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Supplier: Biotium
Description: This MAb recognizes TGF beta 1, 2 and 3. Three TGF betas have been identified in mammals. TGF beta 1, TGF beta 2 and TGF beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecules. Biologically active TGF beta requires dimerization of the monomers (usually homodimers) and release of the latent peptide portion. Overall, the mature region of the TGF beta 3 protein has approximately 80% identity to the mature region of both TGF beta 1 and TGF beta 2. However, the NH2 terminals or precursor regions of their molecules share only 27% sequence identity. TGF betas inhibit the growth of epithelial cells and stimulate the growth of mesenchymal cells.

Catalog Number: (10072-908)
Supplier: Prosci
Description: 4-1BB Receptor, a member of the TNF superfamily of receptors, is mainly expressed on the surface of a variety of T cells, but also found in B cells, monocytes, and various transformed cell lines. 4-1BB Receptor binds to 4-1BBL to provide a co-stimulatory signal for T lymphocytes. Signaling by 4-1BB Receptor has been implicated in the antigen-presentation process and generation of cytotoxic T cells. The human 4-1BB Receptor gene codes for a 255 amino acid type I transmembrane protein containing a 17 amino acid N-terminal signal sequence, a 169 amino acid extracellular domain, a 27 amino acid transmembrane domain and a 42 amino acid cytoplasmic domain. Recombinant human soluble 4-1BB Receptor is a 167 amino acid polypeptide (17.7 kDa), which contains the cysteine rich TNFR-like extracellular domain of 4-1BB Receptor.


Catalog Number: (77438-100)
Supplier: Bioss
Description: Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. May stimulate transcription mediated by nuclear receptors. May be involved in transcriptional regulation of Hox proteins during cell differentiation. May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1 (By similarity).


Catalog Number: (MSPP-100-1389)
Supplier: STEMCELL Technologies
Description: Stimulating T cells with EBV (LMP2A) peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. EBV (LMP2A) peptide pool is a lyophilized mixture of 27 peptides from latent membrane protein 2A (LMP2A) of Epstein-Barr virus (EBV; strain GD1), and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 118 on LMP2A. LMP2A contributes to the survival of EBV-transformed B cells (Mancao and Hammerschmidt) and mediates partial escape of infected B cells from recognition by EBV-specific CD8+ T cells (Rancan et al). Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.


Catalog Number: (10489-884)
Supplier: Bioss
Description: The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM8 (tripartite motif containing 8), also known as GERP (glioblastoma-expressed RING finger protein) or RNF27 (RING finger protein 27), is a 551 amino acid protein that is thought to function as an E3 ubiquitin-protein ligase that promotes SOCS-1 proteasomal degradation. As a widely expressed homodimer, TRIM8 localizes to nuclear bodies and contains two B box-type zinc fingers and one RING-type zinc finger. TRIM8 is expressed in lung, heart, brain and skeletal muscle, with low levels detected in intestine, placenta, leukocytes and liver. The gene encoding TRIM8 maps to human chromosome 10q24.32.


Catalog Number: (10489-862)
Supplier: Bioss
Description: The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM8 (tripartite motif containing 8), also known as GERP (glioblastoma-expressed RING finger protein) or RNF27 (RING finger protein 27), is a 551 amino acid protein that is thought to function as an E3 ubiquitin-protein ligase that promotes SOCS-1 proteasomal degradation. As a widely expressed homodimer, TRIM8 localizes to nuclear bodies and contains two B box-type zinc fingers and one RING-type zinc finger. TRIM8 is expressed in lung, heart, brain and skeletal muscle, with low levels detected in intestine, placenta, leukocytes and liver. The gene encoding TRIM8 maps to human chromosome 10q24.32.


Supplier: Enzo Life Sciences
Description: α-Crystallins composed of αA (~19 kDa) and αB (~19.2 kDa) subunits, are major water-soluble proteins accounting for almost 50% of total protein in the mammalian transparent eye lens and they are also found in a variety of other tissues. Alpha-crystallins are also referred to as small heat shock proteins, since they are induced by increased temperature in a variety of organisms. The α-crystallins have sequence homology as well as structural and functional similarities with the small Hsp’s such as Hsp25/27. Most α-crystallins have four common structural and functional features: (i) molecular weight between 12 and 43kDa; (ii) the formation of large oligomeric complexes composed of αA-crystallin, αB-crystallin and Hsp25/27; (iii) the moderately conserved α-crystallin domain in the central region of the protein; and (iv) molecular chaperone activity. The α-crystallin domain comprises approximately 90 residues, is bounded by variable N-terminal and C-terminal extensions and is involved in oligomer assembly. Oligomers can reach 800 kDa or more and are dynamic, exhibiting subunit exchanges and organizational plasticity, possibly leading to functional diversity. Phosphorylation of serine residues occurs during development and in response to stress, and usually decreases oligomer size. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation. Although productive release and refolding of denatured proteins requires close cooperation with other chaperones. Other proposed functions include a role in membrane stabilization and modulation of intermediate filament organization during physiological stress and neurodegenerative disease. Alpha B Crystallin is phosphorylated on serine 45 by ERK1/2 and serine 59 by MAPKAPK-2. When mono-phosphoylated αB-crystallin is isolated it contains only αB-crystallin phosphorylated at serine 19.

Catalog Number: (10072-796)
Supplier: Prosci
Description: Relaxin-3 (H3 relaxin, Insulin-like peptide-7, INSL7) is a secreted protein structurally related to insulin, which is expressed primarily in the brain and central nervous system. Relaxin-3 has been identified as the ligand for the GPCR135 receptor, previously known as "somatostatin-like” or "angiotensin-like” peptide receptor, and also binds specifically to the LGR7 receptor, previously identified as an "orphan” G protein coupled receptor. Signaling by Relaxin-3 through its target receptors is, most likely, part of a CNS processing system, activated in response to signaling by neuropeptides and other factors. Intracerebroventricular injections of Relaxin-3 have been shown to cause a significant increase of food intake and body weight in Wistar rats. Recombinant Relaxin-3 is a 5.5 kDa disulfide linked heterodimeric protein consisting of a 24 amino acid A-chain and a 27 amino acid B-chain.


Catalog Number: (10073-062)
Supplier: Prosci
Description: GDF-5 is expressed in long bones during embryonic development and postnatally in articular cartilage. Mutations in the GDF-5 gene have been implicated in Grebe Syndrome, which is characterized by short stature, extra digits, short and deformed extremities, and in Hunter-Thompson type dwarfism. The mature and functional form of GDF-5 is a homodimer of two 120 amino-acid polypeptide chain (monomers) linked by a single disulfide bond. Each GDF-5 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 27 amino-acid signal peptide and a 348 amino-acid propeptide. This precursor undergoes intracellular dimerization, and upon secretion it is processed by a furin-type protease. Recombinant murine GDF-5 is a 27.0 kDa homodimeric disulfide-linked protein consisting of two 120 amino acids.


Catalog Number: (76108-856)
Supplier: Bioss
Description: Epstein-Barr virus-induced gene 3 (Ebi3) is a widely expressed homolog to the interleukin IL-12 p40 subunit protein that forms a heterodimer with either IL-12 p35 or an IL-12 p35 homolog, p28, to create a new cytokine (IL-27). Ebi3 may function to antagonize IL-12 and to inhibit the development of a Th1 immune response. Ebi3 is strongly expressed in Hodgkin and Reed-Sternberg cells, independently of the EBV status of the tumor cells. Ebi2 is expressed in B-lymphocytes and lymphoid tissues and may function in the modulation of the immune system. Out of the nine genes that are induced by the Epstein-Barr virus, Ebi2 exhibits the highest levels of up-regulation. In addition, Ebi2 may play a role mediating normal lymphocyte functions.


Catalog Number: (10813-820)
Supplier: Prosci
Description: Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, the specific type of polyubiquitin recognized upon cell stimulation (either 'Lys-63'-linked or linear polyubiquitin) and its functional importance is reported conflictingly. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination.


Supplier: Biotium
Description: This MAb recognizes TGF beta 1, 2 and 3. Three TGF betas have been identified in mammals. TGF beta 1, TGF beta 2 and TGF beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecules. Biologically active TGF beta requires dimerization of the monomers (usually homodimers) and release of the latent peptide portion. Overall, the mature region of the TGF beta 3 protein has approximately 80% identity to the mature region of both TGF beta 1 and TGF beta 2. However, the NH2 terminals or precursor regions of their molecules share only 27% sequence identity. TGF betas inhibit the growth of epithelial cells and stimulate the growth of mesenchymal cells.

Catalog Number: (10663-868)
Supplier: Bioss
Description: Epstein-Barr virus-induced gene 3 (Ebi3) is a widely expressed homolog to the interleukin IL-12 p40 subunit protein that forms a heterodimer with either IL-12 p35 or an IL-12 p35 homolog, p28, to create a new cytokine (IL-27). Ebi3 may function to antagonize IL-12 and to inhibit the development of a Th1 immune response. Ebi3 is strongly expressed in Hodgkin and Reed-Sternberg cells, independently of the EBV status of the tumor cells. Ebi2 is expressed in B-lymphocytes and lymphoid tissues and may function in the modulation of the immune system. Out of the nine genes that are induced by the Epstein-Barr virus, Ebi2 exhibits the highest levels of up-regulation. In addition, Ebi2 may play a role mediating normal lymphocyte functions.


Catalog Number: (10489-882)
Supplier: Bioss
Description: The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM8 (tripartite motif containing 8), also known as GERP (glioblastoma-expressed RING finger protein) or RNF27 (RING finger protein 27), is a 551 amino acid protein that is thought to function as an E3 ubiquitin-protein ligase that promotes SOCS-1 proteasomal degradation. As a widely expressed homodimer, TRIM8 localizes to nuclear bodies and contains two B box-type zinc fingers and one RING-type zinc finger. TRIM8 is expressed in lung, heart, brain and skeletal muscle, with low levels detected in intestine, placenta, leukocytes and liver. The gene encoding TRIM8 maps to human chromosome 10q24.32.


Catalog Number: (10489-876)
Supplier: Bioss
Description: The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM8 (tripartite motif containing 8), also known as GERP (glioblastoma-expressed RING finger protein) or RNF27 (RING finger protein 27), is a 551 amino acid protein that is thought to function as an E3 ubiquitin-protein ligase that promotes SOCS-1 proteasomal degradation. As a widely expressed homodimer, TRIM8 localizes to nuclear bodies and contains two B box-type zinc fingers and one RING-type zinc finger. TRIM8 is expressed in lung, heart, brain and skeletal muscle, with low levels detected in intestine, placenta, leukocytes and liver. The gene encoding TRIM8 maps to human chromosome 10q24.32.


Catalog Number: (10489-880)
Supplier: Bioss
Description: The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM8 (tripartite motif containing 8), also known as GERP (glioblastoma-expressed RING finger protein) or RNF27 (RING finger protein 27), is a 551 amino acid protein that is thought to function as an E3 ubiquitin-protein ligase that promotes SOCS-1 proteasomal degradation. As a widely expressed homodimer, TRIM8 localizes to nuclear bodies and contains two B box-type zinc fingers and one RING-type zinc finger. TRIM8 is expressed in lung, heart, brain and skeletal muscle, with low levels detected in intestine, placenta, leukocytes and liver. The gene encoding TRIM8 maps to human chromosome 10q24.32.


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