin heavy chain binding protein in pre-B cells (1,2). It was also found to be induced at the protein level by glucose starvation (3). When protein folding is disturbed inside ER, BiP synthesis is increased. Subsequently, BiP binds to misfolded proteins to prevent them from forming aggregates and assists in proper refolding (4).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Calnexin (C5C9) Rabbit mAb #2679.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Secretory and transmembrane proteins are synthesized on polysomes and translocate into the endoplasmic reticulum (ER) where they are often modified by the formation of disulfide bonds, amino-linked glycosylation and folding. To help proteins fold properly, the ER contains a pool of molecular chaperones including calnexin. Calnexin was first identified as being involved in the assembly of murine class I histocompatibility molecules (1,2). Calnexin is a calcium-binding protein embedded in the ER membrane that retains the newly synthesized glycoproteins inside the ER to ensure proper folding and quality control (3-5). The specificity of calnexin for a subset of glycoproteins is defined by a lectin site, which binds an early oligosaccharide intermediate on the folding glycoprotein (5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The secretory, intra-organellar and transmembrane proteins translocate into the endoplasmic reticulum (ER) after their synthesis. Inside the ER, they are post-translationally modified and properly folded. Disruptions of ER homeostasis leads to the accumulation of unfolded proteins (1). The ER has developed an adaptive mechanism called unfolded protein response (UPR) to counteract compromised protein folding (1). One of the players in UPR, IRE1, was first identified in Saccharomyces cerevisiae as a transmembrane serine/threonine kinase (2-4). This kinase was proposed to be a proximal sensor for UPR that transmits the unfolded protein signal across the ER membrane (3,4). A human homolog of this kinase, IRE1α, was later identified and shown to be ubiquitously expressed in human tissues (5). Upon activation of UPR, IRE1α splices X-box binding protein (XBP1) mRNA by an unconventional mechanism using its endoribonuclease activity (6). This converts XBP1 into a potent transcriptional activator that induces many UPR responsive genes (6). Recently, IRE1α was shown to mediate the rapid degradation of certain mRNAs based on the ER-localization and primary sequences of their encoded proteins, suggesting a novel mechanism in UPR (7).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Presenilin 1 and presenilin 2 are transmembrane proteins belonging to the presenilin family. Mutation of presenilin genes has been linked to early onset of Alzheimer disease, probably due to presenilin's associated γ-secretase activity for amyloid-β protein processing (1,2). Endogenous presenilin mainly exists in a heterodimeric complex formed from the endoproteolytically processed amino-terminal (34 kDa) and carboxy-terminal (~20, 22, 23 kDa) fragments (CTF) (2,3).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Inositol 1,4,5-triphosphate receptor, also known as IP3R or InsP3R, is a member of the intracellular calcium release channel family and is located in the endoplasmic reticulum. IP3R functions as a Ca2+ release channel for intracellular stores of calcium ions. There are three types of IP3 receptors (IP3R1, 2, and 3) that require the second messenger inositol 1,4,5-triphosphate (IP3) for activation (1). Four individual subunits homo- or hetero-oligomerize to form the receptor's functional channel (2). Phosphorylation of IP3R1 at Ser1756 by cyclic AMP-dependent protein kinase A (PKA) regulates the sensitivity of IP3R1 to IP3 and may be a mode of regulation for Ca2+ release (3,4). IP3R1-mediated Ca2+ release appears to have an effect on the induction of long term depression (LTD) in Purkinje cells (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Inositol 1,4,5-triphosphate receptor, also known as IP3R or InsP3R, is a member of the intracellular calcium release channel family and is located in the endoplasmic reticulum. IP3R functions as a Ca2+ release channel for intracellular stores of calcium ions. There are three types of IP3 receptors (IP3R1, 2, and 3) that require the second messenger inositol 1,4,5-triphosphate (IP3) for activation (1). Four individual subunits homo- or hetero-oligomerize to form the receptor's functional channel (2). Phosphorylation of IP3R1 at Ser1756 by cyclic AMP-dependent protein kinase A (PKA) regulates the sensitivity of IP3R1 to IP3 and may be a mode of regulation for Ca2+ release (3,4). IP3R1-mediated Ca2+ release appears to have an effect on the induction of long term depression (LTD) in Purkinje cells (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Sec61 translocon is a channel complex located on the endoplasmic reticulum (ER) membrane to mediate membrane protein insertion into the organelle (1). There are three components in the complex, Sec61A, Sec61B, and Sec61G (2). Sec61A is the main component of the channel on the ER membrane and directly contacts nascent synthesized polypeptide TMD (transmembrane domain) for insertion (3). Sec61G functions in stablizing the channel (3). In addition to TMD insertion, Sec61 translocon has also been shown to be involved in ER calcium leakage (4,5). Both Bip and calmodulin can inhibit this leakage by their interaction with Sec61A (6,7). Sec61B has no obvious function related to target protein ER membrane insertion, but is involved in other vesicle trafficking processes such as EGFR and Her2 trafficking from the cytosol to nucleus (8,9), Gurken trafficking from Golgi to plasma membrane (10), and copper-transporting ATPase membrane distribution (11).

$115
20 µl
$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Bcl-2 (124) Mouse mAb #15071.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Calreticulin (D3E6) XP® Rabbit mAb #12238.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Calcium is a universal signaling molecule involved in many cellular functions such as cell motility, metabolism, protein modification, protein folding, and apoptosis. Calcium is stored in the endoplasmic reticulum (ER), where it is buffered by calcium binding chaperones such as calnexin and calreticulin, and is released via the IP3 Receptor channel (1). Calreticulin also functions as an ER chaperone that ensures proper folding and quality control of newly synthesized glycoproteins. As such, calreticulin presumably does not alter protein folding but regulates proper timing for efficient folding and subunit assembly. Furthermore, calreticulin retains proteins in non-native conformation within the ER and targets them for degradation (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Presenilin 1 and presenilin 2 are transmembrane proteins belonging to the presenilin family. Mutation of presenilin genes has been linked to early onset of Alzheimer disease, probably due to presenilin's associated γ-secretase activity for amyloid-β protein processing (1,2). Endogenous presenilin mainly exists in a heterodimeric complex formed from the endoproteolytically processed amino-terminal (34 kDa) and carboxy-terminal (~20, 22, 23 kDa) fragments (CTF) (2,3).