You searched for: Proteins and Peptides

Supplier: Adipogen

Interleukin-8 (IL-8) was originally discovered as a neutrophil chemotactic and activating factor and is a member of the alpha (CXC) subfamily of chemokines (including also platelet factor 4, GRO, IP-10, etc.). Many cell types, including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, keratinocytes, hepatocytes, chondrocytes and various tumor cell lines, produce IL-8 in response to a wide variety of proinflammatory stimuli such as exposure to IL-1, TNF, LPS and viruses. IL-8 has a wide range of other proinflammatory effects. It is a potent chemoattractant for neutrophils and causes degranulation of neutrophil specific granules and azurophilic granules. IL-8 induces expression of the cell adhesion molecules CD11/CD18 and enhances the adherence of neutrophils to endothelial cells and subendothelial matrix proteins. Besides neutrophils, IL-8 is also chemotactic for basophils, T cells and eosinophils. IL-8 has been reported to be a co-mitogen for keratinocytes and was also shown to be an autocrine growth factor for melanoma cells. IL-8 was also reported to be angiogenic both in vivo and in vitro.

Supplier: Adipogen

Interleukin-8 (IL-8) was originally discovered as a neutrophil chemotactic and activating factor and is a member of the alpha (CXC) subfamily of chemokines (including also platelet factor 4, GRO, IP-10, etc.). Many cell types, including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, keratinocytes, hepatocytes, chondrocytes and various tumor cell lines, produce IL-8 in response to a wide variety of proinflammatory stimuli such as exposure to IL-1, TNF, LPS and viruses. IL-8 has a wide range of other proinflammatory effects. It is a potent chemoattractant for neutrophils and causes degranulation of neutrophil specific granules and azurophilic granules. IL-8 induces expression of the cell adhesion molecules CD11/CD18 and enhances the adherence of neutrophils to endothelial cells and subendothelial matrix proteins. Besides neutrophils, IL-8 is also chemotactic for basophils, T cells and eosinophils. IL-8 has been reported to be a co-mitogen for keratinocytes and was also shown to be an autocrine growth factor for melanoma cells. IL-8 was also reported to be angiogenic both in vivo and in vitro.

Supplier: STEMCELL Technologies

Vascular endothelial growth factor C (VEGF-C) is a member of the VEGF/platelet-derived growth factor (PDGF) family of proteins. VEGF-C is a potent angiogenic factor and promotes lymphangiogenesis, endothelial cell growth and survival, and can affect blood vessel permeability. VEGF-C is expressed in a range of tissues, but is not expressed in peripheral blood lymphocytes. VEGF-C forms a non-covalent, cell surface-associated, disulfide-linked homodimer that can bind and activate VEGF receptors 2 (VEGFR-2 [Flk1]) and 3 (VEGFR-3 [Flt4]). Interaction with VEGFR-2 results in physiological and intratumoral neoangiogenesis and vessel sprouting (Cao et al.; Tammela et al.), whereas interaction with VEGFR-3 is critical for lymphangiogenesis (Karkkainen et al.; Laakkonen et al.; Mäkinen et al.). Overexpression of VEGF-C in tumor cells has been shown to result in enhanced lymph flow and increased metastasis to regional lymph nodes (Hoshida et al.; Mandriota et al.; Padera et al.; Skobe et al.).

Supplier: STEMCELL Technologies

Vascular endothelial growth factor D (VEGF-D) is a member of the VEGF/platelet-derived growth factor (PDGF) family of proteins. VEGF-D is a potent angiogenic factor and promotes lymphangiogenesis, endothelial cell growth and survival, and can affect blood vessel permeability. VEGF-D is expressed in the lung, heart, small intestine, fetal lung, and at lower levels in the pancreas, colon, and skeletal muscle (Otrock et al.; Roy et al.; Stacker et al.; Yamada et al.). VEGF-D is a ligand for VEGF receptors 2 (Flk1) and 3 (Flt4) (Baldwin et al.). VEFGR-3 is highly expressed in lymphatic endothelial cells and is essential for their growth and differentiation (Otrock et al.; Roy et al.). Binding of VEGF-D to neuropilins contributes to VEGFR-3 signaling during lymphangiogenesis, whereas binding to integrin α9β1 promotes endothelial cell adhesion and migration (Roy et al.; Otrock et al.). During embryogenesis, VEGF-D also plays a role in the formation of the venous and lymphatic systems.

Supplier: STEMCELL Technologies

Persephin is a neurotrophic factor that belongs to the glial cell line-derived neurotrophic factor (GDNF) family. Persephin shares a large degree of structural similarity to GDNF, artemin, and neurturin, and has overall neuroprotective activity. Persephin signals through GRFα4 (glycosylphosphatidylinositol (GPI)-linked GDNF receptor family member) which signals through the receptor tyrosine kinase RET. Unlike GDNF and neurturin, persephin only promotes the growth and survival of central dopaminergic and motor neurons, but not peripheral neurons (Milbrandt et al.). in vitro, persephin only promotes survival of neurons that co-express GPI-linked GRFα4 and RET (Enokido et al.; Lindahl et al.). Mice lacking persephin showed increased cell death after cerebral ischemia, however administration of persephin before ischemia dramatically reduced neuronal cell death (Tomac et al.).

Supplier: STEMCELL Technologies

Fibroblast growth factor 7 (FGF-7) is a member of the FGF family, and acts exclusively through a subset of FGF receptor isoforms expressed predominantly by epithelial cells (Finch and Rubin). FGF-7 seems to act specifically on epithelial cells and stimulates proliferation, migration, and differentiation of these cells, and also participates in epithelial protection and repair both in vitro and in vivo (Finch and Rubin; Werner). In contrast, FGF-7 is produced solely by cells of mesenchymal origin, and functions as a paracrine mediator of mesenchymal-epithelial communication (Rubin et al.). FGF-7 has also been shown to supplement several wound-healing properties of bioengineered skin (Erdag et al.) and to induce autophagy in human keratinocytes (Belleudi et al.). Additionally, FGF-7 has a role in pluripotent stem cell differentiation to endodermal pancreatic-like insulin-producing cells and thymic epithelial cells (Inami et al.; Niu et al.).

Supplier: STEMCELL Technologies

Interleukin 3 (IL-3) is a species-specific pleiotropic cytokine that promotes the survival and proliferation of pluripotent hematopoietic stem cells and lineage-committed progenitor cells and their differentiation into mature cells of most lineages, including mast cells, basophils, neutrophils, eosinophils, macrophages, dendritic cells, erythrocytes, and megakaryocytes (Fung et al.; Metcalf et al.; Broughton et al.). IL-3 is produced by activated T cells, and has a physiological role in inflammation and allergies by promoting the secretion of inflammatory mediators such as histamine, IL-4, and IL-6 by mast cells, basophils and eosinophils. The mouse IL-3 receptor consists of a unique alpha-subunit (CD123) and two beta subunits, one specific for IL-3 (βIL-3), the other shared with the receptors for IL-5 and GM-CSF (beta common chain, βc or CD131). IL-3 binding to heterodimeric receptors containing the alpha subunit and one of either beta subunits activates JAK/STAT, MAPK, and PI3K signaling pathways (Scott and Begley).

Supplier: Adipogen

Interleukin-12 (IL-12), also known as Natural Killer Cell Stimulatory Factor (NKSF) or Cytotoxic Lymphocyte Maturation Factor (CLMF), is a heterodimeric pleiotropic cytokine made up of a 40 kDa (p40) subunit and a 35 kDa (p35) subunit. IL-12 is produced by macrophages and B lymphocytes and has been shown to have multiple effects on T cells and Natural Killer (NK) cells. Some of these IL-12 activities include the induction of IFN-gamma and TNF in resting and activated T and NK cells; the enhancement of cytotoxic activity of resting NK and T cells, the stimulation of resting T cell proliferation in the presence of a comitogen; and the enhancement of NK cell proliferation. Current evidence indicates that IL-12 is a key mediator of cellular immunity and induces the differentiation of Th1 cells from precursor T helper cells. Based on its activities, it has been suggested that IL-12 may have therapeutic potential as a vaccine adjuvant that promotes cellular immunity and as an antitumor and anti viral agent.

Supplier: STEMCELL Technologies

Interleukin 10 (IL-10) is the founding member of the IL-10 family of class II cytokines. All of the IL-10 cytokine family members have a four-helix bundle consisting of α-helical folds. Upon binding to its receptor, IL-10 activates signaling through JAK1 and STAT3. It is produced by dendritic cells, macrophages, and CD4 T cells, as well as mast cells, NK cells, neutrophils, and B cells, under specific stimulating conditions (Saraiva and O'Garra). IL-10 can inhibit the expression of pro-inflammatory cytokines and promote healing processes, and is important for the function of T regulatory cells. IL-10 also enhances B cell proliferation, immunoglobulin secretion, and class II MHC expression, while IL-10 produced by macrophages inhibits activation of neighboring macrophages, thus allowing a level of self-regulation (Ouyang et al.). This product is animal component-free.

Supplier: STEMCELL Technologies

Fibroblast growth factor acidic (FGF-acidic), also known as FGF-1, is a potent activator of DNA synthesis, cell proliferation, and chemotaxis and is known to play numerous roles in development, regeneration, and angiogenesis (Galzie et al.; Jaye et al.; Presta et al.). FGF-acidic is produced by multiple cell types and is capable of activating all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. It is found in large quantities in the brain, but is also expressed in hepatocytes, vascular smooth muscle cells, neurons of the central nervous system, skeletal muscle cells, fibroblasts, keratinocytes, endothelial cells, intestinal columnar epithelial cells, and pituitary basophils and acidophils. FGF-acidic is secreted as a disulfide-linked homodimer and is stored in complex with heparan sulfate, a requirement for its interaction with FGF receptors (Guerrini et al.; Mohammadi et al.). Internalized FGF-acidic signals via protein kinase C and promotes cell survival by inhibiting p53 and proapoptotic signaling (Bouleau et al.). This product is animal component-free.

Supplier: STEMCELL Technologies

Complement factor D is a component of the alternative pathway of the complement system and part of the innate immune system, playing a vital role in the initiation and amplification of complement activation, in order to defend against infection (Barratt and Weitz). A serine protease belonging to the S1 peptidase family, complement factor D is secreted by adipocytes into circulating blood, and is also expressed by macrophages and monocytes (White et al.). In the initiation phase of the complement pathway, complement factor D cleaves complement factor B (bound to component C3) to produce a complex known as C3 convertase. During the amplification phase, complement factor D cleaves complement factor B (bound to component C3b) to produce the C3bBb convertase, and is involved in the propagation of complement activation. In addition to its immunological role, complement factor D is involved in other physiological processes, such as the efficient clearing of damaged cell debris by phagocytes following acute liver injury (Cresci et al.). Complement factor D deficiency is associated with an increased susceptibility to pathogens like Neisseria meningitidis (Biesma et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, complement factor D from STEMCELL comes lyophilized with ≥94% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1.0 EU/μg protein.

Supplier: STEMCELL Technologies

Interleukin 6 receptor (IL-6R) alpha is a type I transmembrane glycoprotein that forms a complex with type I transmembrane signal transducer protein gp130 (CD130) and mediates the biological activities of IL-6. IL-6 binds to the membrane-bound non-signaling IL-6R alpha (mIL-6R), and the complex binds to two molecules of gp130 and leads to ‘classical’ IL-6-signal transduction, which includes activation of JAK/STAT, ERK, and PI3K signal transduction pathways (Scheller et al.). In contrast, a soluble form of IL-6R alpha (sIL-6R), which comprises the extracellular portion of the receptor, binds to the secreted IL-6 to form a complex that promotes bioavailability of IL-6. The complex of IL-6 and sIL-6R can bind to gp130 on cells that do not express the IL-6R and are unresponsive to IL-6. This process is known as trans-signaling (Hunter and Jones; Rose-John S). sIL-6R regulates both local and systemic IL-6-mediated events. Elevated levels of sIL-6R have been documented in several disease conditions such as rheumatoid arthritis, myeloma, and Crohn’s disease (Jones et al.; Mihara et al.).

Supplier: STEMCELL Technologies

Platelet-derived growth factor (PDGF) is a dimeric glycoprotein consisting of two disulfide bridge-stabilized polypeptide chains, A and B, which are assembled as heterodimers (PDGF-AB) or homodimers (PDGF-AA and PDGF-BB) (Fretto et al.; Westermark and Heldin). PDGF signals through the receptor tyrosine kinases PDGFRalpha and PDGFRbeta. It has been shown that PDGF-induced migration involves signaling pathways involving MEK/ERK, EGFR, Src, and PI3K/AKT (Kim et al.). PDGF is a potent mitogen for cells of mesenchymal origin- like fibroblasts, glial cells, and vascular smooth muscle cells. PDGF has been implicated in pathogenesis of atherosclerosis, glomerulonephritis, cancer, and in the contraction of vascular smooth muscle cells of rat aortic tissues (Fretto et al.; Sachinidis et al.). It has been shown that PDGF-AB together with 5-Azacytidine (Catalog #72012), induces the conversion of mature bone and fat cells into tissue-regenerative multipotent stem cells (Chandrakanthan et al.).

Supplier: STEMCELL Technologies

Use Interferon beta (IFN-β) to modulate the activity of genes that control dendritic cell activation, T cell survival, NK cell activation, chemokine expression, lymph node retention, and antiproliferative and antiviral effects (Dunn et al. Nat Rev Immunol, 2006). IFN-β binds to a receptor complex composed of IFNAR1 and IFNAR2, and initiates signal transduction via the JAK/STAT pathway. It is predominantly produced by fibroblasts, with smaller amounts from plasmocytoid dendritic cells. Macrophages and endothelial cells secrete IFN-β in response to viral infection (Reder and Feng. Front Immunol, 2013). IFN-β suppresses Th17 cells by affecting expression of IL-4, IL-10, and IL-27, and is a first-line treatment for multiple sclerosis. IFN-β was also shown to expand regulatory T cells and limit T cell trafficking to the central nervous system (Inoue and Shinohara. Immunology, 2013). Of the two IFN-β variants (IFN-β1 and IFN-β3), this product is the IFN-β1 form.

Supplier: STEMCELL Technologies

Interleukin 2 (IL-2) is a monomeric cytokine that was originally identified as a T cell growth factor (Gaffen and Liu). It binds to heterotrimeric receptors consisting of CD25, CD122, and CD132. Upon binding, it activates JAK3-, STAT5-, and AKT-dependent signaling pathways, which results in cellular proliferation and survival (Ma et al.). The majority of IL-2 is secreted by activated CD4+ and CD8+ T cells, although B cells and dendritic cells were found to produce IL-2 in small amounts. IL-2 downregulates immune responses to prevent autoimmunity during thymic development, influences the development of CD4+CD25+ regulatory T cells, and affects development of follicular helper T cells. IL-2 also controls inflammation by inhibiting Th17 differentiation (Banchereau et al.). High IL-2 levels in serum are associated with progression of scleroderma, rheumatoid arthritis, and gastric and non-small cell lung cancer, though no known disease can be directly attributed to the lack or excess of IL-2 (Gaffen and Liu).

Supplier: STEMCELL Technologies

Granulocyte colony-stimulating factor (G-CSF) is a member of the CSF family of glycoproteins that regulate hematopoietic cell proliferation, differentiation, and function. It is a key cytokine involved in the production of neutrophils and the stimulation of granulocyte colony formation from hematopoietic progenitor cells (Metcalf and Nicola). G-CSF causes a range of effects including a transient reduction of SDF-1 expression (Petit et al.), the activation of metalloproteases that cleave VCAM-1 (Levesque et al.), and the release of norepinephrine from the sympathetic nervous system (Katayama et al.), leading to the release or mobilization of hematopoietic stem cells from the bone marrow into the periphery. The G-CSF receptor is expressed on a variety of hematopoietic cells, including myeloid-committed progenitor cells, neutrophils, granulocytes, and monocytes. In addition to hematopoietic cells, G-CSF is also expressed in cardiomyocytes, neuronal cells, mesothelial cells, and endothelial cells. Binding of G-CSF to its receptor leads to activation of the JAK/STAT, MAPK, PI3K, and AKT signal transduction pathways. This product is animal component-free.

Supplier: Adipogen

IL-36alpha (IL-1F6), IL-36beta (IL-1F8) and IL-36gamma (IL-1F9) bind to IL-36R (IL-1Rrp2) and IL-1RAcP, activating similar intracellular signals as IL-1 and are inhibited by IL-36Ra. The expression of IL-36 cytokines has been shown to occur at different sites including the lung and skin and can be derived from diverse cell types including keratinocytes, bronchial epithelium as well as macrophages, monocytes and different T cell subsets. IL-36 family members induce the production of proinflammatory cytokines, including IL-12, IL-1beta, IL-6, TNF-alpha and IL-23 in BMDC and CD4 T cells, thus promoting neutrophil influx, dendritic cell (DC) activation, polarization of T helper type 1 (Th1) and IL-17-producing T cells (alphabeta T cells and gammadelta T cells) and keratinocyte proliferation. These cytokines may represent potential targets for immune-mediated inflammatory conditions or, alternatively, could be used as adjuvants in vaccination. IL-36gamma is also induced in the lung in various models of asthma and can be produced by bronchial epithelial cells in response to viral infection, smoke or inflammatory cytokines.

Supplier: STEMCELL Technologies

Betacellulin is a member of the epidermal growth factor (EGF) family, and signals through EGF receptor and ERBB4. It activates ERK and AKT pathways, which induces neural stem cell proliferation and prevents spontaneous differentiation in culture. Betacellulin stimulates the expansion of neural stem cells, transit-amplifying cells, and neuroblasts derived from subventricular zone and dentate gyrus (Gómez-Gaviro et al.). It is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Betacellulin down-regulates E-cadherin expression in ovarian cancer cell lines via MEK/ERK1/2 and PI3K/AKT signaling pathways, thus increasing cell migration (Zhao et al.). It is a modulator of interferon (IFN) response and enhances anti-viral effects of IFN (Al-Yahya et al.). Betacellulin is expressed in pancreatic α cells, β cells, and duct cells. It induces the proliferation of pancreatic cancer cell lines, inhibits apoptosis, promotes the neogenesis of β cells, and converts non-β cells into insulin-producing cells (Kawaguchi et al.; Miyagawa al.; Saito et al.).

Supplier: STEMCELL Technologies

Interleukin 31 (IL-31), a four-helix bundle inflammatory cytokine, belongs to the IL-6 cytokine family which includes IL-6 (MSPP-78050), oncostatin M (MSPP-78094), leukemia inhibitory factor (LIF; MSPP-78055), and cardiotrophin-1 (Dillon et al.). IL-31 signals through a heterodimer composed of IL-31RA (also known as gp130-like receptor or GPL) and the oncostatin-M receptor (OSMR), both of which are expressed on monocytes (Diveu et al.; Ghilardi et al.), epithelial cells (Ip et al.), and keratinocytes (Kato et al.). Signaling through the GPL/OSMR complex activates the JAK/STAT, RAS/ERK, and PI3K/AKT signaling pathways, resulting in the downstream activation of STAT1, STAT3, and STAT5 transcription factors (Cornelissen et al.; Dambacher et al.; Dillon et al.; Ip et al.). IL-31 responses have been associated with allergic responses and inflammatory skin diseases including atopic dermatitis (Cornelissen et al.; Gangemi et al.).

Supplier: STEMCELL Technologies

Leukemia inhibitory factor (LIF) is an interleukin 6 class cytokine that regulates a broad variety of developmental functions. After LIF binds to LIF receptor (LIFR), LIFR associates with gp130 and activates JAK/STAT and MAPK signaling (Auernhammer and Melmed; Suman et al.). LIFR activation of STAT3 is essential for maintaining the mouse embryonic stem cell phenotype (Niwa et al.). Produced by the endometrium, LIF plays an important autocrine and paracrine role in implantation by regulating proliferation, invasion, and differentiation of trophoblasts following blastocyst attachment (Auernhammer and Melmed; Suman et al.). Human LIF can be used for the maintenance of mouse embryonic stem cells, however mouse LIF cannot bind to the human receptor, thus rendering mouse LIF inactive (Dahéron et al.). LIF is produced by CD4+ and activated regulatory T cells, and promotes Foxp3 expression, while repressing Th17 lineage-specific genes (Metcalfe). LIF is also secreted by mesenchymal stromal cells, where it supports hematopoiesis and immune modulation (Nasef et al.).

Supplier: STEMCELL Technologies

Interferon-gamma (IFN-γ), also known as type II interferon, is produced by T and NK cells, and in smaller amounts by dendritic cells and macrophages. IFN-γ is controlled by cytokines such as IL-12 and IL-18 secreted in response to infection (Schroder et al.). IFN-γ binds to a receptor complex and initiates signal transduction via the JAK/STAT pathway; this culminates in the transcription and activation of many genes that control a diverse array of immunological functions (de Weerd and Nguyen; Krause et al.). IFN-γ stimulates the antimicrobial and anti-tumor activity of macrophages, NK cells, and neutrophils (Billiau and Matthys) by promoting the activation of microbial effector functions such as production of reactive oxygen species, NO intermediates, and complement (Schroder et al.). IFN-γ enhances MHC class I and II expression in dendritic cells and mononuclear phagocytes, as well as the production of IL-12 by dendritic cells. In B cells, IFN-γ stimulates survival and growth in both mouse and human cells, and redirects B cells from proliferation towards differentiation. IFN-γ favors the development of Th1 vs Th2 cells and stimulates monocyte differentiation and function (Schroder et al.). This product is animal component-free.

Supplier: STEMCELL Technologies

Interleukin 11 (IL-11) is a pleiotropic cytokine with effects on various tissues including the bone marrow, brain, and intestinal mucosa (Du and amp; Williams). It belongs to the IL-6 family of cytokines that share a common signal transducer, gp130. Culture of mouse bone marrow cells with IL-11 in combination with IL-3, IL-6, and stem cell factor induces significant expansion and proliferation of colony-forming cells in vitro (Peters et al.). In addition, in combination with IL-3, IL-11 significantly enhances the growth of megakaryocytic colonies in vitro, suggesting its role in augmenting mouse megakaryopoiesis (Yonemura et al.). IL-11 is expressed in a wide range of normal adult mouse tissues, including the central nervous system, thymus, lung, and bone. The mouse IL-11 cDNA was cloned using an expression library generated from the lipopolysaccharide-induced mouse fetal thymic cell line, T2 (Morris et al.). The binding of IL-11 to its receptor induces heterodimerization with the gp130 subunit and activation of JAK tyrosine kinases. IL-11 also plays a role in cancer progression by inducing the proliferation of epithelial cancer cells and the survival of metastatic cells at distant organs. Recently, IL-11 has gained interest for its role in the pathogenesis of diseases in dysregulated mucosal homeostasis associated with STAT3 upregulation, including gastrointestinal cancers (Putoczki et al.).

Supplier: STEMCELL Technologies

Stem cell factor (SCF) is an early-acting cytokine that plays a pivotal role in the regulation of embryonic and adult hematopoiesis. SCF promotes cell survival, proliferation, differentiation, adhesion, and functional activation of cells at multiple levels of the hematopoietic hierarchy. Together with other cytokines such as thrombopoietin and Flt3/Flk-2 Ligand, SCF is commonly used to promote expansion of primitive hematopoietic stem cells and multi-potent progenitor cells in culture (Huang et al.; Kent et al.). In synergy with various growth factors, including IL-2, IL-3, IL-6, IL-7, G-CSF, and erythropoietin, SCF increases proliferation and differentiation of myeloid and erythroid progenitor cells and a subset of lymphoid progenitor cells (Broudy). In the mouse, SCF is essential during fetal gonadal development (Mauduit). It is produced by stromal cells in the fetal liver, bone marrow, and thymus, in the central nervous system, in keratinocytes, and in the gut mucosa, and can function as a chemotactic and chemokinetic factor. SCF exists in two biologically active splice forms: a soluble and a transmembrane isoform. Upon binding to its receptor (c-kit tyrosine kinase receptor; CD117), it activates PI3K, JAK/STAT, and MAPK pathways. SCF and signaling from c-kit has also been reported to play an important role in pigmentation, fertility, vasculogenesis, motility of the gut via c-kit-positive interstitial cells of Cajal, and in the migration of neuronal stem and progenitor cells to sites of injury in the brain (Lennartsson and Ronnstrand).

Supplier: New England Biolabs (NEB)

NEBExpress GamS nuclease inhibitor is a recombinant protein that inhibits Exonuclease V (RecBCD) activity and stabilizes linear DNA templates in E. coli based in vitro protein synthesis reactions.

Supplier: Abnova

Human DPYSL2 full-length ORF recombinant protein with GST-tag at N-terminal.