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858 results found for “chromobox”
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Name :
CXCL8 MacaqueDescription:
Interleukin-8 Rhesus Macaque Recombinant
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP
Product # :
CHM-004Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL 8 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 79 amino acids and having a molecular mass of 9.1kDa.The IL 8 Rhesus Macaque is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 50-150ng/ml, corresponding to a Specific Activity of 6,667-20,000IU/mg.Citations
More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-8 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 IL-8 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
AVLPRSAKEL RCECIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE PWVQRVVEKF VKRAENQNP
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Background
What is the molecular weight/Mw of CXCL8 MACAQUE Protein?
CXCL8 MACAQUE Protein has a total Mw of 9.1kDa.
What is the source or expression system of CXCL8 MACAQUE Protein?
Escherichia Coli.
What is the Purity of CXCL8 MACAQUE Protein?
CXCL8 MACAQUE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 MACAQUE Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 50-150ng/ml, corresponding to a Specific Activity of 6,667-20,000IU/mg.
What is the amino acid sequence of CXCL8 MACAQUE Protein?
AVLPRSAKEL RCECIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE PWVQRVVEKF VKRAENQNP
What applications can CXCL8 MACAQUE Protein be used in?
CXCL8 MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 MACAQUE Protein?
The endotoxin level is minimal, CXCL8 MACAQUE Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL8 MACAQUE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL8 MACAQUE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
POU5F1 HumanDescription:
POU Class 5 Homeobox 1 Human Recombinant
POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.
Product # :
PRO-088Price :
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Shipped with Ice Packs
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Description
POU5F1 Human Recombinant produced in E. coli is a single polypeptide chain containing 285 amino acids (1-265) and having a molecular mass of 32.2 kDa.POU5F1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The POU5F1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
POU5F1 is a homeodomain transcription factor of the POU family, expressed in embryonic stem (ES) cells and embryonic carcinoma (EC) cells.POU5F1 is significantly involved in the signaling pathway for maintaining self-renewal and pluripotency of ES cells. POU5F1 has 2 distinct DNA binding domains which independently bind half-sites of the canonical octamer motif. This flexibility allows POU5F1 to bind with distinct DNA motifs by forming heterodimers with other transcription factors or by forming homodimers in several conformations. Human POU5F1 contains a 75aa POU specific (POUS) domain and a 60aa POU-Homeo-(POUH) domain connected by a linker region. The Human POU5F1 specifically interacts with Octamer motif ATGCAAAT. In addition, 2 proline-rich domains in the N-terminal and C-terminal regions are vital for POU5F1 transactivation. POU5F1 regulates a number of target genes and has been shown to work jointly with other transcription factors including Sox2 as well as Nanog to sustain stem cell potency and self-renewal.
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Synonyms
POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.
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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 MHFYRLFLGA TRRFLNPEWK GEIDNWCVYV LTSLLPFKIQ SQDIKALQKE LEQFAKLLKQ KRITLGYTQA DVGLTLGVLF GKVFSQTTIC RFEALQLSFK NMCKLRPLLQ KWVEEADNNE NLQEICKAET LVQARKRKRT SIENRVRGNL ENLFLQCPKP TLQQISHIAQ QLGLEKDVVR VWFCNRRQKG KRSSSDYAQR EDFEAAGSPF SGGPVSFPLA PGPHFGTPGY GSPHFTALYS SVPFPEGEAF PPVSVTTLGS PMHSN.
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 :
CREG1 HumanDescription:
Cellular Repressor of E1A-Stimulated Genes 1 Human Recombinant
Cellular repressor of E1A-stimulated genes 1, protein CREG1, CREG.
Product # :
PRO-1196Price :
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Shipped with Ice Packs
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Description
CREG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 213 amino acids (32-220) and having a molecular mass of 23.6 kDa.CREG1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CREG1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cellular Repressor of E1A-Stimulated Genes 1 (CREG1) both activates and inhibits gene expression to stimulate cellular proliferation and hinder differentiation. CREG1 antagonizes transcriptional activation and cellular transformation by E1A. CREG1 shares partial sequence similarity with E1A and binds both the general transcription factor TBP and the tumor suppressor pRb in vitro. CREG1 contributes to the transcriptional control of cell growth and differentiation.
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Synonyms
Cellular repressor of E1A-stimulated genes 1, protein CREG1, CREG.
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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 MGSMRGGRDH GDWDEASRLP PLPPREDAAR VARFVTHVSD WGALATISTL EAVRGRPFAD VLSLSDGPPG AGSGVPYFYL SPLQLSVSNL QENPYATLTM TLAQTNFCKK HGFDPQSPLC VHIMLSGTVT KVNETEMDIA KHSLFIRHPE MKTWPSSHNW FFAKLNITNI WVLDYFGGPK IVTPEEYYNV TVQ
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 :
BLVRB MouseDescription:
Biliverdin Reductase B Mouse Recombinant
Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR.
Product # :
ENZ-1074Price :
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Shipped with Ice Packs
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Description
BLVRB Mouse Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-206 a.a) and having a molecular mass of 24.6kDa.BLVRB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BLVRB protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
BLVRB (EC 1.3.1.24) catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. BLVRB is involved in protecting cells from oxidative damage or in regulating iron metabolism. BLVRB converts biliverdin to bilirubin in the liver, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRB plays a role as in human erythrocytic heme catabolic pathway and most mammalian species. Biliverdin reductase is abundantly expressed in kidney, spleen, liver and brain as well as at lower levels in the thymus and minimal levels being detected in testis.
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Synonyms
Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR.
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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 MGSMTVKKIA IFGATGRTGL TTLAQAVQAG YEVTVLVRDS SRLPSEGPQP AHVVVGDVRQ AADVDKTVAG QEAVIVLLGT GNDLSPTTVM SEGTRNIVTA MKAHGVDKVV ACTSAFLLWD PTKVPPRLQD VTDDHIRMHK ILQESGLKYV AVMPPHIGDQ PLTGAYTVTL DGRGPSRVIS KHDLGHFMLR CLTTNEYDGH TTYPSHQYD.
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 :
HMOX1 AntibodyDescription:
Heme Oxygenase 1, Mouse Anti Human
HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1.
Product # :
ANT-683Price :
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.
Citations
More Info
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Introduction
HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function and its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, and TNF-alpha in murine and human macrophages.
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Synonyms
HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human HMOX1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HMOX1 amino acids 1-266 purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and K light chain.
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Clone
PAT1D6AT.
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Applications
HMOX1 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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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
HMOX1 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 :
C10ORF54 MouseDescription:
Chromosome 10 Open Reading Frame 54 Mouse Recombinant
GI24, Platelet receptor Gi24, VSIR, V-Set Immunoregulatory Receptor, SISP1, GI-24, B7-H5, Stress Induced Secreted Protein 1. VISTA.
Product # :
PRO-2253Price :
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Shipped with Ice Packs
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Description
C10ORF54 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 167 amino acids (33-191a.a.) and having a molecular mass of 18.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).C10ORF54 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
C10ORF54 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Chromosome 10 Open Reading Frame 54, also known as C10ORF54 is part of the immunoglobulin superfamily. Like a transmembrane molecule, C10ORF54 is expressed in the bone on embryonic stem cells (ESCs), and on tumor cell surface as well. Accordingly, C10ORF54 supports the differentiation of ESC and ehhances BMP4 induced signaling in ESC, however C10ORF54 is also down regulated following to BMP4 exposure.
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Synonyms
GI24, Platelet receptor Gi24, VSIR, V-Set Immunoregulatory Receptor, SISP1, GI-24, B7-H5, Stress Induced Secreted Protein 1. VISTA.
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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
FKVTTPYSLY VCPEGQNATL TCRILGPVSK GHDVTIYKTW YLSSRGEVQM CKEHRPIRNF TLQHLQHHGS HLKANASHDQ PQKHGLELAS DHHGNFSITL RNVTPRDSGL YCCLVIELKN HHPEQRFYGS MELQVQAGKG SGSTCMASNE QDSDSITAAL EHHHHHH.
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 :
C-JUN HumanDescription:
Jun Proto-Oncogene Human Recombinant
Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.
Product # :
PKA-323Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
C-JUN amino acids 1-81 produced in E.coli, is a non-glycosylated, polypeptide chain having a molecular mass of 52 kDa.C-JUN is a maltose binding protein (MBP) fusion protein with an amino-terminal polyhistidine tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
C-JUN is supplied as lyophilized powder containing no additives.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
C-Jun is phosphorylatable in vitro, using either recombinant active JNK1 or JNK2, or with JNK immunoprecipitated from stimulated cells. This phosphorylation can be monitored by Western blot analysis using an antibody directed to c-Jun [pS73], in conjunction with chemiluminescence detection methods. Optimization of the cell stimulation protocol, cell lysis procedure, and reaction conditions may be required for each specific application.Citations
More Info
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Introduction
C-JUN is a gene which, in combination with c-Fos, forms the AP-1early response transcription factor. C-JUN is activated by the JNKpathway. C-JUN is the putative transforming gene of avian sarcoma virus 17. C-JUN is a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. The C-JUN gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.
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Synonyms
Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Solubility
It is recommended to centrifuge the vial prior to opening in order to bring the contents to the bottom. The reconstitution of the lyophilized c-Jun is recommended in 40mM Tris, pH 7.5, to a concentration of 0.2-1.0 mg/ml.
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Note
Kinase activity may vary depending on the substrate and reaction conditions.
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 :
HOPX HumanDescription:
HOP homeobox Human Recombinant
Homeodomain-only protein, Lung cancer-associated Y protein, Not expressed in choriocarcinoma protein 1, Odd homeobox protein 1, HOPX, HOD, HOP, LAGY, NECC1, OB1, TOTO, CAMEO, SMAP31.
Product # :
PRO-1158Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HOPX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (1-73 a.a) and having a molecular mass of 10.8kDa.HOPX is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HOPX protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Homeodomain-only protein (HOPX) functions via its interaction with SRF, thus modulating the expression of SRF-dependent cardiac-specific genes and cardiac development. HOPX inhibits SRF-dependent transcription either by hindering SRF binding to DNA or by engaging histone deacetylase (HDAC) proteins which prevent transcription by SRF. HOPX is a homeodomain protein which lacks certain conserved residues required for DNA binding. HOPX overexpression causes cardiac hypertrophy.
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Synonyms
Homeodomain-only protein, Lung cancer-associated Y protein, Not expressed in choriocarcinoma protein 1, Odd homeobox protein 1, HOPX, HOD, HOP, LAGY, NECC1, OB1, TOTO, CAMEO, SMAP31.
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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 MGSHMSAETA SGPTEDQVEI LEYNFNKVDK HPDSTTLCLI AAEAGLSEEE TQKWFKQRLA KWRRSEGLPS ECRSVTD.
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 :
CRMP1 MouseDescription:
Collapsin Response Mediator Protein-1 Mouse Recombinant
Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, Unc-33-like phosphoprotein 3, ULIP-3.
Product # :
PRO-2521Price :
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Shipping Method :
Shipped with Ice Packs
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Description
CRMP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (1-572 a.a) and having a molecular mass of 64.8kDa.CRMP1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRMP1 protein solution (0.25mg/ml) contains 40% glycerol, 20mM Tris-HCl (pH 8.5), 0.2M NaCl & 0.1mM PMSF.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation as well as axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The X-ray crystal structure of murine CRMP1 was determined at 2.1 resolution and demonstrates that CRMP1 is a bilobed ‘lung-shaped’ protein forming a tetrameric assembly.
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Synonyms
Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, Unc-33-like phosphoprotein 3, ULIP-3.
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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. 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 MGSEFMSHQG KKSIPHITSD RLLIRGGRII NDDQSFYADV YLEDGLIKQI GENLIVPGGV KTIEANGRMV IPGGIDVNTY LQKPSQGMTS ADDFFQGTKA ALAGGTTMII DHVVPEPGSS LLTSFEKWHE AADTKSCCDY SLHVDITSWY DGVREELEVL VQDKGVNSFQ VYMAYKDLYQ MSDSQLYEAF TFLKGLGAVI LVHAENGDLI AQEQKRILEM GITGPEGHAL SRPEELEAEA VFRAIAIAGR INCPVYITKV MSKSAADIIA LARKKGPLVF GEPIAASLGT DGTHYWSKNW AKAAAFVTSP PLSPDPTTPD YLTSLLACGD LQVTGSGHCP YSTAQKAVGK DNFTLIPEGV NGIEERMTVV WDKAVATGKM DENQFVAVTS TNAAKIFNLY PRKGRIAVGS DADVVIWDPD KMKTITAKSH KSTVEYNIFE GMECHGSPLV VISQGKIVFE DGNISVSKGM GRFIPRKPFP EHLYQRVRIR SKVFGLHSVS RGMYDGPVYE VPATPKHAAP APSAKSSPSK HQPPPIRNLH QSNFSLSGAQ IDDNNPRRTG HRIVAPPGGR SNITSLG.
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 :
POU6F1 HumanDescription:
POU Class 6 Homeobox 1 Human Recombinant
BRN5, MPOU, TCFB1, Brain-5, Brn-5, mPOU homeobox protein, Brain-specific homeobox/POU domain protein 5.
Product # :
PRO-1484Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
POU6F1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301 a.a.) and having a molecular mass of 35kDa.POU6F1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The POU5F1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
POU6F1 is a member of the POU transcription factor family. POU6F1 is transcription factor that binds favorably to a variant of the octamer motif (5'-ATGATAAT-3'). POU6F1 is exclusively expressed in the embryo in the developing brain, however in the adult its expression is confined to the brain, heart, skeletal muscle and lung. In the brain, the highest expression levels are found in specific cell layers of the cortex, the olfactory bulb, the hippocampus and the cerebellum.
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Synonyms
BRN5, MPOU, TCFB1, Brain-5, Brn-5, mPOU homeobox protein, Brain-specific homeobox/POU domain protein 5.
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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 MGSMPGISSQ ILTNAQGQVI GTLPWVVNSA SVAAPAPAQS LQVQAVTPQL LLNAQGQVIA TLASSPLPPP VAVRKPSTPE SPAKSEVQPI QPTPTVPQPA VVIASPAPAA KPSASAPIPI TCSETPTVSQ LVSKPHTPSL DEDGINLEEI REFAKNFKIR RLSLGLTQTQ VGQALTATEG PAYSQSAICR FEKLDITPKS AQKLKPVLEK WLNEAELRNQ EGQQNLMEFV GGEPSKKRKR RTSFTPQAIE ALNAYFEKNP LPTGQEITEI AKELNYDREV VRVWFCNRRQ TLKNTSKLNV FQIP.
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 :
CPOX HumanDescription:
Coproporphyrinogen Oxidase Human Recombinant
CPO, CPX, HCP, Coproporphyrinogen-III oxidase, mitochondrial, COX, Coprogen oxidase, Coproporphyrinogenase, CPOX.
Product # :
ENZ-701Price :
Quantity :
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Shipped with Ice Packs
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Description
CPOX Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (111-454) and having a molecular mass of 41.6kDa. CPOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CPOX solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Coproporphyrinogen Oxidase (CPOX) which is localized to the internal membrane space of erythrocytes takes part in the 6th phase of heme biosynthesis. CPOX catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III. Mutations in human CPOX gene forecast the clinical result of the disease, with either hepatic hereditary coproporphyria or hematological manifestations of erythropoietic harderoporphyria.
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Synonyms
CPO, CPX, HCP, Coproporphyrinogen-III oxidase, mitochondrial, COX, Coprogen oxidase, Coproporphyrinogenase, CPOX.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTSLGRPE EEEDELAHRC SSFMAPPVTD LGELRRRPGD MKTKMELLIL ETQAQVCQAL AQVDGGANFS VDRWERKEGG GGISCVLQDG CVFEKAGVSI SVVHGNLSEE AAKQMRSRGK VLKTKDGKLP FCAMGVSSVI HPKNPHAPTI HFNYRYFEVE EADGNKQWWF GGGCDLTPTY LNQEDAVHFH RTLKEACDQH GPDLYPKFKK WCDDYFFIAH RGERRGIGGI FFDDLDSPSK EEVFRFVQSC ARAVVPSYIP LVKKHCDDSF TPQEKLWQQL RRGRYVEFNL LYDRGTKFGL FTPGSRIESI LMSLPLTARW EYMHSPSENS KEAEILEVLR HPRDWVR.
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 :
CHMP2B HumanDescription:
Chromatin Modifying Protein 2B Human Recombinant
Chromatin modifying protein 2B, CHMP2.5, VPS2B, Vacuolar protein sorting-associated protein 2-2, hVps2-2, DMT1, DKFZp564O123, VPS2 homolog B.
Product # :
PRO-877Price :
Quantity :
Shipping Method :
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Description
CHMP2B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-213) and having a molecular mass of 26.1 kDa.The CHMP2B is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHMP2B protein 1mg/ml is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 2mM DTT and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
CHMP2B is a member of the vacuolar sorting protein family. CHMP2B is a component of the ESCRT-III complex which is essential for sorting endosomal articles into multivesicular bodies (MVBs), and are also obligatory for the formation of these bodies. CHMP2B is usually found in brain, heart, skeletal muscle, small intestine, pancreas, lung, placenta and leukocytes.
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Synonyms
Chromatin modifying protein 2B, CHMP2.5, VPS2B, Vacuolar protein sorting-associated protein 2-2, hVps2-2, DMT1, DKFZp564O123, VPS2 homolog B.
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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 MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA KIGNKEACKV LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG AMSTTAKTMQ AVNKKMDPQK TLQTMQNFQK ENMKMEMTEE MINDTLDDIF DGSDDEEESQ DIVNQVLDEI GIEISGKMAK APSAARSLPS ASTSKATISD EEIERQLKAL GVD
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 :
Trypanosoma Cruzi B13Description:
Trypanosoma Cruzi B13 Recombinant
Product # :
CCH-003Price :
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Description
Recombinant Trypanosoma Cruzi B13 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 227 amino acids and having a molecular mass of 23kDa. The Trypanosoma Cruzi B13 is fused to a His tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
(1mg/1ml) in phosphate buffer saline and 25mM k2co3.
Purity
Protein is >90% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Recombinant Trypanosoma Cruzi B13 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Background
Among the numerous antigens that T. cruzi expresses, the B13 protein has been identified as a main component involved in immune recognition and host-parasite interactions. Trypanosoma Cruzi B13 is a very immunogenic antigen found in the T. cruzi epimastigote and trypomastigote forms. Trypanosoma Cruzi B13 takes part in host-parasite interactions first by binding to host cells such as cardiac and smooth muscle cells, which are very important in the pathology of Chagas disease. Trypanosoma cruzi is the protozoan parasite responsible for Chagas disease which affects millions of people in Latin America. The parasite has a complex life cycle and eludes the immune response through various mechanisms, making it a complex target for therapeutic interventions.
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 :
TGFB2 Human, CHODescription:
Transforming Growth Factor-Beta 2 Human Recombinant, CHO
Transforming growth factor beta-2, TGF-beta-2, G-TSF, Tgfb-2, TGFbeta2.
Product # :
CYT-1268Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TGFB2 Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.4kDa.
TGFB2 Human Recombinant is purified by proprietary chromatographic techniques.Source
CHO Cells.
Formulation
The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.
Purity
Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
The biological activity was determined by TGFB2 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.2 ng/ml, corresponding to a specific activity of ≥ 5.0 × 106 units/mg.Citations
More Info
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Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 2 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 Transforming Growth Factor-Beta 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS.
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Background
Recombinant TGFB2 protein is used in cell culture to study extracellular matrix remodelling, tissue regeneration, and developmental biology.
TGFB2 takes part in embryonic development and is involved in fibrosis, wound healing, angiogenesis,
What is the molecular weight / Mw of TGFB2 Protein?
TGFB2 Protein has a total Mw of 25.4kDa.
What is the source or expression system of TGFB2 Protein?
CHO Cells
What is the Purity of TGFB2 Protein?
TGFB2 Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of TGFB2 Protein?
Determined by its ability to inhibit the mouse IL4-dependent proliferation of mouse HT2 cells. The expected ED50 for this effect is less than 0.2ng/ml, corresponding to a specific activity of ≥ 5.0 × 106 units/mg.
What is the amino acid sequence of TGFB2 Protein?
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS
What applications can TGFB2 Protein be used in?
TGFB2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TGFB2 Protein?
The endotoxin level is minimal, TGFB2 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 :
BDNF Human, CHODescription:
Brain-Derived Neurotrophic Factor Human Recombinant, CHO
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Product # :
CYT-1262Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
- Citations
Description
Brain-derived Neurotrophic Factor Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 119 amino acids and having a total molecular mass of 27kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.
Source
CHO Cells
Formulation
The protein was lyophilized with 5% trehalose and 1x PBS
Purity
Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.sds-page
Citations
More Info
-
Introduction
BDNF is crucial for the signal survival eukaryotes. BDNF is responsible for the development, repair, adaptation and proper functionality of the nervous system.
BDNF major roles include Neuron survival and development, synaptic flexibility, stress adaptation, Repair and recovery post injury/disease and Pain signaling.
-
Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
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Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.
What is the source or expression system of BDNF Protein?
CHO Cells
What is the Purity of BDNF Protein?
BDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BDNF Protein?
BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.
What is the amino acid sequence of BDNF Protein?
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
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References
Title:Generation of Neurons with Improved Cell Survival and Phenotype Maintenance Using a Degradation-Resistant Nurr1 Mutant†‡
Publication:Article first published online: 11 JUN 2009 DOI: 10.1002/stem.146 Copyright © 2009 AlphaMed Press.
Link:BDNF prospec publication
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 :
TACO1 HumanDescription:
Translational Activator of Mitochondrially Encoded Cytochrome C Oxidase Human Recombinant
Translational Activator Of Mitochondrially Encoded Cytochrome C Oxidase, CCDC44, Coiled-Coil Domain-Containing Protein 44, Coiled-Coil Domain Containing 44, Clone HQ0477 PRO0477p, Translational Activator Of Cytochrome C Oxidase 1, Translational Activator Of Mitochondrially-Encoded Cytochrome C Oxidase I.
Product # :
PRO-1746Price :
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Description
TACO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (61-297 a.a) and having a molecular mass of 28.8kDa.TACO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TACO1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Translational activator of mitochondrially encoded cytochrome c oxidase I (TACO1) belongs to the TACO1 family. TACO1 is a mitochondrial protein which functions as a translational activator of mitochondrially-encoded cytochrome c oxidase 1. Mutations in this gene are associated with Leigh syndrome.
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Synonyms
Translational Activator Of Mitochondrially Encoded Cytochrome C Oxidase, CCDC44, Coiled-Coil Domain-Containing Protein 44, Coiled-Coil Domain Containing 44, Clone HQ0477 PRO0477p, Translational Activator Of Cytochrome C Oxidase 1, Translational Activator Of Mitochondrially-Encoded Cytochrome C Oxidase I.
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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).Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSNKWSKVR HIKGPKDVER SRIFSKLCLN IRLAVKEGGP NPEHNSNLAN ILEVCRSKHM PKSTIETALK MEKSKDTYLL YEGRGPGGSS LLIEALSNSS HKCQADIRHI LNKNGGVMAV GARHSFDKKG VIVVEVEDRE KKAVNLERAL EMAIEAGAEDVKETEDEEER NVFKFICDAS SLHQVRKKLD SLGLCSVSCA LEFIPNSKVQ LAEPDLEQAA HLIQALSNHE DVIHVYDNIE
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 :
CBR1 HumanDescription:
Carbonyl Reductase-1 Human Recombinant
CBR, hCBR1, SDR21C1, CBR1, Carbonyl reductase [NADPH] 1, NADPH-dependent carbonyl reductase 1, Prostaglandin-E(2) 9-reductase, Prostaglandin 9-ketoreductase, 15-hydroxyprostaglandin dehydrogenase [NADP+], CRN.
Product # :
ENZ-415Price :
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Description
Recombinant Human CBR1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 277 amino acids (1-277 a.a) and having a molecular mass of 30 kDa. CBR1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CBR1 protein contains 20mM Tris-HCl buffer pH-8.5, and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Citations
More Info
-
Introduction
CBR1 is one of numerous monomeric, NADPH-dependent oxidoreductases having ubiquistly specificity for carbonyl compounds. CBR1 is broadly distributed in human tissues. CBR1 metabolizes toxic environmental quinones and pharmacological relevant substrates. CBR1 converts prostaglandin E2 to prostaglandin F2-alpha.
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Synonyms
CBR, hCBR1, SDR21C1, CBR1, Carbonyl reductase [NADPH] 1, NADPH-dependent carbonyl reductase 1, Prostaglandin-E(2) 9-reductase, Prostaglandin 9-ketoreductase, 15-hydroxyprostaglandin dehydrogenase [NADP+], CRN.
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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.
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Amino Acid Sequence
MSSGIHVALV TGGNKGIGLA IVRDLCRLFS GDVVLTARDV TRGQAAVQQL QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLDVLVNN AGIAFKVADP TPFHIQAEVT MKTNFFGTRD VCTELLPLIK PQGRVVNVSS IMSVRALKSC SPELQQKFRS ETITEEELVG LMNKFVEDTK KGVHQKEGWP SSAYGVTKIG VTVLSRIHAR KLSEQRKGDK ILLNACCPGW VRTDMAGPKA TKSPEEGAET PVYLALLPPD AEGPHGQFVS EKRVEQW.
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 :
CIRBP HumanDescription:
Cold Inducible RNA Binding Protein Human Recombinant
Cold-inducible RNA-binding protein, A18 hnRNP, Glycine-rich RNA-binding protein CIRP, CIRBP, A18HNRNP, CIRP.
Product # :
PRO-746Price :
Quantity :
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Description
CIRBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (1-172 a.a.) and having a molecular mass of 20.8kDa.CIRBP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CIRBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Cold inducible RNA-binding protein (CIRBP) has a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. CIRBP localizes to the nucleus and contains one RRM (RNA recognition motif) domain. Expressed ubiquitously, CIRBP is believed to play a crucial role in the suppression of cellular proliferation in response to UV irradiation or extreme cold.
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Synonyms
Cold-inducible RNA-binding protein, A18 hnRNP, Glycine-rich RNA-binding protein CIRP, CIRBP, A18HNRNP, CIRP.
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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 MASDEGKLFV GGLSFDTNEQ SLEQVFSKYG QISEVVVVKD RETQRSRGFG FVTFENIDDA KDAMMAMNGK SVDGRQIRVD QAGKSSDNRS RGYRGGSAGG RGFFRGGRGR GRGFSRGGGD RGYGGNRFES RSGGYGGSRD YYSSRSQSGG YSDRSSGGSY
RDSYDSYATH NE.
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 :
CKBB Human HisDescription:
Creatine Kinase Brain Human Recombinant, His Tag
EC 2.7.3.2, Creatine kinase B chain, Creatine kinase B type, CKB, CKBBB, B-CK, Creatine Kinase Brain.
Product # :
CKI-274Price :
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Description
CKBB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-381 a.a.) and having a molecular mass of 44.8 kDa. The CKB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CKBB Human solution containing 20mM Trsi pH-8, 1mM DTT, & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
CKB is a cytoplasmic enzyme that takes part in energy homeostasis. CKB enzyme reversibly catalyzes the transfer of phosphate among ATP and various phosphogens such as creatine phosphate. CKB functions as a homodimer in the brain as well as in different tissues, and as a heterodimer with a similar muscle isozyme in heart. Creatine kinases supply the energy of phosphate hydrolysis essential to drive the normal role of many cellular systems including muscle, tumor and cancer cells.
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Synonyms
EC 2.7.3.2, Creatine kinase B chain, Creatine kinase B type, CKB, CKBBB, B-CK, Creatine Kinase Brain.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
CKBB Human although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD
RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ 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 :
CXCL3 Mouse, HisDescription:
GRO-Gamma Mouse Recombinant (CXCL3), His Tag
C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.
Product # :
CHM-283Price :
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Description
GRO-g Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (28-100 a.a.) and having a molecular mass of 10.6kDa.CXCL3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GRO-gamma protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.15M NaCl and 5mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
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Synonyms
C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.
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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 MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.
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Background
What is the molecular weight/Mw of CXCL3 MOUSE, HIS Protein?
CXCL3 MOUSE, HIS Protein has a total Mw of 10.6kDa.
What is the source or expression system of CXCL3 MOUSE, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL3 MOUSE, HIS Protein?
CXCL3 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL3 MOUSE, HIS Protein?
The biological functionality of CXCL3 MOUSE, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL3 MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.
What applications can CXCL3 MOUSE, HIS Protein be used in?
CXCL3 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL3 MOUSE, HIS Protein?
The endotoxin level is minimal, CXCL3 MOUSE, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL3 MOUSE, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL3 MOUSE, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
CCL22 MouseDescription:
Macrophage-Derived Chemokine Mouse Recombinant (CCL22)
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.
Product # :
CHM-370Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
CCL22 Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 7.8kDa. The Mouse CCL22 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCL22 filtered (0.2µm) and lyophilized from a concentrated solution containing 20mM phosphate buffer & 150mM NaCl pH-7.4.
Purity
Greater than 97.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.Citations
More Info
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Introduction
MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4. CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph
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Synonyms
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL22 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 CCL22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
GPYGANVEDS ICCQDYIRHP LPSRLVKEFF WTSKSCRKPG VVLITVKNRD ICADPRQVWV KKLLHKLS.
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Background
What is the molecular weight/Mw of CCL22 MOUSE Protein?
CCL22 MOUSE Protein has a total Mw of 7.8kDa.
What is the source or expression system of CCL22 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL22 MOUSE Protein?
CCL22 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL22 MOUSE Protein?
Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CCL22 MOUSE Protein?
GPYGANVEDS ICCQDYIRHP LPSRLVKEFF WTSKSCRKPG VVLITVKNRD ICADPRQVWV KKLLHKLS.
What applications can CCL22 MOUSE Protein be used in?
CCL22 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL22 MOUSE Protein?
The endotoxin level is minimal, CCL22 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 :
TRAIL MouseDescription:
TNF-Related Apoptosis Inducing Ligand/Apo2L Mouse 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-806Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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- Citations
Description
TRAIL Recombinant Mouse produced in E.coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20.2kDa.
Source
Escherichia Coli.
Formulation
The protein was lyophilized containing PBS, pH 7.4, and 3mM DTT.
Purity
Greater than 95.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Biological Activity
Fully biologically active when compared to standard. The ED50 as determined by a cytotoxicity assay using murine L929 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2,000,000 IU/mg in the presence of actinomycin D.Citations
More Info
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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.
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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.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TRAIL although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TRAIL recombinant should be stored at 4C between 2-7 days and for future use below -18C.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 TRAIL Mouse Recombinant in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MPRGGRPQKV AAHITGITRR SNSALIPISK DGKTLGQKIE SWESSRKGHS FLNHVLFRNG ELVIEQEGLY YIYSQTYFRF QEAEDASKMV SKDKVRTKQL VQYIYKYTSY PDPIVLMKSA RNSCWSRDAE YGLYSIYQGG LFELKKNDRI FVSVTNEHLM DLDQEASFFG AFLIN
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 :
CREB3L2 HumanDescription:
CAMP Responsive Element Binding Protein 3-Like 2 Human Recombinant
CAMP Responsive Element Binding Protein 3-Like 2, BBF2H7, CAMP-Responsive Element-Binding Protein 3-Like Protein 2, BBF2 Human Homolog On Chromosome 7, Cyclic AMP-Responsive Element-Binding Protein 3-Like Protein 2, Basic Transcription Factor 2, B-ZIB Transcription Factor, FUS/BBF2H7 Protein, TCAG_1951439, Cyclic AMP-responsive element-binding protein 3-like protein 2, cAMP-responsive element-binding protein 3-like protein 2.
Product # :
PRO-2153Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
CREB3L2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-378 a.a) and having a molecular mass of 44kDa. CREB3L2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CREB3L2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CAMP Responsive Element Binding Protein 3-Like 2, also known as CREB3L2 belongs to the oasis bZIP transcription factor family. Members of this family are able to dimerize however from homodimers only. CREB3L2 is a transcriptional activator. Translocations between CREB3L2 on chromosome 7 and the gene fused in sarcoma on chromosome 16 can be found in some tumors. One disease which is associated with CREB3L2 is myxofibrosarcoma.
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Synonyms
CAMP Responsive Element Binding Protein 3-Like 2, BBF2H7, CAMP-Responsive Element-Binding Protein 3-Like Protein 2, BBF2 Human Homolog On Chromosome 7, Cyclic AMP-Responsive Element-Binding Protein 3-Like Protein 2, Basic Transcription Factor 2, B-ZIB Transcription Factor, FUS/BBF2H7 Protein, TCAG_1951439, Cyclic AMP-responsive element-binding protein 3-like protein 2, cAMP-responsive element-binding protein 3-like protein 2.
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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 MGSMEVLESG EQGVLQWDRK LSELSEPGDG EALMYHTHFS ELLDEFSQNV LGQLLNDPFL SEKSVSMEVE PSPTSPAPLI QAEHSYSLCE EPRAQSPFTH ITSDSFNDDE VESEKWYLST DFPSTSIKTE PITDEPPPGL VPSVTLTITA ISTPLEKEEP PLEMNTGVDS SCQTIIPKIK LEPHEVDQFL NFSPKEAPVD HLHLPPTPPS SHGSDSEGSL SPNPRLHPFS LPQTHSPSRA APRAPSALSS SPLLTAPHKL QGSGPLVLTE EEKRTLIAEG YPIPTKLPLS KSEEKALKKI RRKIKNKISA QESRRKKKEY MDSLEKKVES CSTENLELRK KVEVLENTNR TLLQQLQKLQ TLVMGKVSRT CKLAGTQTGT C.
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 :
CHMP4A HumanDescription:
Chromatin Modifying Protein 4A Human Recombinant
Charged multivesicular body protein 4A, C14orf123, HSPC134, VPS32A, Vacuolar protein sorting-associated protein 32-1, chromatin modifying protein 4A, SHAX2, SNF7-1, SNF7 homolog associated with Alix-2, chromosome 14 open reading frame 123, CHMP4B, CHMP4a.
Product # :
PRO-1024Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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- Citations
Description
CHMP4A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-265) and having a molecular mass of 32.0kDa.CHMP4A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CHMP4A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 0.1mM PMSF, 1mM EDTA, 2mM DTT and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CHMP4A is a member of the SNF7 family and operates as chromatin-modifying protein. CHMP4A is a key component of the endosomal sorting vital for transport complex III (ESCRT-III) which takes part in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. Additionally, during HIV-1 infection, the virus utilizes the ESCRT-III complex to facilitate budding and exocytosis of viral proteins through the connection of CHMP4 and a protein engaged by HIV-1 p6, which exists in viral Gag assembly and budding. CHMP4A is expressed in higher quantities in skeletal muscle, kidney, liver and heart.
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Synonyms
Charged multivesicular body protein 4A, C14orf123, HSPC134, VPS32A, Vacuolar protein sorting-associated protein 32-1, chromatin modifying protein 4A, SHAX2, SNF7-1, SNF7 homolog associated with Alix-2, chromosome 14 open reading frame 123, CHMP4B, CHMP4a.
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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 MSRRRPEDGL GKAGPCVMRH HPPRSKAEVW RTLRGGGGRG ELAMSGLGRL FGKGKKEKGP TPEEAIQKLK ETEKILIKKQ EFLEQKIQQE LQTAKKYGTK NKRAALQALR RKKRFEQQLA QTDGTLSTLE FQREAIENAT TNAEVLRTME LAAQSMKKAY QDMDIDKVDE LMTDITEQQE VAQQISDAIS RPMGFGDDVD EDELLEELEE LEQEELAQEL LNVGDKEEEP SVKLPSVPST HLPAGPAPKV DEDEEALKQL AEWVS
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.