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Monoclonal Antibody Fibril Organization and Biogenesis

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

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

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunoprecipitation, Western Blotting

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin)

Background: Mucins are a family of macromolecules that line and protect the respiratory epithelium from microbes and pollutants in the local environment. Of the family members that are known to date, some are produced in a cell type and tissue-specific manner, suggesting distinct biological roles for members. Some members polymerize after secretion to form gel-like substances that coat the epithelial layer. MUC5AC and MUC5B are members of the family that polymerize in this manner. Others do not polymerize, and others yet, have a transmembrane domain and remain physically attached to the epithelia (1). While it is known that mucins are protective to the respiratory epithelium, it has been reported that changes in expression of mucins are associated with several forms of lung disease such as cystic fibrosis, COPD, asthma, pulmonary fibrosis, and others (2,3,4,1). Multiple epithelial malignancies have been described to show changes in expression, localization, and glycosylation of MUC5AC. This wide association with multiple malignancy types has led to the emergence of MUC5AC as both a prognostic and therapeutic target for cancer (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Monkey, Mouse, Pig, Rat, Zebrafish

Application Methods: Immunoprecipitation, Western Blotting

Background: Integrin-linked kinases (ILKs) couple integrins and growth factors to downstream pathways involved in cell survival, cell cycle control, cell-cell adhesion and cell motility (1). ILK functions as a scaffold bridging the extracellular matrix (ECM) and growth factor receptors to the actin cytoskeleton through interactions with integrin, PINCH (which links ILK to the RTKs via Nck2), CH-ILKBP and affixin (1). ILK phosphorylates Akt at Ser473, GSK-3 on Ser9, myosin light chain 2 (MLC2) on Ser18/Thr19, as well as affixin (2-5). These phosphorylation events are key regulatory steps in modulating the activities of the targets. ILK activity is stimulated by PI3 kinase and negatively regulated by the tumor suppressor PTEN and a PP2C protein phosphatase, ILKAP (1,3,6). It has been suggested that the conserved Ser343 residue in the activation loop plays a key role in the activation of ILK1 (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Cystatin C (cystatin-3, CST3) belongs to the cystatin type 2 superfamily of cysteine peptidase inhibitors (1). The 146 amino acid cystatin C precursor protein contains a 26 residue, amino-terminal secretory signal sequence. The mature 120 amino acid cystatin C protein contains two disulfide bridges (2,3). Cystatin C is secreted in body fluids and is a marker of kidney (4) and cardiovascular (5) dysfunction. Research studies report of changes in cystatin C levels in the cerebral spinal fluid as well as in specific neuronal cell populations in a number of neurodegenerative diseases (6-8). Interestingly, experimental evidence suggests that cystatin C has protective effects against neurodegeneration, such as inhibition of amyloid-β oligomerization and fibril formation (9,10), induction of autophagy (11), induction of neurogenesis (12), and inhibition of cysteine proteases whose activity has been associated with several neurodegenerative diseases (13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGF-β elicits signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-β with high affinity but lacks a cytoplasmic signaling domain (6,7). Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex. The only known direct TGF-β signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8,9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Neurofibromin is a Ras-specific GTPase activating protein (RasGAP), down-regulating Ras signaling (1). Studies have shown, that mutations in NF1 inhibit its activity, resulting in benign tumors such as neurofibromas, which may form along nerves throughout the body resulting in neurofibromatosis type 1 (NF1) (2). NF1 is one of the most common autosomal dominant diseases however it remains unclear how mutation of NF1 may lead to other features of NF1 (3). In addition, NF1 mutations occur in 5-10% of human sporadic malignancies such as glioblastomas, lung adenocarcinomas, melanomas, breast and ovarian cancers, and acute myeloid leukemias. Mutations in NF1 can cause resistance to therapies including chemotherapy and radiation therapy (3).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Type 1 collagen is the most abundant collagen in many human tissues, including bone, skin, and tendons. It is a trimeric complex comprised of two molecules of COL1A1 (alpha-1 type 1 collagen) and one molecule of COL1A2 (alpha-2 type 1 collagen) (1-3). The expression levels of COL1A1 are regulated by multiple mechanisms, including mRNA stability, translation, and posttranslational modification (3-5). Overexpression of COL1A1 has been positively associated with tissue fibrosis disorders, including systemic sclerosis (6), while loss-of-function mutations in the COL1A1 gene are a major causative factor for osteogenesis imperfecta (brittle bone disease) (7). Notably, COL1A1 expression levels have also been associated with tumor development in gastric, lung, thyroid, and breast cancers. Research studies suggest that upregulation of COL1A1 can generate a modified extracellular matrix environment that promotes cancer cell survival, proliferation, metastasis, and invasion (8-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Type 1 collagen is the most abundant collagen in many human tissues, including bone, skin, and tendons. It is a trimeric complex comprised of two molecules of COL1A1 (alpha-1 type 1 collagen) and one molecule of COL1A2 (alpha-2 type 1 collagen) (1-3). The expression levels of COL1A1 are regulated by multiple mechanisms, including mRNA stability, translation, and posttranslational modification (3-5). Overexpression of COL1A1 has been positively associated with tissue fibrosis disorders, including systemic sclerosis (6), while loss-of-function mutations in the COL1A1 gene are a major causative factor for osteogenesis imperfecta (brittle bone disease) (7). Notably, COL1A1 expression levels have also been associated with tumor development in gastric, lung, thyroid, and breast cancers. Research studies suggest that upregulation of COL1A1 can generate a modified extracellular matrix environment that promotes cancer cell survival, proliferation, metastasis, and invasion (8-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: LOX (lysyl oxidase) is a secreted copper-dependent amine oxidase and a member of the lysyl oxidase family (1). It primarily catalyzes the oxidation of lysine (or hydroxylysine) residues in collagen and elastin to form peptidyl aldehyde derivatives (2). These modifications are required for further cross-linking of target proteins to enhance ECM (extracellular matrix) stiffness. LOX plays critical roles in vascular, lung, and skin development, and tissue damage repair (3-5). Upregulation of LOX is associated with various diseases, including cancer progression and tissue fibrosis. Aberrant LOX activity creates a favorable tumor microenvironment to promote tumor metastasis and distal colonization (6-8).