You Searched For: Thiol-PEG3-acid

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Anti-CRP55 Mouse Monoclonal Antibody (PE (Phycoerythrin)) [clone: FMC 75]

Supplier: ENZO LIFE SCIENCES

Description: The multifunctional, multi -compartmental protein Calreticulin (Crt) functions as a soluble molecular chaperone of new or misfolded proteins, as well as a Ca2+-binding protein. Most abundant in the ER lumen, Crt expression also occurs in other membrane-bound organelles, the cell surface, and extracellularly. Also known as CRP-55, calregulin and HACBP (high affinity calcium-binding protein), Crt contains the ER-retrieval sequence, KDEL, and is the solub le paralog of the ER membrane protein Calnexin (Cnx). Crt's three domains include a 180 residue N-terminal domain, a proline-rich Pdomainresidues 189 -288) that binds Ca2+ with high affinity and shares homology with Cnx and calmegin, and a 110 residue C-terminal domain that binds Ca2+ with low affinity but high capacity. The P-domain may interact with the co-chaperone ERp57 (Grp58), a thiol reductase. The NMR structure of the P -domain consists of an extended hairpin that appears to form a curved protrusion from the Crt core domain. Both Crt and its membrane bound homolog CNX interact with proteins and glycoproteins possessing monoglucosylated N -glycans. The Crt/Cnx cycle promotes correct folding, inhibits aggregation of folding intermediates, blocks premature oligomerization, regulates ER degradation, and prevents incompletely folded glycoproteins from exiting to the Golgi complex. Crt also appears to function as an auto-antigen in systemic lupus erythematosus, rheumatoid arthritis, celiac disease, complete congenital heart block, and halothane hepatitis. A diversity of additional functions attributed to Crt includes adhesion, blood function, and cardiac and neuronal development gene expression.

Human recombinant Cathepsin B (from HEK293 cells)

Catalog Number: (PRSI96-223)

Supplier: ProSci Inc.

Description: Cathepsin B (CTSB) is also known as APP secretase (APPS) and CPSB, is an enzymatic protein belonging to the peptidase C1 family. Cathepsin B / CTSB is synthesized as a preproenzyme. Following removal of the signal peptide, the inactive proenzyme undergoes further modifications including removal of the pro region to result in the active enzyme. The catalytic activity of Cathepsin B / APPS contains: Hydrolysis of proteins with broad specificity for peptide bonds; Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L); In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides. As a thiol protease, cathepsin B / CPSB is believed to participate in intracellular degradation and turnover of proteins and has also been implicated in tumor invasion and metastasis. Overexpression of cathepsin B has been associated with esophageal adenocarcinoma and other tumors.

UOM: 1 * 50 µG

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Anti-C3 Chicken Polyclonal Antibody

Catalog Number: (PRSIXW-7061)

Supplier: ProSci Inc.

Description: Human complement component C3. Complement C3 contains two chains linked by a disulfide bond. Its activation by a C3 convertase releases the C3a anaphylatoxin from the amino end of the beta chain and generates C3b, which associates with the Bb fragment of complement factor B to form the alternative-complement-pathway C3/C5 convertase.C3a anaphylatoxin is a vasoactive peptide and a mediator of inflammation. C3b, with its highly reactive thiol group, binds to the surface of foreign particles and facilitates phagocytosis. It binds to complement C5 and renders it susceptible to proteolysis by the classical-complement-pathway C3/C5 convertase. The activity of C3b is regulated by proteolytic cleavage involving factors H and I. Its degradation products can also be biologically active.

UOM: 1 * 50 µG

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Anti-CAPN10 Rabbit Polyclonal Antibody

Catalog Number: (PRSI26-646)

Supplier: ProSci Inc.

Description: CAPN10 is the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.Calpains are ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. The calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits. The large catalytic subunit has four domains: domain I, the N-terminal regulatory domain that is processed upon calpain activation; domain II, the protease domain; domain III, a linker domain of unknown function; and domain IV, the calmodulin-like calcium-binding domain. This gene encodes a large subunit. It is an atypical calpain in that it lacks the calmodulin-like calcium-binding domain and instead has a divergent C-terminal domain. It is similar in organization to calpains 5 and 6. This gene is associated with type 2 or non-insulin-dependent diabetes mellitus (NIDDM) and located within the NIDDM1 region. Multiple alternative transcript variants encoding different isoforms have been described for this gene.

UOM: 1 * 50 µG

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