"AbFrontier"

Supplier: AbFrontier

The members of the Src-family kinases are Src, Lyn, Fyn, Yes, Hck, Lck, Fgr, Blk, and Yrk. Each of these have a common structure consisting of an unique domain at the N-terminal, followed by SH3, SH2 and tyrosine kinase domains.
In immume cells, the Src-family kinases play roles as critical regulators of a large number of intracellular signaling pathways, including integrin signaling pathway. Integrins are major cellular receptor that mediate cell to cell and cell to substratum interactions.
The intracellular protein kinase Lyn participates both positively and negatively in B cell, mast cell, platelet and myeloid cell signaling. Lyn is the predominantly expressed Src-family kinase in B cells and its positive role is done through phosphorylation of the Igα and Igβ subunits of B cell receptor. Genetic deletion of Lyn results in autoimmunity, renal disease and premature mortality in mice, and generation of hyperactive Lyn results in the same phenotype, revealing the importance of the balance of Lyn signaling.

Supplier: AbFrontier

The complement system is a part of the larger immune system and three biochemical pathways are present: the classical complement pathway, the alternative pathway, and the mannose-binding lectin pathway.
Human complement factor C8 is one of five components (C5b, C6, C7, C8, and C9) that interact to form the cytolytic membrane attack complex (MAC) which is the cytolytic end product of the complement cascade. MAC is typically formed on the surface of intruding pathogenic bacterial as a result of the activation of the complement system, and it is one of the ultimate weapons of the immune system.
C8 is composed of an α (64 kDa), β (64 kDa), and γ (22 kDa) subunit. Within C8, the subunits are arranged as a disulfide-linked C8 α-γ heterodimer that is noncovalently associated with C8 β. During MAC formation, C8 α mediates binding and self-polymerization of C9 to form a pore-like structure on the membrane of target cells.

Supplier: AbFrontier

Protein phosphatase-1(PP1) is one of the major Ser/Thr protein phosphatases and is ubiquitous in eukaryotic cells. PP1 is localized to its site of action by interacting with targeting or regulatory proteins, a majority of which contains a primary docking site referred to as the RVXF/W motif.
The catalytic subunit of PP1 exists as three isoforms, PP1a, PP1b, and PP1r. The PP1 catalytic subunits are small proteins of 37kDa, which are highly conserved, with their main differences falling in the C-term. The PP1 catalytic subunit exists in the cell in complex with a large number of targeting/regulatory subunits, thereby generating different enzyme forms that allow it to perform a diverse number of cellular functions.

Supplier: AbFrontier

Chromogranin A (CGA) was identified as a major soluble protein in adrenal medullary chromaffin granules. CHGA derived peptides are also known as Catestatin, Vasostatin-I,-II, Prochromacin, Pancreastatin and Parastatin.
CGA and its processed products are involved in the biogenesis of densecore secretory granules and have a role in immunity against microbes, and function as potential markers for several types of tumors. They have also been implicated in neurodegenerative disorders and cardiovascular diseases such as a hypertension. CGA accumulates in the senile and preamyloid plaques of Alzheimer’s disease, in Lewy bodies of Parkinson’s disease, and in the swollen neurons of Pick’s disease.

Supplier: AbFrontier

IκB kinase β (IKKβ) is a component of a multiprotein kinase complex that regulates the activity of the transcription factor NF-κB. Activation of the IKK complex via upstream stimuli leads to phosphorylation and degradation of NF-κB bound IκB (Inhibitor of κB). Subsequently, free NF-κB dimers enter the nucleus and regulate the transcription of a variety of target genes involved in cell proliferation and differentiation, apoptosis, and inflammation, etc. The IKK complex consists of 2 highly homologous kinase subunits, IKKα and IKKβ, and a nonenzymatic regulatory component, IKKγ/NEMO. The relative contributions of IKKα and IKKβ to the signaling complex vary according to the requirements of the cell. IKKβ plays a predominant role in immune responses, while IKKα alone appears to be sufficient for at least some developmental systems. Recently, IKK/NF-κB signaling pathway was studied as therapeutic targets in cancer.

Supplier: AbFrontier

The complement system is a crucial component of the innate immunity against microbial infection. Complement factor H, a 155 kDa plasma glycoprotein, is an essential regulatory protein that plays a critical role in the homeostasis of the complement system in plasma and in the protection of bystander host cells and tissues from damage by complement activation. Factor H binds to C3b, accelerates the decay of the alternative pathway C3-convertase and acts as a cofactor for the factor I-mediated proteolytic inactivation of C3b. In addition, factor H has multiple physiological activities 1) acts as an extracellular matrix component, 2) binds to cellular receptors of the integrin type, and 3) interacts with a wide selection of ligands, such as the C-reactive protein, thrombospondin, bone sialoprotein, osteopontin, and heparin. Complement factor H has revealed an association with two different renal diseases, glomerulonephritis and atypical hemolytic uremic syndrome (aHUS).

Supplier: AbFrontier

Enolase (2-phosphogly-cerate hydrolyase or phosphopyruvate hydrates) is a glycolytic enzyme that catalyzes the dehydration and conversion of 2-phosphoglycerate to phospho-enolpyruvate. It comprises three distint subunits, α, β and γ. The γγ and αγ dimeric forms of enolase, referred to as neuron-specific enolase(NSE), are localized mainly in neurons and neuroectodermal tissue. NSE has a high stability in biological fluids and can easily diffuse to the extracellular medium and cerebrospinal fluid(CSF) when neuronal membranes are injured. NSE is used clinically as a sensitive and useful marker of neuronal damage in several neurological disorders including stroke, hypoxic brain damage, status epilepticus, Creutzfeldt-Jakob disease, and herpetic encephalitis.

Supplier: AbFrontier

Bcl-2 (B-cell lymphoma 2) family govern mitochondrial outer membrane permeabilization (MOMP) and can be either pro-apoptotic (Bax, BAD, Bak, Bid and Bok) or anti-apoptotic (Bcl-2, Bcl-xL, and Bcl-w). Mitochondrial membrane permeabilization and subsequent release of apoptotic factors are key mechanisms during this process.
The members of the Bcl-2 family share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4).
Bid consists of only one Bcl-2 homology domain, BH3. Bid cleavage to tBid (truncated Bid) activates apoptotic pathway at the mitochondrial level. Cleavage of cytosolic Bid and subsequent mitochondrial translocation have been detected in neuronal cell death related to acute or chronic neurodegeneration. Pharmacological inhibition of Bid can be a promising therapeutic strategy in neurological diseases where programmed cell death is prominent.
After Bid activation and mitochondrial translocation, the most prominent downstream mechanisms of Bid-dependent neuronal apoptosis involve disruption of mitochondrial membrane integrity and intracellular calcium homoeostasis and the release of pro-apoptotic mitochondrial factors such as cytochrome c.

Supplier: AbFrontier

Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis.
Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx VI belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 – 30 kilodalton in molecular size and vary in subcellular localization: Prx I, II, and VI in cytosol, Prx III in mitochondria, Prx IV in ER and secretion, Prx V showing complicated distribution including peroxisome, mitochondria and cytosol.

Supplier: AbFrontier

Plasminogen, a 92kDa glycoprotein, is produced by the liver and is present in plasma and extracellular fluids. Plasminogen is the inactive precursor of plasmin, a potent serine protease involved in the dissolution of fibrin blood clots. Plasminogen can be converted into the active plasmin by plasminogen activators urokinase (uPA), tissue plasminogen activator (tPA), factor XII-dependent components. The plasmin system has been implicated in a variety of physiological and pathological processes such as fibrinolysis, tissue remodeling, cell migration, inflammation, and tumor invasion and metastasis. Hereditary defects of plasminogen is a predisposing risk factor for thromboembolic disease.

Supplier: AbFrontier

Anti-DUSP12 Mouse Monoclonal Antibody [clone: PK15-AF28F3]

Supplier: AbFrontier

Cathepsin D(CatD) is a ubiquitously expressed lysosomal aspartyl protease involved in the normal degradation of proteins apoptosis and autophagy. Human CatD is synthesized on the endoplasmic reticulum as a pre-pro-enzyme. Preprocathepsin D(412aa) is cleaved and glycosylated
to form an inactive procathepsin D (392aa) and then further cleaved to generate an active intermediate (348aa) single-chain molecule. The active intermediate is further processed into mature two chain form of cathepsin D, this processing step is carried out by cathepsin B or L. The two-chain form consists of an amino terminal light chain and a carboxyl-terminal heavy chain. Additionally, several more amino acids are removed from the carboxyl terminus of the heavy chain.
Procathepsin D (pCD), secreted from cancer cells, acts as a mitogen on both cancer and stromal cells and stimulates their proinvasive and pro-metastatic properties.

Supplier: AbFrontier

Syk, Spleen tyrosine kinase, is expressed in a wide range of hematopoietic and non-hematopoietic cells and plays a key role in adaptive immune system, which is the immunoreceptor (B cell receptor and Fc-receptors) signaling pathways including Fcγ receptor-mediated phagocytosis. In hematopoietic cells such as B and T lymphocytes, natural killer cells, mast cells, macrophages and platelets, Syk is involved in the proximal signaling downstream of activated immunoreceptors (e.g. BCR, TCR, Fc receptors) containing immunoreceptor tyrosine-based activation motifs (ITAMs) to which it binds using its tandem SH2 domains. Activated and autophosphorylated Syk then phosphorylates its specific substrates including other enzymes and adaptor proteins, orchestrating a complex series of cellular responses such as cell proliferation, differentiation, survival and phagocytosis.

Supplier: AbFrontier

Lactoferrin(Lf), one of transferrin family, is found in external fluids, including milk and mucosal secretions, and prominent components of the secondary granules of neutrophils. Lf consists of a single polypeptide chain (approximately 80 kDa) folded into two structurally homologous lobes, each of which can reversibly bind one ferric ion (Fe3+). Lf plays a central role in iron metabolism and host defense system against microbial infection.

Supplier: AbFrontier

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a catalytic enzyme commonly known to be involved in glycolysis. The enzyme exists as a tetramer of identical 37 kDa subunits. GAPDH catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Apart from playing a key role in glycolysis, this ubiquitously expressed enzyme also displays other activities unrelated to its  glycolytic function. GAPDH is reported to be involved in the processes of DNA replication (1), DNA repair (2), nuclear RNA export (3-4), membrane fusion (5) and microtubule bundling. Other studies also provide evidence of GAPDH playing an essential part of the program of gene expression observed in apoptosis and as part of the cellular phenotype of age-related neurodegenerative diseases (6-7).

Supplier: AbFrontier

Cyclin-dependent kinase-5 (CDK5) is a member of the cyclin-dependent kinase family of serine/threonine kinases. Its mRNA and protein are expressed in kidney, testes, and ovary. And Its activity is detected almost exclusively in brain extracts.
Similar to other Cdks, monomeric Cdk5 displays no enzymatic activity, but Cdk5 is not activated by cyclins. Instead, Cdk5 activity requires association with one of two brain-specific regulatory subunits called p35 and p39. The two activators regulate the spatial and temporal expression of active Cdk5 to restrict its activity primarily to post-mitotic neurons.