Search results
1000 results found for “keratinocyte growth factor”
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Name :
CNTF RatDescription:
Ciliary Neurotrophic Factor Rat Recombinant
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Product # :
CYT-654Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CNTF Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids and having a molecular mass of 22834 Dalton. The CNTF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.025% NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active by its ability to phosphorylate STAT3 in several cells lines.More Info
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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CNTF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CNTF in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.
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Amino Acid Sequence
AFAEQTPLTL HRRDLSSRSIWLARKIRSDLTALMESYVKHQGLNKNI
NLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRV
HFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPA
TVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESH
YGAKDKQM. -
Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 22kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
Fully biologically active by its ability to phosphorylate STAT3 in several cells lines.
What is the amino acid sequence of CNTF Protein?
AFAEQTPLTL HRRDLSSRSIWLARKIRSDLTALMESYVKHQGLNKNI
NLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRV
HFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPA
TVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESH YGAKDKQM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ARF1 HumanDescription:
ADP-Ribosylation Factor 1 Human Recombinant
ARF-1, ADP-ribosylation factor 1.
Product # :
PRO-867Price :
Quantity :
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Shipped with Ice Packs
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Description
ARF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.8 kDa. The ARF1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARF1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ARF1 is a small guanine nucleotide-binding protein that increases the enzymatic activities of cholera toxin. ARF1 is necessary and ubiquitous in eukaryotes. ARF1 takes part in vesicular transport and functioning via phospholipase D activation. ARF1 is involved in membrane traffic and organelle integrity which are closely tied to their reversible association with membranes and distinct interactions with membrane phospholipids.
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Synonyms
ARF-1, ADP-ribosylation factor 1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ K.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KRT20 AntibodyDescription:
Cytokeratin 20, Mouse Anti Human
Keratin type I cytoskeletal 20, Cytokeratin-20, CK-20, Keratin-20, K20, Protein IT, KRT20, CD20, CK20, KRT21, MGC35423.
Product # :
ANT-563Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
KRT20 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. This cytokeratin is a major cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa. The type I cytokeratin genes are clustered in a region of chromosome 17q12-q21.
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Synonyms
Keratin type I cytoskeletal 20, Cytokeratin-20, CK-20, Keratin-20, K20, Protein IT, KRT20, CD20, CK20, KRT21, MGC35423.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human KRT20 mAb, clone PAT10D8AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human KRT20 protein 1-424 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and k light chain.
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Clone
PAT10D8AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:200.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
KRT20 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Midkine Human, HisDescription:
Midkine Human Recombinant, His Tag
NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.
Product # :
CYT-444Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Midkine Human Recombinant is manufactured with N-terminal fusion of His Tag, having a molecular mass of 14.6 kDa protein and containing 121 amino acid residues of the Midkine human and 10 additional amino acid residues – His Tag (underlined).
Source
Escherichia Coli.
Formulation
Lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.1M NaCl, pH 7.2.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis. -
Synonyms
NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add 0.2 ml of PBS pH 7.2 and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
MKHHHHHHHM KKKDKVKKGG PGSECAEWAW GPCTPSSKDC GVGFREGTCG AQTQRIRCRV PCNWKKEFGA DCKYKFENWG ACDGGTGTKV RQGTLKKARY NAQCQETIRV TKPCTPKTKA KAKAKKGKGK D.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
EREG Human, HEKDescription:
Epiregulin Human Recombinant, HEK
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
Product # :
CYT-1206Price :
Quantity :
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Shipped with Ice Packs
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Description
EREG Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (63-108a.a) containing 289 amino acids and having a molecular mass of 32.6 kDa.EREG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
EREG protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
More Info
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Introduction
"Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence."
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Synonyms
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 32.6kDa.
What is the source or expression system of EREG Protein?
HEK293 cells.
What is the Purity of EREG Protein?
EREG Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
What is the amino acid sequence of EREG Protein?
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IF HumanDescription:
Intrinsic Factor Human Recombinant
Gastric intrinsic factor, Intrinsic factor, INF, IF, GIF, IFMH, TCN3, Cobalamin/Vitamin B-12 binding transport protein.
Product # :
PRO-375Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Intrinsic Factor Human Recombinant produced in baculovirus is a glycosylated, polypeptide chain having a molecular mass of 55,000 Dalton. The Intrinsic Factor is fused to a hexa-histidine at the C-terminus and purified by proprietary chromatographic techniques for removal of bound Vitamin B-12.
Source
Sf9 Insect Cells.
Formulation
The protein solution contains 20mM HEPES pH-8.0, 100mM NaCl and 20% Glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Intrinsic Factor is a member of the cobalamin transport protein family. It encodes a glycoprotein secreted by parietal cells of the gastric mucosa and is required for adequate absorption of vitamin B12 in the terminal ileum. Vitamin B12 is essential for erythrocyte maturation and mutations in the Intrinsic Factor may lead to congenital pernicious anemia. Upon entry into the stomach, vitamin B12 binds to one of two B12 binding proteins present in the gastric fluid. In the less acidic environment of the small intestine, these proteins dissociate from the vitamin, allowing it to bind to intrinsic factor and enter the portal circulation through a receptor in the ileal mucosa specific for the B12-intrinsic factor complex.
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Synonyms
Gastric intrinsic factor, Intrinsic factor, INF, IF, GIF, IFMH, TCN3, Cobalamin/Vitamin B-12 binding transport protein.
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Physical Appearance
Sterile Filtered pink solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BATF HumanDescription:
Basic Leucine Zipper Transcription Factor Human Recombinant
Basic leucine zipper transcriptional factor ATF-like, B-cell-activating transcription factor, B-ATF, SF-HT-activated gene 2 protein, SFA-2, BATF, SFA2, BATF1.
Product # :
PRO-119Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BATF Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids (1-125 a.a.) and having a molecular mass of 16.2kDa. The BATF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BATF solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl and 40% glycerol.
Purity
BATF purity was found to be greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
BATF is a nuclear basic leucine zipper protein which is a member of the AP-1/ATF superfamily of transcription factors. BATF is intensely expressed in mature T and B lymphocytes, and is up-regulated after transformation by human T-cell leukemia virus type I. BATF acts as a tissue-specific modulator of the AP-1 transcription complex in human cells. Furthermore, BATF connects with IFP35 which is a leucine zipper protein that translocates to the nucleus following IFN treatment.
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Synonyms
Basic leucine zipper transcriptional factor ATF-like, B-cell-activating transcription factor, B-ATF, SF-HT-activated gene 2 protein, SFA-2, BATF, SFA2, BATF1.
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Physical Appearance
BATF is supplied as a sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPHSSDSSDS SFSRSPPPGK QDSSDDVRRV QRREKNRIAA QKSRQRQTQK ADTLHLESED LEKQNAALRK EIKQLTEELK YFTSVLNSHE PLCSVLAAST PSPPEVVYSA HAFHQPHVSS PRFQP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LITAF HumanDescription:
Lipopolysaccharide-Induced TNF Factor Human Recombinant
Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.
Product # :
PRO-1350Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LITAF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (1-161) and having a molecular mass of 19.2 kDa. LITAF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LITAF solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Lipopolysaccharide-induced TNF-alpha factor (LITAF) is a small integral membrane protein of lysosome/late endosome. The expression of inflammatory cytokines such as TNF-alpha in Lipopolysaccharide-induced processes is mediated by LITAF. LITAF connects to STAT6B, which belongs to the STAT6 family forming a complex on the TNF-alpha promoter that modifies TNF activity. High levels of expression of LITAF mRNA are observed mostly in the placenta, peripheral blood leukocytes, lymph nodes and spleen.
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Synonyms
Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG SLCLLGCIAG CCFIPFCVDA LQDVDHYCPN CRALLGTYKR L.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CRK HumanDescription:
V-crk Sarcoma Virus CT10 Oncogene Human Recombinant
Adapter molecule crk, Proto-oncogene c-Crk, p38, CRK, CRKII.
Product # :
PRO-275Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRK Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids (1-204 a.a.) and having a molecular mass of 25kDa. The CRK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRK solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CRK belongs to the signaling adapter protein family which binds to several tyrosine-phosphorylated proteins. CRK is involved in many cellular processes such as apoptosis, proliferation, and differentiation. CRK has a modular domain architecture consisting of an SH2 followed by two SH3 domains (src-homology domains). The N-terminal SH2 domain of the CRK protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation.
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Synonyms
Adapter molecule crk, Proto-oncogene c-Crk, p38, CRK, CRKII.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS VSENSRVSHY IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL LEFYKIHYLD TTTLIEPVSR SRQGSGVILR QEEAEYVRAL FDFNGNDEED LPFKKGDILR IRDKPEEQWW NAEDSEGKRG MIPVPYVEKY RPASASVSAL IGGR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 12 p35 HumanDescription:
Interleukin-12 p35 Human Recombinant
NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.
Product # :
CYT-487Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Interleukin-12 p35 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 197 amino acids fragment (57-253) with an amino-terminal hexahistidine tag. The IL-12 p35 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin-12 p35 His-Tag is supplied in 1xPBS and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
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Synonyms
NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GMFG HumanDescription:
Glia Maturation Factor Gamma Human Recombinant
Glia maturation factor gamma, GMF-gamma, GMFG, MGC126867.
Product # :
CYT-632Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
Glia Maturation Factor-Gamma (GMF-Gamma) Human Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 142 amino acids and having a total molecular mass of 16.8 kDa. Glia Maturation Factor-Gamma, GMF-Gamma, Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GMF-gamma protein contains 20mM Tris-HCl pH-8, 1mM DTT, 1mM EDTA and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
GMFG is a hematopoietic-specific protein that mediates the pluripotentiality and lineage commitment of human hematopoietic stem cells. Glia maturation factor gamma is a cytokine-responsive protein in EPO-induced and G-CSF-induced hematopoietic lineage development. Glia maturation factor also acts as a Nerve Growth Factor in nervous system development, angiogenesis and immune function. GMFG possesses hematopoietic tissue-specific gene expression, a promoter concentrated with high-score hematopoiesis-specific transcription factors, and molecular coevolution with a rudimentary blood/immune system.
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Synonyms
Glia maturation factor gamma, GMF-gamma, GMFG, MGC126867.
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Physical Appearance
Sterile Filtered colorless clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MSDSLVVCEV DPELTEKLRK FRFRKETDNA AIIMKVDKDR QMVVLEEEFQ NISPEELKME LPERQPRFVV YSYKYVHDDG RVSYPLCFIF SSPVGCKPEQ
QMMYAGSKNR LVQTAELTKV FEIRTTDDLT EAWLQEKLSF FR. -
Background
What is the molecular weight/Mw of GMFG HUMAN Protein?
GMFG HUMAN Protein has a total Mw of 16.8kDa.
What is the source or expression system of GMFG HUMAN Protein?
Escherichia Coli.
What is the Purity of GMFG HUMAN Protein?
GMFG HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GMFG HUMAN Protein?
The biological functionality of GMFG HUMAN Protein will be determined in the future.
What is the amino acid sequence of GMFG HUMAN Protein?
MSDSLVVCEV DPELTEKLRK FRFRKETDNA AIIMKVDKDR QMVVLEEEFQ NISPEELKME LPERQPRFVV YSYKYVHDDG RVSYPLCFIF SSPVGCKPEQ
QMMYAGSKNR LVQTAELTKV FEIRTTDDLT EAWLQEKLSF FR.
What applications can GMFG HUMAN Protein be used in?
GMFG HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GMFG HUMAN Protein?
The endotoxin level is minimal, GMFG HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CDNF MouseDescription:
Cerebral Dopamine Neurotrophic Factor Mouse Recombinant
Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.
Product # :
CYT-729Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CDNF Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 163 amino acids and having a molecular mass of 18.5kDa.The CDNF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
CDNF Mouse is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-30 µg/mL on a nitrocellulose-coated microplate.More Info
-
Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for dopamine neurons. CDNF inhibits the 6-hydroxydopamine (6-OHDA)-induced degeneration of dopaminergic neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the dopaminergic function and inhibits the degeneration of dopaminergic neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
-
Synonyms
Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.
-
Background
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.5kDa.
What is the source or expression system of CDNF Protein?
Escherichia Coli.
What is the Purity of CDNF Protein?
CDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CDNF Protein?
CDNF Mouse is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-30 µg/mL on a nitrocellulose-coated microplate.
What is the amino acid sequence of CDNF Protein?
QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.
What applications can CDNF Protein be used in?
CDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CDNF Protein?
The endotoxin level is minimal, CDNF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LGALS2 MouseDescription:
Galectin-2 Mouse Recombinant
Galectin-2, Gal-2, Lgals2, AI324147, 2200008F12Rik.
Product # :
CYT-019Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- SDS-PAGE
Description
LGALS2 mouse Recombinant produced E. coli is a single polypeptide chain containing 153 amino acids (1-130) and having a molecular mass of 17.3kDa.LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LGALS2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
-
Introduction
LGALS2 is a soluble beta-galactoside binding lectin that controls cell-to-cell adhesion and cell-to-extracellular matrix interactions and takes part in tumor progression, pre-mRNA splicing and apoptosis. LGALS2 induces apoptosis in activated T cells and binds to the cytokine lymphotoxin-alpha (LTA) with threat of myocardial infarction.
-
Synonyms
Galectin-2, Gal-2, Lgals2, AI324147, 2200008F12Rik.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.
-
Background
What is the molecular weight/Mw of LGALS2 MOUSE Protein?
LGALS2 MOUSE Protein has a total Mw of 17.3kDa.
What is the source or expression system of LGALS2 MOUSE Protein?
Escherichia Coli.
What is the Purity of LGALS2 MOUSE Protein?
LGALS2 MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS2 MOUSE Protein?
The biological functionality of LGALS2 MOUSE Protein will be determined in the future.
What is the amino acid sequence of LGALS2 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.
What applications can LGALS2 MOUSE Protein be used in?
LGALS2 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS2 MOUSE Protein?
The endotoxin level is minimal, LGALS2 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TACI Human, HisDescription:
Tumor Necrosis Factor Receptor 13B Human Recombinant, His Tag
CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.
Product # :
CYT-032Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
TACI Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 188 amino acids (1- 165a.a.) and having a molecular mass of 20.9kDa. The TACI is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TACI solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.
-
Synonyms
CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSGLGRS RRGGRSRVDQ EERFPQGLWT GVAMRSCPEE QYWDPLLGTC MSCKTICNHQ SQRTCAAFCR SLSCRKEQGK FYDHLLRDCI SCASICGQHP KQCAYFCENK LRSPVNLPPE LRRQRSGEVE NNSDNSGRYQ GLEHRGSEAS PALPGLKLSA DQVALVYS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CBFB HUmanDescription:
Core Binding Factor Beta Human Recombinant
PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.
Product # :
PRO-534Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CBFB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-202 a.a.) and having a molecular mass of 23.6 kDa. The CBFB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
0.5mg/ml solution containing 20mM MES pH-6, 0.1mM PMSF & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
CBFB beta subunit is a heterodimeric core-binding transcription factor that is part of the PEBP2/CBF transcription factor family which controls a host of genes particulary to hematopoiesis and osteogenesis. CBFB is a non-DNA binding regulatory subunit which increases DNA binding by alpha subunit.
-
Synonyms
PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
CBFB Human although stable at 4C for 1 week, should be stored below -18C. Please prevent freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QARFQNACRD GRSEIAFVAT GTNLSLQFFP
ASWQGEQRQT PSREYVDLER EAGKVYLKAP MILNGVCVIW KGWIDLQRLD GMGCLEFDEE RAQQEDALAQ QAFEEARRRT REFEDRDRSH
REEMEVRVSQ LLAVTGKKTT RP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TRAIL HumanDescription:
TRAIL / APO2 Ligand Human Recombinant
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
Product # :
CYT-443Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
TRAIL/APO 2 Ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (Met+Arg115-Gly281) and having a molecular mass of ~21kDa. The sTRAIL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a filtered (0.2µm) solution containing 20mM Tris-HCl pH 8.0 and 150mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the cytolysis of Murine L929 cells in the presence of Actinomycin D, ED50 for this effect is less than 2ng/ml, corresponding to a specific activity of 5,000,000IU/mg.More Info
-
Introduction
TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
In humans, the gene that encodes for TRAIL is located at chromosome 3q26. TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues. -
Synonyms
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized APO 2 Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized TRAIL in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MRERGPQRVA AHITGTRGRS NTLSSPNSKN EKALGRKINS WESSRSGHSF LSNLHLRNGE LVIHEKGFYY IYSQTYFRFQ EEIKENTKND KQMVQYIYKY TSYPDPILLM KSARNSCWSK DAEYGLYSIY QGGIFELKEN DRIFVSVTNE HLIDMDHEAS FFGAFLVG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GTF3C6 HumanDescription:
General Transcription Factor IIIC Polypeptide 6 Human Recombinant
bA397G5.3, C6orf51, TFIIIC35, General transcription factor 3C polypeptide 6, Transcription factor IIIC 35 kDa subunit, TFIIIC 35 kDa subunit, TFIIIC35, Transcription factor IIIC subunit 6, CDA020, NPD020.
Product # :
PRO-2127Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GTF3C6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-213 a.a) and having a molecular mass of 26.4kDa.GTF3C6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GTF3C6 protein solution (0.5mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
In the absence of additional proteins - the general transcription factors (GTFs) RNA polymerases are unable to initiate RNA synthesis. GTFs accumulate in a complex on the DNA promoter and recruit the RNA polymerase. GTF3C family proteins are vital for RNA polymerase III to produce several small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin.
-
Synonyms
bA397G5.3, C6orf51, TFIIIC35, General transcription factor 3C polypeptide 6, Transcription factor IIIC 35 kDa subunit, TFIIIC 35 kDa subunit, TFIIIC35, Transcription factor IIIC subunit 6, CDA020, NPD020.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAAADE RSPEDGEDEE EEEQLVLVEL SGIIDSDFLS KCENKCKVLG IDTERPILQV DSCVFAGEYE DTLGTCVIFE ENVEHADTEG NNKTVLKYKC HTMKKLSMTR TLLTEKKEGE ENIGGVEWLQ IKDNDFSYRP NMICNFLHEN EDEEVVASAP DKSLELEEEE IQMNDSSNLS CEQEKPMHLE IEDSGPLIDI PSETEGSVFM ETQMLP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
YWHAG Human, HisDescription:
Tyr-3/Trp-5 Monooxygenase Activation Protein Gamma Human Recombinant, His Tag
14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.
Product # :
PKA-262Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
YWHAG Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids (2-247) and having a molecular mass of 36 kDa. YWHAG is fused to His Tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
YWHAG solution containing 1x PBS and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.
-
Synonyms
14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MIF MouseDescription:
Macrophage Migration Inhibitory Factor Mouse Recombinant
Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase, Glif.
Product # :
CYT-744Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
MIF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa.The MIF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution containing 1mM sodium phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase, Glif.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized MIF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTNDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL-6 PAT1F10AT AntibodyDescription:
Interleukin-6 Clone PAT1F10AT, Mouse Anti Human
IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, Interferon beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
Product # :
ANT-540Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.
-
Synonyms
IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, Interferon beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
-
Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human IL-6, clone PAT1F10AT mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IL-6 protein 30-212 amino acids purified from E. coli.
-
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
-
Clone
PAT1F10AT.
-
Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
-
Background
Research Paper on Interleukin-6 Clone PAT1F10AT, Mouse Anti-Human
Abstract:
Interleukin-6 (IL-6) Clone PAT1F10AT, a Mouse Anti-Human monoclonal antibody, plays a pivotal role in deciphering the complexities of immune modulation. This research paper provides an insightful exploration of its molecular attributes and its profound implications in immunological research. We examine its interactions, functions, and synonyms, including DIF, TNFA, and TNFSF2, shedding light on its significance in understanding immune responses.
Introduction:
IL-6 Clone PAT1F10AT, a Mouse Anti-Human antibody, has emerged as a cornerstone in immunology research. This paper delves into its unique characteristics and its critical role in unraveling immune mechanisms.
Molecular Precision and Specificity:
The exceptional affinity and specificity of IL-6 Clone PAT1F10AT for human IL-6 distinguish it as an invaluable tool for immunodetection and functional studies. Its targeted binding facilitates accurate identification of IL-6 in various experimental contexts.
Unveiling Immune Dynamics:
IL-6 is a central player in immune orchestration, and IL-6 Clone PAT1F10AT offers a window into its world. By investigating its involvement in immune responses, inflammation, and signaling pathways, researchers gain insights into immune regulation.
Synonyms and Interactions:
Understanding IL-6 synonyms, such as DIF, TNFA, and TNFSF2, underscores its intricate web of interactions. IL-6 Clone PAT1F10AT's ability to decipher these connections enhances our understanding of cytokine-mediated immune modulation.
Disease Implications and Therapeutic Avenues:
With its relevance in diseases like autoimmune disorders and inflammatory conditions, IL-6 Clone PAT1F10AT assumes significance in disease-focused investigations. It enables researchers to dissect disease mechanisms and evaluate potential therapeutic interventions.
Clinical Utility and Diagnostic Precision:
IL-6 Clone PAT1F10AT's utility transcends research settings, finding application in clinical diagnostics. Its role in immunoassays facilitates accurate disease diagnosis and monitoring, contributing to improved patient management.
Conclusion:
In the realm of immunology, IL-6 Clone PAT1F10AT stands as a potent ally in unraveling immune intricacies. Its molecular precision, diverse functions, and potential therapeutic implications make it a cornerstone in advancing our understanding of immune responses and diseases.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
IL-6 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin DogDescription:
Leptin Dog Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-506Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Dog Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MIF Mouse, HisDescription:
Macrophage Migration Inhibitor Factor Mouse Recombinant, His Tag
Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
Product # :
CYT-896Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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- More Info
Description
MIF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 14.9kDa. MIF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIF protein solution (0.5mg/ml) containing Phosphate buffered saline , 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPMFIVN TNVPRASVPE GFLSELTQQL AQATGKPAQY IAVHVVPDQL MTFSGTNDPC ALCSLHSIGK IGGAQNRNYS KLLCGLLSDR LHISPDRVYI NYYDMNAANV GWNGSTFA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TNFRSF10A Human FcDescription:
TRAIL Receptor-1 Human Recombinant Fc
Tumor Necrosis Factor Receptor Superfamily Member 10a, TRAILR1, APO2, DR4, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261, TNFRSF10A.
Product # :
CYT-877Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
TRAIL R1 Fc Human Recombinant (24-240) produced in E.Coli is a non-glycosylated, disulfide-linked homodimer containing two polypeptide chains of 217 amino acids each and having a molecular mass of 41kDa [including tag] each chain. TRAILR1 is fused to a 236 amino acid Fc tag at C-terminal and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to inhibit Trail-mediated cytotoxicity in mouse L-929 cells, is less than 1.25ng/ml.More Info
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Introduction
Human TNFRSF10A is a type 1 transmembrane protein in the TNF R superfamily. TNFRSF10A is not expressed in rodents. The trimeric ligand Trail binds TNFRSF10A and induces apoptosis, and recombinant, soluble forms of the receptor inhibit Trail-induced apoptosis. TNFRSF10A is expressed generally in damaged, infected, and malignant cells. TNFRSF10A functions in immune surveillance, inducing apoptosis in cancer cells but not normal cells.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 10a, TRAILR1, APO2, DR4, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261, TNFRSF10A.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TNFRSF10A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL-R1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized TNFRSF10A in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ASGTEAAAAT PSKVWGSSAG RIEPRGGGRG ALPTSMGQHG PSARARAGRA PGPRPAREAS PRLRVHKTFK FVVVGVLLQV VPSSAATIKL HDQSIGTQQW EHSPLGELCP PGSHRSERPG ACNRCTEGVG YTNASNNLFA CLPCTACKSD EEERSPCTTT RNTACQCKPG TFRNDNSAEM CRKCSTGCPR GMVKVKDCTP WSDIECVHKE SGNGHNIEGR MDPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CNTF Human, HisDescription:
Ciliary Neurotrophic Factor Human Recombinant, His Tag
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Product # :
CYT-573Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain (aa 1-200) containing a total of 220 amino acids and having a molecular mass of 25kDa. The CNTF protein is fused to a 20 aa His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNTF protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH-8 and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
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Physical Appearance
Sterile Filtered colorless clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAFTEHSPLT PHRRDLCSRS IWLARKIRSDLTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.
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Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 25kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
The biological functionality of CNTF Protein will be determined in the future.
What is the amino acid sequence of CNTF Protein?
MGSSHHHHHH SSGLVPRGSH MAFTEHSPLT PHRRDLCSRS IWLARKIRSDLTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.