Sie suchten nach: Antikörper

Lieferant: ENZO LIFE SCIENCES

Beschreibung: 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.

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Lieferant: ENZO LIFE SCIENCES

Beschreibung: 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.

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Lieferant: ENZO LIFE SCIENCES

Beschreibung: 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.

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Artikel-Nr: (NOVUDDX0210P-100)

Lieferant: Novus Biologicals

Beschreibung: 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.

UOM: 1 * 100 µG

Aktion

Artikel-Nr: (NOVUNBP2-33054AF64)

Lieferant: Novus Biologicals

Beschreibung: Mucosa-associated lymphoid tissue lymphoma translocation protein 1 (MALT1), also known as MLT1 or paracaspase 1, is a member of the human paracaspase family and an interacting partner of B-cell lymphoma 10 (Bcl-10) (1). <i>In vitro</i>, <i>In vitro</i>, MALT1 synergises with BCL10 to enhance nuclear factor B activation (2) and to mediate IB kinase (IKK) activation by facilitating the ubiquitinylation of the NF-B essential modulator (NEMO) (3).

UOM: 1 * 0,1 mL

Aktion

Artikel-Nr: (ENZOADIKAPTF120E)

Lieferant: ENZO LIFE SCIENCES

Beschreibung: 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).

UOM: 1 * 100 µG

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Artikel-Nr: (ENZOADIMSA115E)

Lieferant: ENZO LIFE SCIENCES

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

UOM: 1 * 100 µl

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Lieferant: ENZO LIFE SCIENCES

Beschreibung: 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.

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Artikel-Nr: (ENZOALX805053C100)

Lieferant: ENZO LIFE SCIENCES

Beschreibung: Host: Mouse, Isotype: IgG2a

UOM: 1 * 100 µG

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Artikel-Nr: (ENZOALX8049120100)

Lieferant: ENZO LIFE SCIENCES

Beschreibung: 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.

UOM: 1 * 100 µG

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Artikel-Nr: (ENZOALX805045C050)

Lieferant: ENZO LIFE SCIENCES

Beschreibung: Host: Rat, Isotype: IgG1

UOM: 1 * 50 µG

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Artikel-Nr: (ENZOALX805023C100)

Lieferant: ENZO LIFE SCIENCES

Beschreibung: Host: Mouse, Isotype: IgG1

UOM: 1 * 100 µG

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Artikel-Nr: (ENZOALX805016C050)

Lieferant: ENZO LIFE SCIENCES

Beschreibung: Host: Mouse, Isotype: IgG1

UOM: 1 * 50 µG

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Artikel-Nr: (ENZOALX805037C100)

Lieferant: ENZO LIFE SCIENCES

Beschreibung: Host: Mouse, Isotype: IgG1

UOM: 1 * 100 µG

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Artikel-Nr: (ENZOALX804867C100)

Lieferant: ENZO LIFE SCIENCES

Beschreibung: 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.

UOM: 1 * 100 µG

New Product Aktion

Lieferant: ENZO LIFE SCIENCES

Beschreibung: 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.

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