1mg

Molecular Formula : C27 D7 H28 N3 O6

Molecular Formula : C22H22BrNO2

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.

Molecular Formula : C9H9D6NO

Molecular Formula : C9 2H10 H7 N O2

Molecular Formula : C9 D4 H13 N O2

Molecular Formula : C9 H11 D6 N O2 . H Cl

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.

Molecular Formula : C6 H13 N O7 S

Molecular Formula : C18 H20 D6 O

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.

Molecular Formula : C15H14O7 (C2H6O)

Molecular Formula : C40H46N4O6 . C 2HF3O2

Molecular Formula : C40 H76 N2 O12

Molecular Formula : C40H72D4N2O12

Molecular Formula : C15H15D5O4

Molecular Formula : C48H80O40 (Undeuterated)

Molecular Formula : C9H8D5N5O4

Molecular Formula : C95H162N5Na3O47

Molecular Formula : C80H113ClN18O13 • x(C2HF3O2)

Molecular Formula : C30 H44 O7

Molecular Formula : C30 H44 O7

Molecular Formula : C13 H27 N3 O6 . 3 C2 H4 O2

Molecular Formula : C17 H24 O11

Molecular Formula : C19 2H4 H18 F N3 O4

Molecular Formula : C18H11Cl2N2NaO3

Molecular Formula : C28H32N2O • 2(HCl)

Molecular Formula : C19H19N3O3

Molecular Formula : C20H24O4

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.

Molecular Formula : C28 H34 O7

Molecular Formula : C22H21D3ClFN4O3

Molecular Formula : C14 H24 F2 N4 O10 P2

Molecular Formula : C27H58F2N6O10P2

Molecular Formula : C9 H12 F2 N3 O7 P

Molecular Formula : C21H44F2N5O13P3

Molecular Formula : C813CH12ClF2N15N2O4

Molecular Formula : C21H30O9

Molecular Formula : C21H24D6O9

Molecular Formula : C15 2H6 H16 O3

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.