1mg

Fibroblast Growth Factor 8a (FGF-8a) is a cytokine belonging to the heparin-binding FGF family, which has at least 23 members. FGF-8 has 8 different isoforms, named FGF-8a through FGF-8h. Different FGF-8 isoforms have different affinities to the receptors, and thus participate in different signaling cascade pathways. FGF-8 has very widespread expression during embryonic development, and is an organizer and inducer for gastrulation, somitogenesis, morphogenesis, and limb induction. However, FGF-8 is also a potential oncogene: in normal adult cells, FGF-8 has very low expression, but FGF-8 is highly expressed in cancer cells of breast, prostate, and ovarian tumors. FGF-8 promotes tumor angiogenesis by increasing neovascularization, and induces osteoblastic differentiation.

Fibroblast Growth Factor 8e (FGF-8e) is a cytokine belonging to the heparin-binding FGF family, which has at least 23 members. FGF-8 has 8 different isoforms, named FGF-8a through FGF-8h. Different FGF-8 isoforms have different receptor affinities, and thus participate in different signaling cascade pathways. FGF-8 has widespread expression during embryonic development, promoting gastrulation, somitogenesis, morphogenesis, and limb formation. FGF-8 also has oncogenic potential. While in normal cells FGF-8 is expressed at very low levels, in breast, prostate and ovarian cancer FGF-8 is highly expressed.FGF-8 promotes tumor angiogenesis by increasing neovascularization, and inducing osteoblastic differentiation.

Fibroblast Growth Factor-9 (FGF-9) is a heparin binding growth factor that belongs to the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-9 was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development.

Fibroblast growth factor-9 (FGF-9) is an approximately 26 kDa secreted glycoprotein of the FGF family. Secreted mouse FGF-9 lacks the N-terminal 1-3 aa and shares >98% sequence identity with rat, human, equine, porcine and bovine FGF-9. FGF-9 plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. In the mouse embryo, the location and timing of FGF-9 expression affect the development of the skeleton, cerebellum, lungs, heart, vasculature, digestive tract, and testes. It may have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors. Deletion of mouse FGF-9 is lethal at birth due to lung hypoplasia, and causes rhizomelia, or shortening of the proximal skeleton. An unusual constitutive dimerization of FGF 9 buries receptor interaction sites which lower its activity and increases heparin affinity which inhibits diffusion. A spontaneous mouse mutant, Eks, interferes with dimerization, resulting in monomeric, diffusible FGF-9 that causes elbow and knee synostoses (joint fusions) due to FGF-9 misexpression in developing joints.

Fibroblast Growth Factor- acidic (FGF-acidic), also known as FGF-1 and endothelial cell growth factor, is a member of the FGF family which currently contain 23 members. FGF acidic and basic, unlike the other members of the family, lack signal peptides and are apparently secreted by mechanisms other than the classical protein secretion pathway. FGF acidic has been detected in large amounts in the brain. Other cells known to express FGF acidic include hepatocytes, vascular smooth muscle cells, CNS neurons, skeletal muscle cells, fibroblasts, keratinocytes, endothelial cells, intestinal columnar epithelium cells and pituitary basophils and acidophils. As with other FGF’s, FGF acidic exhibits considerable species cross reactivity. FGF acidic and FGF basic stimulate the proliferation of all cells of mesodermal origin, and many cells of neuroectodermal, ectodermal and endodermal origin.

Fibroblast Growth Factor- acidic (FGF-acidic) is a mitogen targeting at the endothelial cells, and belongs to the heparin binding FGF family, which contains 22 members. FGF-acidic binds to the receptor family FGFR1-4 in vivo with the assistance of heparin. However, along with FGF -basic, FGF-acidic lacks the signal peptide segment, and thus is not secreted via endoplasmic reticulum (ER) and Golgi bodies. Studies have shown that FGF-acidic is highly regulated, and it is a direct angiogenesis factor. If unregulated, angiogenesis could contribute to several diseases including arthritis, diabetes, ocular neovascularization, and especially tumors. Therefore, FGF-acidic is treated as a potential oncogene, and its overexpression is correlated tightly with several cancers.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, bFGF has the β trefoil structure. In vivo, bFGF is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. bFGF regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. bFGF can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of bFGF can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as HBGF-2, is a non-glycosylated heparin-binding growth factor that belongs to the FGF family. FGF-basic is present in basement membranes and in the subendothelial extracellular matrix of blood vessels. FGF-basic signals through FGFR1, 2, 3 and 4 that plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomyocytes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast growth factor receptor 2 (FGFR2) also known as CD332 is a receptor for fibroblast growth factor and it has important roles in embryonic development and tissue repair, especially bone and blood vessels. FGFR2 has two naturally occurring isoforms, FGFR2IIIb and FGFR2IIIc, created by splicing of the third immunoglobulin-like domain. FGFR2IIIb is predominantly found in ectoderm derived tissues and endothelial organ lining. Like the other members of the fibroblast growth factor receptor family, these receptors signal by binding to their ligand and dimerisation (pairing of receptors), which causes the tyrosine kinase domains to initiate a cascade of intracellular signals. On a molecular level these signals mediate cell division, growth and differentiation.

Fibroblast growth factor receptor 3(FGFR3) also known as CD333 (cluster of differentiation 333) is a member of the fibroblast growth factor receptor family, where amino acid sequence is highly conserved between members and throughout evolution. The FGFR3 gene produces various forms of the FGFR3 protein and the location varies depending on the isoform of the FGFR3 protein. Since the different forms are found within different tissues, the protein is responsible for multiple growth factor interactions. Gain of function mutations in FGFR3 inhibits chondrocyte proliferation and underlies achondroplasia and hypochondroplasia.

Fibroblast growth factor receptor 4(FGFR4) also known as CD334 (cluster of differentiation 334) is a member of the fibroblast growth factor receptor family, where amino acid sequence is highly conserved between members and throughout evolution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation.

FGL1 (Fibrinogen-like protein 1), also known as hepatocyte-derived fibrinogen-related protein 1 (HFREP-1), HP-041, hepassocin (HPS), and liver fibrinogen-related protein 1 (LFIRE-1), is a liver-specific secreted protein belonging to the fibrinogen superfamily whose members share a fibrinogen domain at their C-termini. FGL1 is an immune suppressive molecule that inhibits the activation of antigen-specific T cells by acting as a major ligand of LAG3, and binds LAG3 independently of MHC class II.

Protein L is a cell surface protein from Peptostreptoccocus magnus that binds to the variable light chains (kappa chain) of immunoglobulins without interfering with antigen binding. In contrast to IgG-binding proteins, such as protein A and protein G, which bind to the Fc region of immunoglobulins, protein L can be used for the detection and purification of mammalian kappa light chain antibodies of all classes. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than Protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (scFv) and Fab fragments also bind to Protein L.

Fms-related tyrosine kinase 3 ligand (Flt3L) is growth fator stimulates the proliferation and differentiation of hematopoietic multipotent progenitors and promotes proliferation of NK cells and dendritic cell subgroups by combination with other growth factors. Flt3L is produced by T cells and stromal fibroblasts, and targeted various cells including hematopoietic stem cells, B cells, T cells, dendritic cells, and NK cells. Flt3L binds to it cognate tyrosine kinase receptor Flt3 and activates JAK/STAT signaling pathway.Flt3L is a hematopoietic four helical bundle cytokine with structurally homologous to stem cell factor (SCF) and colony stimulating facor 1 (CSF-1) demonstrated four conserved cysteines and two glycosylation sites. Flt3L naturally as a non-disulfide-linked homodimer with multiple isoforms. The extracellular portion is approximately 160 amino acid residues in length and the cytoplasmic segment is approximately 20-30 amino acid residues in length.

Fractalkine, also named neurotactin, is a novel chemokine recently identified through bioinformatics. Fractalkine has a unique C-X3-C cysteine motif near the amino-terminus and is the first member of a fourth branch of the chemokine superfamily. Unlike other known chemokines, fractalkine is a type 1 membrane protein containing a chemokine domain tethered on a long mucin-like stalk. Human fractalkine cDNA encodes a 397 amino acid (aa) residue membrane protein with a 24 aa residue predicted signal peptide, a 76 aa residue chemokine domain, a 241 aa residue stalk region containing 17 degenerate mucin-like repeats, a 19 aa residue transmembrane segment and a 37 aa residue cytoplasmic domain. The extracellular domain of human fractalkine can be released, possibly by proteolysis at the dibasic cleavage site proximal to the membrane, to generate soluble fractalkine. The soluble chemokine domain of human fractalkine was reported to be chemotactic for T cells and monocytes while the soluble chemokine domain of mouse fractalkine was reported to chemoattract neutrophils and T-lymphocytes but not monocytes.

Chemokine (C-X3-C motif) ligand 1 (CX3CL1) is a known member of the CX3C chemokine family. It is also commonly known under the names fractalkine (in humans) and neurotactin (in mice). The polypeptide structure of CXC3L1 differs from the typical structure of other chemokines. For example, the spacing of the characteristic N-terminal cysteines is different; there are three amino acids separating the initial pair of cysteines in CX3CL1, while there are none in CC chemokines and only one in CXC chemokines. CX3CL1 is produced as a long protein (with 373-amino acid in humans) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk allows it to bind to the surface of certain cells. Soluble CX3CL1 potently chemoattracts T cells and monocytes, while the cell-bound chemokine promotes strong adhesion of leukocytes to activated endothelial cells, where it is primarily expressed. CX3CL1 can signal through the chemokine receptor CX3CR1.

Granulocyte Colony-Stimulating Factor (G-CSF) contains internal disulfide bonds. Among the family of colony-stimulating factors, Granulocyte Colony Stimulating Factor (G-CSF) is the most potent inducer of terminal differentiation to granulocytes and macrophages of leukemic myeloid cell lines. The synthesis of Granulocyte Colony Stimulating Factor (G-CSF) can be induced by bacterial endotoxins, TNF, Interleukin-1 and GM-CSF. Prostaglandin E2 inhibits the synthesis of Granulocyte Colony Stimulating Factor (G-CSF). In epithelial, endothelial, and fibroblastic cells secretion of Granulocyte Colony Stimulating Factor (G-CSF) is induced by Interleukin-17.

Human Granulocyte Colony Stimulating Factor (G-CSF) contains internal disulfide bonds. Among the family of colony-stimulating factors, Granulocyte Colony Stimulating Factor (G-CSF) is the most potent inducer of terminal differentiation to granulocytes and macrophages of leukemic myeloid cell lines. The synthesis of Granulocyte Colony Stimulating Factor (G-CSF) can be induced by bacterial endotoxins, TNF, Interleukin-1 and GM-CSF. Prostaglandin E2 inhibits the synthesis of Granulocyte Colony Stimulating Factor (G-CSF). In epithelial, endothelial, and fibroblastic cells, the secretion of Granulocyte Colony Stimulating Factor (G-CSF) is induced by Interleukin-17.

Granulocyte Colony-Stimulating Factor (G-CSF), also known as CSF-3 and MGI-1G, is a cytokine and hormone belonging to the IL-6 superfamily. It is expressed by monocytes, macrophages, endothelial cells, fibroblasts and bone marrow stroma. G-CSF stimulates the bone marrow to produce granulocytes and stem cells, and specifically stimulates the proliferation and differentiation of the neutrophilic granulocyte lineage. G-CSF has been used to stimulate white blood cell production after chemotherapy. It has also been used to boost the number of hematopoietic stem cells after bone marrow transplantation.

gAcrp30 is the globular head domain of Adipocyte complement-related protein of 30 kDa (Acrp30), a cytokine expressed in adipocytes. The name of Acrp30 is bases on its closest homolog, complement factor c1q, and the globular domain of Acrp30 has an unexpected homology with the Tumor Necrosis Factor (TNF) family of cytokines. Acrp30 is recognized by two receptors: adipoR1 expressed in skeletal muscle, and adipoR2 expressed in liver. The expression level of Acrp30 in adipocytes is negatively correlated with body weight and is lower in obese mouse than normal mouse. The globular domain of Acrp30 induces free fatty acid oxidation in muscle and weight reduction in mouse, suggesting its potential use as a pharmacological agent in obesity.

Galectin-9 is a cytoplasmic protein that contains two galectin domains. Galectin-9 is an S-type lectin that is over-expressed in Hodgkin’s disease tissue. Galectin-9 binds galactosides and has high affinity for the Forssman pentasaccharide. Galectin-9 plays a role in thymocyte-epithelial interactions relevant to the biology of the thymus and Inhibits cell proliferation. Galectin-9 is a ligand for HAVCR2/TIM3 and induces T-helper type 1 lymphocyte (Th1) death. In addition, Galectin-9 suppresses tumor cell metastasis by interfering with the associations CD44, VCAM-1, Integrin α4β1.

Glial cell line-derived neurotrophic factor (GDNF) is a neurotrophic factor belonging to the TGF-beta super family and is necessary for neuron survival and phenotypic maintenance in the central and peripheral nervous systems. G-DNF has the potential to support the differentiation and survival of many neuron subpopulations, especially dopaminergic neurons and motor neurons, as well as Purkinje cells and sympathetic neurons. Sertoli cells, type 1 astrocytes, Schwann cells, neurons, pinealocytes and skeletal muscle cells are known to express GDNF in human. GDNF has been shown to interact with GFRA2 and GDNF family receptor alpha 1. Mutations in this gene may be associated with Hirschsprung’s disease, Parkinson’s disease and amyotrophic lateral sclerosis (ALS).The recombinant human G-DNF expressed in E.coli is a disulfide-linked homo-dimer, with an apparent molecular weight of 17 kDa.

The
clustered regularly interspaced short palindromic repeats, known as CRISPR  systems are adaptive immune mechanisms commonly
present in archaea and bacteria. The CRISPR systems enable the host to specifically
target and cleave foreign nucleic acids thus targeting infectiousviruses and
plasmids. Recently, a type V CRISPR system has been identified in several
bacteria, the Cpf1 CRISPR from Prevotella and Francisella 1. In contrast to
Cas9 systems, CRISPR/Cpf1 systems are smaller in size, do not require an
additional trans-activating crRNA (tracrRNA), and allow for targeting of
additional genomic regions by cleaveing the target DNA proceeded by a short
T-rich protospacer-adjacent motif (PAM). On the other hand, the Cas9 system requires
a G-rich PAM following the target DNA. Furthermore, Cas12a/Cpf1 introduces a
staggered DNA double stranded break with a 4 or 5-nt 5’ overhang. Recombinant
Acidaminococcus sp. BV3L6 Cas12a (cpf1) nuclease is expressed in E. coli and
purified. The nuclease contains nuclear localization sequence (NLS) at the
C-terminus and 6× His-tag at the C-terminus.

GenCRISPR Cas13a (C2c2) Nuclease is an RNA-guided, RNA-targeting CRISPR enzyme, commonly referred to as C2c2. This enzyme is a member of Type VI CRISPR family containing a single protein effector with two HEPN domains. The Cas13a exhibits two RNase activities. The first activity, a cis- sequence-specific RNA guided cleavage, activates the secondary RNase activity of the enzyme, a non-specific trans- ribonuclease activity. This Cas13a protein can be applied to detect single RNA molecules with proven high specificity.

The GenCRISPR™
Cas9 v1.1 can be formed
with the guide RNA into a ribonucleoprotien (RNP) complex. The use of an RNP
complex to perform gene editing has been shown to reduce the challenges
encountered with other CRISPR gene editing techniques such as viral and plasmid
delivery. Challenges include off-target effects, cell viability and transcription/translational
challenges.

GenCRISPR™
Cas9 v1.1 is a tag free nuclease produced by expression in an E. coli strain carrying a plasmid
encoding the Cas9 gene from Streptococcus
pyogenes with a biparticle nucleus localization signal (BPNLS) at both
N-terminal and C-terminal. It has been reported that BPNLS is able to improve
the gene editing efficiency.

The GenCRISPR™
Cas9 v1.2 can be formed
with the guide RNA into a ribonucleoprotien (RNP) complex. The use of an RNP
complex to perform gene editing has been shown to reduce the challenges
encountered with other CRISPR gene editing techniques such as viral and plasmid
delivery. Challenges include off-target effects, cell viability and transcription/translational
challenges.

GenCRISPR™ Cas9 v1.2 is a tag
free nuclease produced by expression in an E.
coli strain carrying a plasmid encoding the Cas9 gene from Streptococcus pyogenes with a biparticle
nucleus localization signal (BPNLS) at N-terminal and a nucleoplasmin nucleus
localization signal (nucleoplasmin NLS) at C-terminal. It has been reported
that BPNLS and nucleoplasmin NLS are able to improve the gene editing
efficiency. 

GenCRISPR™ ErCas12a Nuclease is an RNA-guided DNA endonuclease from Eubacterium rectale. It recognizes a T-rich protospacer adjacent motif (PAM) and results in a staggered DNA double-strand break (DSB). After the specific cleavage, Cas12a can also activate collateral cleavage activity towards adjacent non-specific ssDNA sequences. Hence, Cas12a nuclease is a good alternative for Cas9 in certain target DNA editing, and provides a novel strategy for DNA detection.

GenCRISPR™ LbuCas13a Nuclease is an RNA-guided, RNA-targeting CRISPR enzyme, commonly referred to as LbuC2c2. This Cas13a protein can be applied to detect single RNA molecules with proven high specificity. Recently, Cas13a has been leveraged as a diagnostic nucleic acid detection tool.

The GenCRISPR™
SaCas9 2NLS Nuclease can be formed with the guide RNA into a ribonucleoprotien
(RNP) complex. The use of an RNP complex to perform gene editing has been shown
to reduce the challenges encountered with other CRISPR gene editing techniques
such as viral and plasmid delivery. Challenges include off-target effects, cell
viability and transcription/translational challenges. The SaCas9 recognizes an
NNGRRT protospacer adjacent motif (PAM) and cleaves target DNA at high
efficiency with a variety of guide RNA (gRNA) spacer lengths.

GenCRISPR™ SaCas9 2NLS
Nuclease is a tag free nuclease produced by expression in an E. coli strain carrying a plasmid
encoding the Cas9 gene from Staphylococcus
aureus with a nuclear localization signal at both N-terminal and C-terminal.The
small size of the nuclease facilitates enhanced in vivo delivery for genome
editing in various organisms.

GenCRISPR™ Ultra eSpCas9-2NLS-basic GMP is utilized for CRISPR gene editing applications. The Cas9 nuclease forms a stable ribonucleoprotein (RNP) complex with the guide RNA (gRNA) component. With the help of two nuclear localization signals (NLS) expressed with the Cas9 nuclease, the RNP complex enters the nucleus and cleaves target gene. When compared with a plasmid-based delivery system, the RNP delivery system has been observed to increase the on-target gene editing efficiency and decrease off-target effects.

The GenCRISPR™
Ultra eSpCas9 product line provides customers with a selection of research use,
basic GMP and GMP compliant Cas9 nucleases. The Cas9 protein can be formed with
the guide RNA into a ribonucleoprotien (RNP) complex. The use of an RNP complex
to perform gene editing has been shown to reduce the challenges encountered
with other CRISPR gene editing techniques such as viral and plasmid delivery.
Challenges include off-target effects, cell viability and transcription/translational
challenges.

GenCRISPR™
Ultra eSpCas9-2NLS is a mutant form of Cas9 nuclease and is produced by
expression in an E. coli strain
carrying a plasmid encoding the eSpCas9 gene from Streptococcus pyogenes with double-ended nuclear localization
signal (NLS). GenCRISPR™ Ultra eSpCas9-2NLS delivers higher fidelity and less
off-target activity than wild-type SpCas9 nuclease.

The GenCRISPR™
Ultra eSpCas9 product line provides customers with a selection of research use,
basic GMP and GMP compliant Cas9 nucleases. The Cas9 protein can be formed with
the guide RNA into a ribonucleoprotien (RNP) complex. The use of an RNP complex
to perform gene editing has been shown to reduce the challenges encountered
with other CRISPR gene editing techniques such as viral and plasmid delivery.
Challenges include off-target effects, cell viability and transcription/translational
challenges.

GenCRISPR™ Ultra eSpCas9-N-NLS
Research, tag-free is a mutant form of Cas9
nuclease and is produced by expression in an E. coli strain carrying a plasmid encoding the eSpCas9 gene from Streptococcus pyogenes with an N-terminal
nuclear localization signal (N-NLS). GenCRISPR™ Ultra eSpCas9-N-NLS Research,
tag-free delivers higher fidelity
and less off-target activity than wild-type SpCas9 nuclease.

GenCRISPR™ Ultra NLS-Cas9-basic GMP is utilized for CRISPR gene editing applications. The Cas9 nuclease forms a stable ribonucleoprotein (RNP) complex with the guide RNA (gRNA) component. With the help of nuclear localization signal (NLS) expressed with the Cas9 nuclease, the RNP complex enters the nucleus and cleaves the target gene. When compared with a plasmid-based delivery system, the RNP delivery system has been observed to increase the on-target gene editing efficiency and decrease off-target effects.

The
GenCRISPR™ Ultra Cas9 product line provides customers with a selection of
research use, GMP preclinical and GMP compliant Cas9 nucleases. The Cas9
protein can be formed with the guide RNA into a ribonucleoprotien (RNP)
complex. The use of an RNP complex to perform gene editing has been shown to
reduce the challenges encountered with other CRISPR gene editing techniques
such as viral and plasmid delivery. Challenges include off-target effects, cell
viability and trascprition/translational challenges.

GenCRISPR™ Ultra Cas9 is
produced by expression in an E. coli
strain carrying a plasmid encoding the Cas9 gene from Streptococcus pyogenes with an N-terminal nuclear localization
signal (NLS).

Growth Hormone (GH) is a member of the somatotropin/prolactin family which play an important role in growth control. The human GH cDNA encodes a 217 amino acid (aa), and the first 26 aa is a signal peptide. By alternative splicing, at least four isoforms of GH have been identified. The major role of GH in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. GH stimulates both the differentiation and proliferation of myoblasts, and also stimulates amino acid uptake and protein synthesis in muscle and other tissues.

Growth Hormone (GH) is a member of the somatotropin/prolactin family which play an important role in growth control. The human GH cDNA encodes a 217 amino acid (aa), and the first 26 aa is a signal peptide. By alternative splicing, at least four isoforms of GH have been identified. The major role of GH in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. GH stimulates both the differentiation and proliferation of myoblasts, and also stimulates amino acid uptake and protein synthesis in muscle and other tissues.

Growth Hormone (GH), is a member of the somatotropin / prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

GITR Ligand, also known as TNFSF18 and TL6, is an approximately 30 kDa type II transmembrane glycoprotein in the TNF superfamily (1). Human GITR Ligand consists of a 50 amino acid cytoplasmic domain, a 21 aa transsmembrane segment, and a 128 aa extracellular domain (ECD). Within the ECD, human GITR Ligand shares 56% and 60% aa sequence identity with mouse and rat GITR Ligand, respectively. TNFSF18 is expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells. GITRL/TNFSF18 is up-regulated after stimulation by bacterial lipopolysaccharides (LPS). TNFSF18 Can function as costimulator and lower the threshold for T-cell activation and T-cell proliferation. TNFSF18 / GITR Ligand is important for interactions between activated T-lymphocytes and endothelial cells.Recombinant Human GITR Ligand Fc Chimera produced in HEK293 cells is a polypeptide chain containing 359 amino acids with the C-termimal human IgG1 Fc fragment. A fully biologically active molecule, rhGITRL has a molecular mass of 50 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.

Glutathione S-Transferase (GST), an antioxidant enzyme, is involved in the primary cellular defense mechanism against reactive oxygen species. GST is soluble in water and has a mass of 26.98 kDa. It occurs as a dimer in all aerobic organisms.

Glycerolkinase

Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is produced by a number of different cell types, including activated T cells, B cells, macrophages, mast cells, endothelial cells, and fibroblasts, in response to cytokine of immune and inflammatory stimuli. Besides granulocyte-macrophage progenitors, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is a growth factor for erythroid, megakaryocyte, and eosinophil progenitors. On mature hematopoietic, monocytes/macrophages and eosinophils. Human Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) can induce human endothelial cells to migrate and proliferate. Additionally, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma, and adenocarcinoma cell lines.

Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is produced by a number of different cell types, including activated T cells, B cells, macrophages, mast cells, endothelial cells, and fibroblasts, in response to cytokine of immune and inflammatory stimuli. Besides granulocyte-macrophage progenitors, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is a growth factor for erythroid, megakaryocyte, and eosinophil progenitors. On mature hematopoietic, monocytes/macrophages and eosinophils. Human Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) can induce human endothelial cells to migrate and proliferate. Additionally, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma, and adenocarcinoma cell lines.

Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is produced by a number of different cell types, including activated T cells, B cells, macrophages, mast cells, endothelial cells, and fibroblasts, in response to cytokine of immune and inflammatory stimuli. Besides granulocyte-macrophage progenitors, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is a growth factor for erythroid, megakaryocyte, and eosinophil progenitors. On mature hematopoietic, monocytes/macrophages and eosinophils. Human Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) can induce human endothelial cells to migrate and proliferate. Additionally, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma, and adenocarcinoma cell lines.

Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is produced by a number of different cell types, including activated T cells, B cells, macrophages, mast cells, endothelial cells, and fibroblasts, in response to cytokine of immune and inflammatory stimuli. Besides granulocyte-macrophage progenitors, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is a growth factor for erythroid, megakaryocyte, and eosinophil progenitors. On mature hematopoietic, monocytes/macrophages and eosinophils. Human Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) can induce human endothelial cells to migrate and proliferate. Additionally, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma, and adenocarcinoma cell lines.

Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is produced by a number of different cell types, including activated T cells, B cells, macrophages, mast cells, endothelial cells, and fibroblasts, in response to cytokine of immune and inflammatory stimuli. Besides granulocyte-macrophage progenitors, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is a growth factor for erythroid, megakaryocyte, and eosinophil progenitors. On mature hematopoietic, monocytes/macrophages and eosinophils. Additionally, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma, and adenocarcinoma cell lines.