Microsize antibodies for $99 | Learn More >>

Antibody Sampler Kit Zinc Ion Binding

The Jumonji Family Antibody Sampler Kit provides an economical means of evaluating total levels of Jumonji family proteins. The kit contains enough primary antibodies to perform two western blot experiments with each primary antibody.
The Nuclear Receptor Antibody Sampler Kit provides an economical means to evaluate the presence and status of nuclear receptors. This kit contains enough primary antibody to perform two western blots per primary.
The Matrix Remodeling Antibody Sampler Kit provides an economical means of detecting different MMPs and TIMPs using the specific corresponding antibodies. The kit contains enough antibody to perform at least two western blot experiments with each primary antibody.

Background: Matrix remodeling is mainly controlled by MMPs and TIMPs. The matrix metalloproteinase (MMP) family of proteases are a group of zinc-dependent enzymes that target extracellular proteins, including growth factors, cell surface receptors, adhesion molecules, matrix structural proteins, and other proteases (1, 2). Among the family members, MMP-2, MMP-3, MMP-7, MMP-9, and MMP14 (MT1-MMP) have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis (3). MMP activity is regulated by mechanisms of both transcriptional control and post translational protein processing. Once synthesized, MMPs exist as latent proenzymes. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full-length protein (4). MMP activity can be inhibited through its binding to endogenously expressed TIMPs. TIMPs are members of the family of tissue inhibitors of matrix metalloproteinases that include TIMP1, TIMP2, TIMP3, and TIMP4. The main function of TIMPs is their inhibitory effect on MMPs. TIMPs irreversibly inactivate MMPs by direct binding MMPs and chelating their zinc cofactor at the catalytic site to inhibit the proteinase function (5,6).

The Retinoic Acid and Retinoid X Receptors Antibody Sampler Kit provides an economical means to investigate the expression of various subtypes of retinoic acid and retinoid X receptors. The kit contains enough primary antibody to perform two western blot experiments per primary.
The Jak/Stat Pathway Inhibitors Antibody Sampler Kit provides an economical means to examine several inhibitors of Jak/Stat signaling, including PIAS1, PIAS3, PIAS4, SOCS1, SOCS2, and SOCS3. The kit contains enough primary antibody to perform two western blot experiments with each primary antibody.
The IAP Family Antibody Sampler Kit provides an economical means to investigate the expression of various IAP family members within the cell. The kit contains enough primary and secondary antibodies to perform two Western blot experiments.

Background: The inhibitor of apoptosis protein (IAP) family consists of an evolutionarily conserved group of apoptosis inhibitors containing a conserved 70 amino acid BIR (baculovirus inhibitor repeat) domain (1,2). Human members of this family include c-IAP1, c-IAP2, XIAP, survivin, livin, and NAIP. Overexpression of IAP family members, particularly survivin and livin, in cancer cell lines and primary tumors suggests an important role for these proteins in cancer progression (3-5). In general, the IAP proteins function through direct interactions to inhibit the activity of several caspases, including caspase-3, caspase-7, and caspase-9 (5,6). In addition, binding of IAP family members to the mitochondrial protein Smac blocks their interaction with caspase-9, thereby allowing the processing and activation of the caspase (2).

The TRAF Antibody Sampler Kit provides an economical means to evaluate endogenous levels of TRAF1, 2, 3, and 6. The kit contains enough primary and secondary antibodies to perform two western mini-blot experiments.

Background: TRAFs (TNF receptor-associated factors) are a family of multifunctional adaptor proteins that bind to surface receptors and recruit additional proteins to form multiprotein signaling complexes capable of promoting cellular responses (1-3). Members of the TRAF family share a common carboxy-terminal "TRAF domain", which mediates interactions with associated proteins; many also contain amino-terminal Zinc/RING finger motifs. The first TRAFs identified, TRAF1 and TRAF2, were found by virtue of their interactions with the cytoplasmic domain of TNF-receptor 2 (TNFRII) (4). The six known TRAFs (TRAF1-6) act as adaptor proteins for a wide range of cell surface receptors and participate in the regulation of cell survival, proliferation, differentiation, and stress responses.

The Sirtuin Antibody Sampler Kit provides an economical means of evaluating total levels of sirtuin proteins. The kit includes enough antibody to perform at least two western blot experiments with each primary antibody.
The SET1/COMPASS Antibody Sampler Kit provides an economical means of detecting SET1/COMPASS proteins using control antibodies against SET1A, SET1B, MLL1, MLL2, WDR5, WDR82, and Menin. This kit contains enough primary antibodies to perform at least two western blot experiments.

Background: The Set1 histone methyltransferase protein was first identified in yeast as part of the Set1/COMPASS histone methyltransferase complex, which methylates histone H3 on lysine 4 and functions as a transcriptional co-activator (1). While yeast contain only one known Set1 protein, mammals contain six Set1-related proteins: SET1A, SET1B, MLL1, MLL2, MLL3 and MLL4, all of which methylate histone H3 on lysine 4 (2,3). These Set1-related proteins are each found in distinct protein complexes, all of which share the common core structural subunits WDR5, RBBP5 and ASH2L (2-6). WDR82 is a core subunit specific to SET1A and SET1B complexes, while Menin is a core subunit specific to the MLL complexes (4,5,7).Like yeast Set1, all six Set1-related mammalian proteins methylate histone H3 on lysine 4 (2-6). SET1A, SET1B, MLL1 and MLL2 mediate di- and tri-methylation of histone H3 Lys4 at gene promoters to facilitate transcription activation. MLL3 and MLL4 function primarily to mono-methylate histone H3 Lys4 at gene enhancers. MLL1 and MLL2 function as master regulators of both embryogenesis and hematopoiesis, and are required for proper expression of Hox genes (8-10). MLL1 is a large approximately 4000 amino acid protein that is cleaved by the Taspase 1 threonine endopeptidase to form N-terminal (MLL1-N) and C-terminal MLL1 (MLL1-C) fragments, both of which are subunits of the functional MLL1/COMPASS complex (11,12). MLL1 translocations are found in a large number of hematological malignancies, suggesting that Set1 histone methyltransferase complexes play a critical role in leukemogenesis (6). Like MLL1, MLL2 is also a large, approximately 2700 amino acid protein that is cleaved by the Taspase 1 threonine endopeptidase to form N-terminal (MLL2-N) and C-terminal (MLL2-C) fragments, both of which are subunits of the functional MLL2/COMPASS complex. MLL2 has also been implicated as a modulator of hematological malignancies (13). MLL3 and MLL4 proteins are not cleaved by Taspase 1.

The Huntingtin Interaction Antibody Sampler kit provides an economical means of detecting transcription-related proteins that interact with Huntingtin (Htt). This kit contains enough antibody to perform two western blot experiments per primary antibody.
The DUB Antibody Sampler Kit offers an economical means of evaluating the presence and status of selected DUB enzymes. This kit contains enough primary antibody to perform two western blot experiments per primary.
The Parkinson's Research Antibody Sampler Kit provides an economical means of detecting target proteins related to Parkinson's disease. The kit contains enough primary and secondary antibody to perform two western blots per primary.

Background: Autophagy is a catabolic process for the autophagosome-lysosomal degradation of bulk cytoplasmic contents (1, 2). Selective autophagy targets the degradation of distinct sets of substrates and organelles (3-5). One of the best studied examples of selective autophagy involves the clearance of damaged mitochondria through a process called mitophagy. Several pathways have been described for various contexts of mitophagy, including the FUNDC1 pathway, the BNIP3 and BNIP3L/Nix pathway, and the PINK1/Parkin pathway. FUNDC1 is a mitochondrial protein that is phosphorylated by the autophagy kinase ULK1 and regulates hypoxia induced mitophagy (6, 7). BNIP3L/Nix and BNIP3 are members of the Bcl-2 family of apoptosis regulators that are expressed on mitochondria, induced by hypoxia, and have have been shown to play a role in mitophagy (8). BNIP3L/Nix is also important in the autophagic maturation of erythroid cells (9). FUNDC1, BNIP3 and BNIP3L/Nix bind to LC3 family members, targeting the mitochondria to the autophagosome.Non-hypoxic induction of mitophagy can be regulated by the PINK1/Parkin pathway, which plays causative roles in neurodegenerative disease, most notably Parkinson’s disease (10, 11). PINK1 is a mitochondrial serine/threonine kinase that is stabilized on the outer mitochondrial membrane of damaged mitochondria. Substrates of PINK1 include the E3 ubiquitin ligase Parkin and ubiquitin itself (12-14). Phosphorylation of Parkin as well as binding to phosphorylated ubiquitin leads to accumulation of ubiquitinated chains on multiple mitochondrial proteins. Ubiquitinated proteins are recognized by selective cargo receptors including SQSTM1/p62, Optineurin, and NDP52 (15-16). Autophagy cargo receptors contain an LC3-interacting region (LIR) required for binding to Atg8/LC3 family members and targeting to the autophagosome (3).

The Stress and Apoptosis Antibody Sampler Kit provides an economical means of evaluating stress and apoptotic responses of each protein. The kit contains enough primary and secondary antibody to perform two western blot experiments per primary antibody.
The Notch Receptor Interaction Antibody Sampler Kit provides an economical means to evaluate Notch signaling. The kit contains enough primary antibody to perform two western blots per primary.
The Class II HDAC Antibody Sampler Kit provides an economical means of detecting Class II HDAC proteins using control antibodies against HDAC4, HDAC5, HDAC6, and HDAC7. The kit contains enough primary antibodies to perform at least two western blot experiments.

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

The Vesicle Trafficking Antibody Sampler kit provides an economical means to analyze proteins involved in the intracellular transport of cargo proteins. This kit includes enough primary and secondary antibody to perform two western blot experiments.
The Histone Deacetylase (HDAC) Antibody Sampler Kit provides a fast and economical means to evaluate the endogenous levels of HDACs. The kit contains enough primary and secondary antibodies to perform two Western blot experiments.

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

The Endosomal Marker Antibody Sampler Kit provides an economical means of distinguishing endosomes in the early, late, and recycling phases. The kit includes enough antibody to perform two western blot experiments with each primary antibody.