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Catalog Number: (97062-538)
Supplier: VWR
Description: Offers blocking and hybridization for optimized complimentary base pairing of DNA and RNA in Southern blot, Northern blot, dot blot, colony and in situ hybridization.

Catalog Number: (56615-928)
Supplier: 3M
Description: Accessories for PELTOR™ Optime™ Series Earmuffs, 3M


Catalog Number: (10232-868)
Supplier: Bioss
Description: Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity.


Supplier: Enzo Life Sciences
Description: 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
Description: 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.

SDS

Catalog Number: (95056-572)
Supplier: Enzo Life Sciences
Description: 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.

SDS


Supplier: Arlington Scientific
Description: A non-mammalian blocking reagent supplied in PBS for diagnostic systems involving membrane or other solid phase material.

Catalog Number: (10295-878)
Supplier: Bioss
Description: GCN1L1 is a 2,671 amino acid protein that is ubiquitously expressed and belongs to the GCN1 family. Functioning as a translation activator, GCN1L1 interacts with IMPACT to regulproteinate GCN2 kinase activity. GCN1L1 contains 24 HEAT repeats and is encoded by a gene that maps to human chromosome 12q24.23. Chromosome 12 encodes over 1,100 genes and comprises approximately 4.5% of the human genome. Chromosome 12 is associated with a variety of diseases and afflictions, including hypochondrogenesis, achondrogenesis, Kniest dysplasia, Noonan syndrome and trisomy 12p, which causes facial developmental defects and seizure disorders.


Supplier: Enzo Life Sciences
Description: 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.

Catalog Number: (10802-414)
Supplier: Rockland Immunochemical
Description: CNOT4 is a component of the CCR4-NOT transcription complex, a complex that is implicated in the repression of RNA polymerase II transcription. In the CCR4-NOT complex, CNOT4 acts as an E3 ubiquitin-protein ligase and interacts with a subset of E2 ubiquitin-conjugating enzymes through a unique C4C4 RING domain. This E3 ligase activity was shown to be dependent on the selective and specific interaction with the ubiquitin conjugating enzyme UbcH5B. In yeast, mutations in CNOT4 that prevented its interaction with the UbcH5B homolog UBC4 caused increased sensitivity to hydroxyurea, heat shock, and hygromycin B, suggesting that CNOT4 and UbcH5B are involved in stress response in vivo. Multiple isoforms of CNOT4 are known to exist.


Supplier: Rockland Immunochemical
Description: Use BLOTTO whenever procedures call for immunoanalytical grade non-fat dry milk

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Catalog Number: (10206-668)
Supplier: Boster Biological Technology
Description: Polyclonal antibody for COFILIN/CFL1 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: ELISA. Reactive species: Human. COFILIN/CFL1 information: Molecular Weight: 18502 MW; Subcellular Localization: Nucleus matrix . Cytoplasm, cytoskeleton . Cell projection, ruffle membrane ; Peripheral membrane protein ; Cytoplasmic side . Cell projection, lamellipodium membrane ; Peripheral membrane protein ; Cytoplasmic side . Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide; Tissue Specificity: Widely distributed in various tissues.


Catalog Number: (10463-304)
Supplier: Bioss
Description: SAP 155 is a 1,304 amino acid member of the SF3B1 family and contains eleven HEAT repeats. Localized to nuclear speckles and also to the cytoplasm during mitosis, SAP 155 is a subunit of the SF3B splicing factor. The SF3B splicing factor is a U2 snRNP-associated protein complex essential for spliceosome assembly. SF3B contains the spliceosomal proteins SAP 49, SAP 130, SAP 145 and SAP 155. Concomitant with splicing catalysis, SAP 155 is phosphorylated at its N-terminal Thr-Pro dipeptide motifs by Dyrk1A and cyclin E/Cdk2. This modification of SAP 155 is vital for a functional spliceosome as it is an essential event in the basic splicing reaction. Due to alternative splicing events, various SAP 155 isoforms are produced.


Catalog Number: (10463-306)
Supplier: Bioss
Description: SAP 155 is a 1,304 amino acid member of the SF3B1 family and contains eleven HEAT repeats. Localized to nuclear speckles and also to the cytoplasm during mitosis, SAP 155 is a subunit of the SF3B splicing factor. The SF3B splicing factor is a U2 snRNP-associated protein complex essential for spliceosome assembly. SF3B contains the spliceosomal proteins SAP 49, SAP 130, SAP 145 and SAP 155. Concomitant with splicing catalysis, SAP 155 is phosphorylated at its N-terminal Thr-Pro dipeptide motifs by Dyrk1A and cyclin E/Cdk2. This modification of SAP 155 is vital for a functional spliceosome as it is an essential event in the basic splicing reaction. Due to alternative splicing events, various SAP 155 isoforms are produced.


Catalog Number: (95046-292)
Supplier: Enzo Life Sciences
Description: 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.


Catalog Number: (77438-204)
Supplier: Bioss
Description: This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two repeats of quasi-RRM domains that bind to RNAs. It is localized in nuclear bodies of the nucleus. This protein is involved in the splicing process and it also participates in early heat shock-induced splicing arrest by transiently leaving the hnRNP complexes. Several alternatively spliced transcript variants have been noted for this gene, however, not all are fully characterized. [provided by RefSeq, Jul 2008].


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