Hledali jste: Protilátky

Supplier: ENZO LIFE SCIENCES

The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.

Supplier: ENZO LIFE SCIENCES

The Hsp70 family of heat shock proteins contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.

Supplier: ENZO LIFE SCIENCES

The Hsp70 family of heat shock proteins contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.

Supplier: Novus Biologicals

The DERP2 Antibody (H.AK6.A3.F4) from Novus Biologicals is a human monoclonal antibody to DERP2. This antibody reacts with human, other. The DERP2 Antibody (H.AK6.A3.F4) has been validated for the following applications: ELISA.

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Acetylation and methylation of lysine are important post-translational modifications that regulate numerous protein-protein and protein-DNA interactions. Lysine acetylation and methylation involves the transfer of acetylCoA, or one or more methyl groups, to the e-amino group of lysine by modifying enzymes and cofactors. Histones and transcription factors are the primary targets of lysine acetylation and methylation, with either modification capable of inducing gene silencing or expression due to differential regulation of cofactors. For example, varying degrees of mono-, di-, and tri-methylation or acetylation of histone H3 at lysine residue 9 are known to demark distinct chromatin regions during various states of gene activation (methylation) or repression (acetylation).

Supplier: ENZO LIFE SCIENCES

The VSV-G Tag (YTDIEMNRLGK) corresponds to the partial peptide sequence of the vesicular stomatitis virus glycoprotein.

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Heme Oxygenase-1 (HO-1) also known as Hsp32, is the inducible isoform of heme oxygenase that catalyzes the NADPH, oxygen, and cytochrome P450 reductase dependent oxidation of heme to carbon monoxide, ferrous iron and biliverdin which is rapidly reduced to bilirubin. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator and has been implicated to be a physiological regulator of cGMP and vascular tone; biliverdin and its product bilirubin are potent antioxidants; "free" iron increases oxidative stress and regulates the expression of many mRNAs (e.g., DCT-1, ferritin and transferring receptor) by affecting the conformation of iron regulatory protein (IRP)-1 and its binding to iron regulatory elements (IREs) in the 5'- or 3'- UTRs of the mRNAs. To date, three identified heme oxygenase isoforms are part of the HO system that catalyze heme into biliverdin and carbon monoxide. These are inducible HO-1 or Hsp32, constitutive HO-2 that is abundant in the brain and testis, and HO-3 which is related to HO-2 but is the product of a different gene. The HO system is the rate-limiting step in heme degradation and HO activity decreases the levels of heme which is a well known potent catalyst of lipid peroxidation and oxygen radical formation.

Supplier: ENZO LIFE SCIENCES

Host: Mouse, Isotype: IgG2a

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DR4 is 56kDa member 10A of the TNFR superfamily (TNFRSF10A), also known as TRAIL-R1, Apo-2, and CD261. It is expressed at low levels by activated T cells and some tumors. After TRAIL engagement, DR4 (TRAIL-R1), through activation of NF-κB, induces apoptosis in the TRAIL ligated cell.

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Host: Rat, Isotype: IgG1

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Host: Mouse, Isotype: IgG1

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Host: Mouse, Isotype: IgG1

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Host: Mouse, Isotype: IgG1

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LRRC32 (leucine rich repeat containing 32; also known as GARP or Garpin; Glycoprotein A repetitions predominant) is a glycoprotein expressed on the cell surface of megakaryocytes, platelets and activated regulatory T (Treg) cells.

Supplier: ENZO LIFE SCIENCES

CaMKIIa, the alpha subunit of Ca2+ calmodulin-dependent protein kinase II is part of a family of multifunctional protein kinases, which play a major role in Ca2+-mediated signal transduction.  CaMKIIa is expressed in many different tissues but is specifically found in the neurons of the forebrain and its mRNA is found within the dendrites as well as the soma of the neuron.  The neuronal CaMKII consists of two major subunits of 52 and 60 kDa which are encoded by a- and b-CaMKII genes, respectively.  Additional isoforms are generated by alternative splicing of these as well as of the ubiquitious g- and d-CaMKII genes.  Each subunit has an ATP-binding domain (arginine-X-X-serune/threonine), consensus phosphorylation site, catalytic domain, and a centrally located regulatory domain which has calmodulin binding activity. Activation and autophosphorylation of CaMKII may regulate numerous neuronal processes which includes two forms of synaptic plasticity, long term potentiation and long term depression.  Neuronal CaMKII subunits assemble as large multimeric holoenzymes.  The C-terminal association domains of  6-12 subunits assemble into a central globular structure from which the N-terminal catalytic/regulatory domains extend radially like petals of a flower. The subunit composition of the rat forebrain CaMKII holoenzyme consists of heteromers composed of a and β subunits at a ratio of 2:1 and homomers composed of only a subunits.  The association of CaMKII subunits leads to the positioning of their catalytic/regulatory domains in close proximity and the neighboring calmodulin-bound subunits cooperate to rapidly phosphorylate each other.  Autophosphorylation also enables CaMKII to attain an enhanced affinity for NMDA receptors in postsynaptic densities.

Supplier: ENZO LIFE SCIENCES

Tumor necrosis factor alpha (TNF-α), also known as cachectin, is a 17.5 kDa 157 amino acid member of the TNF superfamily of cytokines that is a potent lymphoid factor with effects on a wide range of target cells. Active TNFalpha is produced in both soluble and membrane-anchored trimers by macrophages, NK cells, and T- and B-lymphocytes. TNF exerts proinflammatory signals via binding and inducing trimerization of TNF-receptor1 (TNF-R1) expressed on most normal and transformed cells, or to TNF-receptor 2 (TNF-R2), expressed on endothelial and most immune cells. TNF signaling regulates hematopeiesis, differentation, endothelial cell activation, apoptosis, lipid metabolism, tumor progression, and immune suveillance, and dysregulation of TNF or its receptors is implicated in numerous disease states including cancer, osteoporosis, autoimmune disease, diabetes, and atherosclerosis.

Supplier: ENZO LIFE SCIENCES

The TLRs (Toll-like receptors) are a group of evolutionarily conserved pattern recognition molecules that play a key role in host defense during microbial infection by regulating both innate and adaptive immune responses. TLRs are type I transmembrane proteins with ectodomains containing interspersed leucine-rich repeat (LRR) motifs that are involved in the recognition of various microbial ligands.

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Vasoactive intestinal peptide (VIP) is a 28-amino-acid peptide belonging to the secretin-glucagon family of peptide hormones. Its sequence is identical in man, ox, pig and rat. VIP is widely distributed in the central and peripheral nervous systems, acting as a neurotransmitter or neuromodulator. Peripherally it is involved in vaso- and bronchodilatation, smooth muscle relaxation and stimulation of secretion. Ectopic endocrine tumors secreting VIP (VIPomas) lead to raised plasma levels of VIP and are associated with watery diarrhea, hypokalemia and achlorhydria syndrome. VIP shows high sequence homology with peptide histidine-methionine (PHM) in man or peptide histidine-serine (PHI) in pigs or rats, present in the same precursor, and with the neuropeptide pituitary adenylate cyclase activating polypeptide (PACAP).

Supplier: ENZO LIFE SCIENCES

Anti-GRP78 Rabbit Polyclonal Antibody

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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.

Supplier: ENZO LIFE SCIENCES

p23 is a ubiquitous, highly conserved co-chaperone for Hsp90 that participates in the folding of a number of cell regulatory proteins including progesterone and glucocorticoid receptors, HSF1, and telomerase. p23 is thought to modulate Hsp90 activity in the last stages of the chaperoning pathway by binding and stabilizing Hsp90 in its ATP-bound state.

Supplier: ENZO LIFE SCIENCES

Hsp60 is a member of the chaperonin family of heat shock proteins, with homologs functioning in the cytosol and mitochondria to fold nascent and aggregated proteins. Hsp60 is the eukaryotic homolog of the E. coli GroEL protein, and forms a multimeric complex in the mitochondria with Hsp10 (Cpn10) to form a large central cavity in which ATP-dependent protein folding takes place. TRiC/CCT, a eukaryotic relative of Hsp60, is expressed in the cytosol and participates in the folding of actin and tubulin substrates, but lacks any association with an Hsp10-like co-factor.

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Recommended Applications: IF, IHC, IP, WB

Species reactivity:

Supplier: ENZO LIFE SCIENCES

Recommended Applications: Flow Cytometry, IF

Species reactivity: Human

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Host: Mouse, Isotype: IgM

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Host: Mouse, Isotype: IgG1

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The proteasome is widely recognised as the central enzyme of non-lysosomal protein degradation. It is responsible for intracellular protein turnover and it is also critically involved in many regulatory processes and, in higher eukaryotes, in antigen processing.

Supplier: ENZO LIFE SCIENCES

Recombinant PI31 has been shown to compete with the proteasome regulators PA28 and 19S PA700 for binding to 20S, indicating that PI31 binds the 20S α-rings and may function by hindering substrate access to the 20S catalytic channel.

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PDK-1 (Pyruvate dehydrogenase kinase-1) is a 48 kDa protein kinase. It is a member of the mitrochondrial matrix protein kinase family and is related to the histidine protein kinases found in prokaryotes. PDK-1 is responsible for phosphorylation and concomitant inactivation of pyruvate dehydrogenase.

Supplier: ENZO LIFE SCIENCES

Protein Kinase C (PKC) is a large superfamily of serine/threonine kinases that mediate essential cellular signals required for activation, proliferation, differentiation and survival. There are at least ten PKC isotypes that are closely related in structure but that have distinct patterns of tissue distribution and function. The PKC isotypes can be subdivided into three classes based on primary structure and biochemical properties. These are: classical or conventional PKC isotypes (cPKC), novel PKC isotypes (nPKC) and atypical PKC isotypes (aPKC).