Text Search >
Nepsilon-(2,4-dinitrophenyl)-L-lysine+hydrochloride
Print…
You Searched For:
37,406 results were found
Nepsilon-(2,4-dinitrophenyl)-L-lysine+hydrochloride
Catalog Number:
(10670-756)
Supplier:
Bioss
Description:
Eukaryotic RNA polymerase II mediates the synthesis of mature and functional messenger RNA. This is a multistep process, called the transcription cycle, that includes five stages: preinitiation, promoter, clearance, elongation and termination. Elongation is thought to be a critical stage for the regulation of gene expression. ELL (11-19 lysine-rich leukemia protein), also designated MEN, functions as an RNA polymerase II elongation factor that increases the rate of transcription by suppressing transient pausing by RNA polymerase II. It is also thought to regulate cellular proliferation. ELL is abundantly expressed in peripheral blood leukocytes, skeletal muscle, placenta and testis, with lower expression in spleen, thymus, heart, brain, lung, kidney, liver and ovary. ELL3 is a 397 amino acid nuclear protein that functions as an RNA polymerase II elongation factor that increases the rate of transcription by suppressing transient pausing by RNA polymerase II. Though similar to ELL and ELL2, ELL3 is exclusively expressed in testis.
Catalog Number:
(10261-422)
Supplier:
Bioss
Description:
ESET is a nuclear protein belonging to the histone-lysine methyltransferase family and to the Suvar3-9 subfamily. It is a highly conserved protein of 150 amino acids that has been implicated in chromatin structure modulation. ESET is excluded from cell nucleoli and areas of condensed chromatin and can associate with the nonpericentromeric regions of chromatin. The gene encoding for this protein, SETDB1, maps to chromosome 1q21. ESET is a histone methyltransferase, methylating Lys-9 of histone H3 and mutations within the SETDB1 gene abolishes its methyltransferase activity. This methylation acts as a tag for epigenetic transcriptional repression by rounding up HP1 proteins to methylated histones. ESET is widely expressed with highest levels found in testis.
Catalog Number:
(10359-474)
Supplier:
Bioss
Description:
Tripartite motif-containing protein 32 (TRIM32) belongs to the tripartite motif (TRIM) protein family. TRIM32, like all TRIM proteins, contains a domain structure composed of a B-box, a RING-finger and a coiled-coil motif. Additionally, TRIM32 has six C-terminal NHL domains; it is expressed mainly in the skeletal muscle. The TRIM32 gene encodes an E3 ubiquitin ligase, a protein that attaches ubiquitin to a lysine residue on a target protein and acts in conjunction with ubiquitin-conjugating enzymes UbcH5a, UbcH5c and UbcH6. Mutations in the TRIM32 gene cause two forms of autosomal recessive muscular dystrophy designated limb girdle muscular dystrophy type 2H (LGMD2H) and sarcotubular myopathy (STM). TRIM32 mutations can also result in Bardet-Biedl syndrome (BBS), an autosomal recessive disorder characterized by pigmentary retinopathy, polydactyly, hypogenitalism, renal abnormalities, learning disabilities and obesity.
Catalog Number:
(62405-113)
Supplier:
Corning
Description:
Tested for ability to initiate neurite outgrowth of NG-108 rat glioma/mouse neuroblastoma cells. Found negative for bacteria, fungi. PDL source: Synthetic molecule. Laminin source: EHS mouse tumor. Stable for 3 months at 2 to 8[degree]C.
Catalog Number:
(10303-904)
Supplier:
Bioss
Description:
Fyb (Fyn binding protein) and the anchoring proteins SKAP55 and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn. SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells. SKAP55 contains an N-terminal pleckstrin homology domain and a C-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain. SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation. The human SKAP55 gene maps to chromosome 17q21.32 and encodes a 359 amino acid protein.
Catalog Number:
(10304-104)
Supplier:
Bioss
Description:
Fyb (Fyn binding protein) and the anchoring proteins SKAP55 and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn. SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells. SKAP55 contains an N-terminal pleckstrin homology domain and a C-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines. SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain. SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation. The human SKAP55 gene maps to chromosome 17q21.32 and encodes a 359 amino acid protein.
Catalog Number:
(75929-402)
Supplier:
Rockland Immunochemical
Description:
KAT8 (MYST1) control protein-GST fusion
Supplier:
Bachem Americas
Description:
Sequence: Fmoc-Lys(4-methoxytrityl)-OH
Catalog Number:
(10347-746)
Supplier:
Bioss
Description:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.
Catalog Number:
(10347-742)
Supplier:
Bioss
Description:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.
Catalog Number:
(10347-738)
Supplier:
Bioss
Description:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.
Catalog Number:
(10347-744)
Supplier:
Bioss
Description:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.
Catalog Number:
(75929-326)
Supplier:
Rockland Immunochemical
Description:
JMJD2b, belongs to the JMJD2 family of histone demethylases which play an important role in the establishment of the histone code. JMJD2b specifically demethylates the trimethylated K9 of histone H3. It is not able to demethylate K4, K27 and K36 of histone H3, nor K20 of histone H4. Anti-JMJD2b Antibody is ideal for research in Epigenetics and Chromatin Remodeling.
Catalog Number:
(10068-440)
Supplier:
Prosci
Description:
Histone Deacetylases (HDACs) are a group of enzymes closely related to sirtuins. They catalyze the removal of acetyl groups from lysine residues in histones and non-histone proteins, resulting in transcriptional repression. In general, they do not act autonomously but as components of large multiprotein complexes, such as pRb-E2F and mSin3A, that mediate important transcription regulatory pathways. There are three classes of HDACs; classes 1, 2 and 4, which are closely related Zn2+-dependent enzymes. HDACs are ubiquitously expressed and they can exist in the nucleus or cytosol. Their subcellular localization is effected by protein-protein interactions (for example HDAC-14.3.3 complexes are retained in the cytosol) and by the class to which they belong (class 1 HDACs are predominantly nuclear whilst class 2 HDACs shuttle between the nucleus and cytosol). HDACs have a role in cell growth arrest, differentiation and death and this has led to substantial interest in HDAC inhibitors as possible antineoplastic agents.
Catalog Number:
(103294-344)
Supplier:
Novus Biologicals
Description:
The Histone H4 [ac Lys8] Antibody from Novus Biologicals is a rabbit polyclonal antibody to Histone H4. This antibody reacts with human, mouse, c. elegans. The Histone H4 [ac Lys8] Antibody has been validated for the following applications: Western Blot, Chromatin Immunoprecipitation, Immunocytochemistry / Immunofluorescence, Dot Blot.
Catalog Number:
(76107-522)
Supplier:
Bioss
Description:
Eukaryotic RNA polymerase II mediates the synthesis of mature and functional messenger RNA. This is a multistep process, called the transcription cycle, that includes five stages: preinitiation, promoter, clearance, elongation and termination. Elongation is thought to be a critical stage for the regulation of gene expression. ELL (11-19 lysine-rich leukemia protein), also designated MEN, functions as an RNA polymerase II elongation factor that increases the rate of transcription by suppressing transient pausing by RNA polymerase II. It is also thought to regulate cellular proliferation. ELL is abundantly expressed in peripheral blood leukocytes, skeletal muscle, placenta and testis, with lower expression in spleen, thymus, heart, brain, lung, kidney, liver and ovary. ELL3 is a 397 amino acid nuclear protein that functions as an RNA polymerase II elongation factor that increases the rate of transcription by suppressing transient pausing by RNA polymerase II. Though similar to ELL and ELL2, ELL3 is exclusively expressed in testis.
Inquire for Price
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
 is still displayed and you need assistance, please call us at 1-800-932-5000.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
is still displayed and you need assistance, please call us at 1-800-932-5000.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
This product has been blocked by your organization. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
This product is no longer available. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service at 1-800-932-5000.
|
|||||||||
List View
