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Image Unavailable-76100-512

Anti-Calpain 2 Rabbit Polyclonal Antibody (Alexa Fluor® 750)

Catalog Number: (76100-512)
Supplier: Bioss
Description: Calpain, and m calpain, also known as Calpain 2, are intracellular, calcium dependent cysteine proteases. Mu calpain has a micromolar sensitivity (thus the mu) as compared to the millimolar calcium sensitivity of m calpain. Both Calpains 1 and 2 are composed of an 80 kD subunit and a 30 kD subunit. Whereas the 30 kDa subunit is shared by both enzymes, the larger catalytic subunits are different and exhibit the distinct Ca++ requirements that are suggested by their names. The calpains have papain like activity, thus the pain nomenclature. Both Calpain 1 and Calpain 2 are ubiquitously expressed, and are countered by the endogenous calpain inhibitor, calpastatin. Other calpain family members (calpain 94, ncl2, ncl3, etc) have more limited tissue distribution, and perhaps different functions. The calpain family members consist of a common small subunit (Calpain 4), and a large variable subunit. It is not clear that all calpains contain a small subunit. Domains in the large subunit include the amino terminal domain I, the proteinase domain II, domain III, and the EF hand domain IV. The calpains appear to serve multiple physiological roles, and ideas concerning the functions of these enzymes are in a state of rapid flux.
Image Unavailable-76120-926

Anti-CLNS1A Rabbit Polyclonal Antibody (Alexa Fluor® 680)

Catalog Number: (76120-926)
Supplier: Bioss
Description: The formation of the spliceosome includes the assembly of Sm proteins in an ordered manner onto snRNAs. This process is mediated by the survival of motor neuron (SMN) protein, and is enhanced by modification of specific arginine residues in the Sm proteins to symmetrical dimethylarginines (sDMAs). sDMA modification of Sm proteins is catalyzed by the methylosome, a complex comprised of the type II methyltransferase PRMT5 (also designated Jak-binding protein 1, JBP1), pICln, and two novel factors. PRMT5 binds the Sm proteins via their arginine- and glycine-rich (RG) domains, while pICln binds the Sm domains. pICln also acts as an inhibitor of SnRNP assembly by preventing specific interactions between Sm proteins required for the formation of the Sm core. pICln is a highly conserved, ubiquitously expressed protein that localizes primarily to the cytoplasm, and may play a role as a swelling-activated anion channel or a channel regulator in addition to its function in the methylosome. The gene encoding human pICln maps to chromosome 11q14.1.
Image Unavailable-CA80017-326

Anti-MMP-1 (Ab-1) Mouse Monoclonal Antibody [clone: 41-1E5]

Catalog Number: (CA80017-326)
Supplier: MilliporeSigma
Description: Matrix metalloproteinases (MMPs) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. In addition to sequence homology, all MMPs share the following characteristics: the catalytic mechanism is dependent upon a zinc ion at the active center, they cleave one or more extracellular matrix components, they are secreted as zymogens which are activated by removal of an ~10 kDa segment from the N-terminus and they are inhibited by tissue inhibitor of metalloproteinases (TIMP). These enzymes are involved in normal physiological processes such as embryogenesis and tissue remodeling and may play an important role in arthritis, periodontitis, and metastasis.MMP-1 (interstitial collagenase, tissue collagenase, fibroblast collagenase) is secreted as a 57/52 kDa zymogen which is proteolytically processed to the 46/42 kDa active forms. This enzyme displays substrate specificity toward type I, II, III, VII, VIII and X collagens and gelatin. MMP-1 is thought to play an important role in pathophysiological degradation processes associated with conditions such as rheumatoid arthritis, osteoarthritis, and cancer cell invasion.
Image Unavailable-76303-716

Human;Mouse;Rat Recombinant Myostatin (from E. coli)

Catalog Number: (76303-716)
Supplier: Peprotech
Description: Myostatin is a TGF-beta family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation, and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the activin-binding protein follistatin, and by the propeptide of myostatin. Recombinant Human/Murine/Rat Myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond. The amino acid sequence of mature myostatin is extremely conserved across species, and is the same in murine, rat, chicken, turkey, porcine, and human. Myostatin is expressed as the C-terminal part of a precursor polypeptide, which also contains a short N-terminal signal sequence for secretion, and a propeptide of 243 amino acids. After dimerization of this precursor, the covalent bonds between the propeptide and the mature ligand are cleaved by furin-type proteases. However, the resulting two proteins remain associated through non-covalent interactions, and are secreted as a latent complex.
Image Unavailable-75789-538

Human Recombinant IFN alpha (from Cells)

Catalog Number: (75789-538)
Supplier: Prosci
Description: Interferon alpha/ beta Receptor 2 (IFN- alpha/ beta R2) is a single-pass type I membrane protein which belongs to the type II cytokine receptor family. It complexes with IFN- alpha/ beta R1 to form the signaling receptor complex for the family of alpha and beta IFN subtypes. By alternative splicing, IFN- alpha/ beta R2 can exist as a secreted soluble protein or as a type I membrane protein. IFN- alpha/ beta R2 is the principal ligand binding subunit of the receptor. Ligand binding is stabilized by the subsequent association with IFN- alpha/ beta R1, resulting in the formation of a signaling ternary receptor complex. IFNAR2 was detected in most lymphocytes, monocytes, and granulocytes, although IFNAR2 expression was higher in the monocytes and granulocytes than in the lymphocytes. Among the lymphocyte subsets, IFNAR2 showed high expression in natural killer (NK) cells and low expression in T lymphocytes. Isoform 1 and isoform 3 of IFNAR2 are directly involved in signal transduction due to their interaction with the TYR kinase, JAK1. Isoform 1 also interacts with the transcriptional factors, STAT1 and STAT2. Both forms are potent inhibitors of type I IFN activity.
Product Image-10797-858

Human Recombinant Renin1 (from HEK293 Cells)

Catalog Number: (10797-858)
Supplier: Prosci
Description: Renin is also known as REN and angiotensinogenase, is a circulating enzyme that participates in the body's renin-angiotensin system (RAS), and plays an essential role in the elevation of arterial blood pressure and increased sodium retention by the kidney. Renin activates the renin-angiotensin system by cleaving angiotensinogen, produced by the liver, to yield angiotensin I, which is further converted into angiotensin II by ACE, the angiotensin-converting enzyme primarily within the capillaries of the lungs. Renin is secreted from kidney cells, which are activated via signaling from the macula densa, which responds to the rate of fluid flow through the distal tubule, by decreases in renal perfusion pressure (through stretch receptors in the vascular wall), and by sympathetic nervous stimulation, mainly through beta-1 receptor activation. Renin can bind to ATP6AP2, which results in a fourfold increase in the conversion of angiotensinogen to angiotensin I over that shown by soluble renin. In addition, renin binding results in phosphorylation of serine and tyrosine residues of ATP6AP2. The level of renin mRNA appears to be modulated by the binding of HADHB, HuR and CP1 to a regulatory region in the 3' UTR. An over-active renin-angiotension system leads to vasoconstriction and retention of sodium and water. These effects lead to hypertension. Therefore, renin inhibitors can be used for the treatment of hypertension.
Image Unavailable-10779-064

Human;Mouse;Rat Recombinant Myostatin (from E. coli)

Supplier: Peprotech
Description: Myostatin is a TGF-β family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation, and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the activin-binding protein follistatin, and by the propeptide of myostatin. The amino acid sequence of mature myostatin is extremely conserved across species, and is the same in murine, rat, chicken, turkey, porcine, and human. Myostatin is expressed as the C-terminal part of a precursor polypeptide, which also contains a short N-terminal signal sequence for secretion, and a propeptide of 243 amino acids. After dimerization of this precursor, the covalent bonds between the propeptide and the mature ligand are cleaved by furin-type proteases. However, the resulting two proteins remain associated through non-covalent interactions, and are secreted as a latent complex. Recombinant Human/Murine/Rat Myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond.

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Image Unavailable-75790-406

Human Recombinant IFN alpha (from Cells)

Catalog Number: (75790-406)
Supplier: Prosci
Description: Interferon alpha/ beta Receptor 2 (IFN- alpha/ beta R2) is a single-pass type I membrane protein which belongs to the type II cytokine receptor family. It complexes with IFN- alpha/ beta R1 to form the signaling receptor complex for the family of alpha and beta IFN subtypes. By alternative splicing, IFN- alpha/ beta R2 can exist as a secreted soluble protein or as a type I membrane protein. IFN- alpha/ beta R2 is the principal ligand binding subunit of the receptor. Ligand binding is stabilized by the subsequent association with IFN- alpha/ beta R1, resulting in the formation of a signaling ternary receptor complex. IFNAR2 was detected in most lymphocytes, monocytes, and granulocytes, although IFNAR2 expression was higher in the monocytes and granulocytes than in the lymphocytes. Among the lymphocyte subsets, IFNAR2 showed high expression in natural killer (NK) cells and low expression in T lymphocytes. Isoform 1 and isoform 3 of IFNAR2 are directly involved in signal transduction due to their interaction with the TYR kinase, JAK1. Isoform 1 also interacts with the transcriptional factors, STAT1 and STAT2. Both forms are potent inhibitors of type I IFN activity.
Product Image-10095-188

Anti-SRPX2 Rabbit Polyclonal Antibody

Catalog Number: (10095-188)
Supplier: Proteintech
Description: SRPX2 (sushi-repeat-containing protein, X-linked 2) is a secreted protein expressed in neurons of the human adult brain, including the rolandic area . Firstly described as sushi-repeat protein up-regulated in leukemia (SPRUL) in leukemia cells with dysregulated expression at the transcriptional level, SRPX2 has been recently shown as a multifunctional protein. SRPX2 is a ligand for uPAR, the urokinase-type plasminogen activator (uPA) receptor . It is involved in seizure disorders, angiogenesis and cellular adhesion . The involvement of SRPX2 in disorders of language cortex and cognition suggests it has an important role in the perisylvian region critical for language and cognitive development .
Product Image-10110-136

Anti-POLR2H Rabbit Polyclonal Antibody

Catalog Number: (10110-136)
Supplier: Prosci
Description: POLR2H is one of the essential subunits of RNA polymerase II that is shared by the other two eukaryotic DNA-directed RNA polymerases, I and III.This gene encodes one of the essential subunits of RNA polymerase II that is shared by the other two eukaryotic DNA-directed RNA polymerases, I and III. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. This gene encodes a member of the E2F transcription factor protein family. E2F family members play a crucial role in control of the cell cycle and of the action of tumor suppressor proteins. They are also a target of the transforming proteins of small DNA tumor viruses. Many E2F proteins contain several evolutionarily conserved domains: a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. The encoded protein of this gene is atypical because it lacks the transactivation and tumor suppressor protein association domains. It contains a modular suppression domain and is an inhibitor of E2F-dependent transcription. The protein is part of a multimeric protein complex that contains a histone methyltransferase and the transcription factors Mga and Max. Multiple transcript variants have been reported for this gene, but it has not been clearly demonstrated that they encode valid isoforms. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. PRIMARYREFSEQ_SPAN PRIMARY_IDENTIFIER PRIMARY_SPAN COMP 1-400 AU142999.1 1-400 401-907 BI772069.1 287-793 908-1792 BC008348.1 928-1812 1793-3185 AC099344.4 111461-112853 c
Image Unavailable-CAPIPA5-18806

Anti-F13A1 Goat Polyclonal Antibody

Catalog Number: (CAPIPA5-18806)
Supplier: Thermo Scientific
Description: This antibody is predicted to react with mouse based on sequence homology. This gene encodes the coagulation factor XIII A subunit. Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as plasma carrier molecules. Platelet factor XIII is comprised only of 2 A subunits, which are identical to those of plasma origin. Upon cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. It also crosslinks alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin. Factor XIII deficiency is classified into two categories: type I deficiency, characterized by the lack of both the A and B subunits; and type II deficiency, characterized by the lack of the A subunit alone. These defects can result in a lifelong bleeding tendency, defective wound healing, and habitual abortion.
Image Unavailable-102943-466

Recombinant Human Proline-Rich Acidic Protein 1, Bon Opus Biosciences

Supplier: Bon Opus Biosciences
Description: Bon Opus Biosciences offers quality recombinant proteins products covering a broad collection of cytokines, enzymes, diagnostic and detection reagents, and other protein-related products

Image Unavailable-CA80001-992

Human Recombinant MMP-3

Catalog Number: (CA80001-992)
Supplier: MilliporeSigma
Description: Recombinant, human pro-MMP-3 purified from cell culture supernatant. May be used as a positive control or standard for zymographic analysis, or substrate assay. Requires activation for immunoblotting, prior to use. M.W. 57000/58000. Matrix metalloproteinases (MMPs) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. In addition to sequence homology, all MMPs share the following characteristics: the catalytic mechanism is dependent upon a zinc ion at the active center, they cleave one or more extracellular matrix components, they are secreted as zymogens which are activated by removal of an approximately 10 kDa segment from the N terminus and they are inhibited by tissue inhibitor of metalloproteinases (TIMP). These enzymes are involved in normal physiological processes such as embryogenesis and tissue remodeling and may play an important role in angiogenesis, arthritis, periodontitis, and metastasis. Matrix metalloproteinase-3 (MMP-3) also known as stromelysin-1 and transin (EC 3.4.24.17) cleaves a number of substrates including cartilage proteoglycan, collagen types II, III, IV, V and IX, fibronectin, laminin, and can activate MMP 1. MMP-3 is secreted as ~57 and ~59 kDa proenzymes and can be activated in vitro by organomercurials (e.g., 4 aminophenylmercuric acetate, APMA) and in vivo by proteases via intermediate forms to a 45 kDa active MMP 3 enzyme. Further autolysis to a ~28 kDa form can also occur. MMP-3 is thought to play an important role in pathophysiological degradation processes associated with conditions such as rheumatoid arthritis and cancer cell invasion.

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Image Unavailable-10072-930

Human Recombinant IGFBP4

Catalog Number: (10072-930)
Supplier: Prosci
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 25.8 kDa protein consisting of 237 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Product Image-89150-664

Mitoxantrone dihydrochloride (synthetic) ≥97%

Supplier: Enzo Life Sciences
Description: Antiviral, antibacterial, antiprotozoal, immunomodulating, and antineoplastic cytostatic anthraquinone derivative

Product Image-97062-922

Ribonuclease Inhibitor (RNase Inhibitor)

Catalog Number: (97062-922)
Supplier: VWR
Description: RNase Inhibitor is used to inhibit the activity of RNases in reaction mixtures for cDNA synthesis and in vitro transcription, as well as for long term storage of valuable RNA samples

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