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1000 results found for “Calreticulin”
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- View Data Sheet
Name :
Gliadin Gamma 18.6kDa WheatDescription:
Gliadin Gamma 18.6kD Wheat Recombinant
Product # :
PRO-114Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Gliadin is a cDNA coding for an epitope-carrying fragment of a wheat gamma-gliadin isoform, having a molecular mass of 19 kDa (high proline content and the low pI are likely causes for the observed discrepancy between calculated molecular weight and the observed electrophoretic mobility of approx. 50 kDa on standard SDS-PAGE), pH 4.6. By sequence design the epitopes correspond to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation. Gliadin protein is fused to a hexa-histidine purification tag.
Source
Escherichia Coli.
Formulation
Gliadin is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl, and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG- and IgA-type human autoantibodies associated with celiac disease. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot.
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coating concentration
0.15-0.5 µg/ml (depending on the type of ELISA plate and coating buffer).
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Applications
Western blot with monoclonal anti-hexa-His-tag antibody.
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 :
CNTFR RatDescription:
Ciliary Neurotrophic Factor Receptor Rat Recombinant
Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.
Product # :
CYT-959Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CNTFR Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 328 amino acids (23-342a.a) and having a molecular mass of 36.9kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CNTFR is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CNTFR protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ciliary Neurotrophic Factor Receptor, also known as CNTFR is a member of the type I cytokine receptor family. CNTFR binds to CNTF.The alpha subunit provides the receptor specificity.Sole nucleotide polymorphisms in CNTFR has been associated with variations in muscle strength, in addition to early onset of eating disorders.
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Synonyms
Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.
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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
QKHSPQEAPH VQYERLGTDV TLPCGTASWD AAVTWRVNGT DLAPDLLNGS QLILRSLELG HSGLYACFHR DSWHLRHQVL LHVGLPPREP VLSCRSNTYP KGFYCSWHLS APTYIPNTFN VTVLHGSKMM VCEKDPALKN RCHIRYMHLF STIKYKVSIS VSNALGHNTT AITFDEFTIV KPDPPENVVA RPVPSNPRRL EVTWQTPSTW PDPESFPLKF FLRYRPLILD QWQHVELSNG TAHTITDAYA GKEYIIQVAA KDNEIGTWSD WSVAAHATPW TEEPRHLTTE AQAPETTTST TSSLAPPPTT KICDPGELSS LEHHHHHH.
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Background
What is the molecular weight/Mw of CNTFR Protein?
CNTFR Protein has a total Mw of 36.9kDa.
What is the source or expression system of CNTFR Protein?
Sf9, Baculovirus cells.
What is the Purity of CNTFR Protein?
CNTFR Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTFR Protein?
The biological functionality of CNTFR Protein will be determined in the future.
What is the amino acid sequence of CNTFR Protein?
QKHSPQEAPH VQYERLGTDV TLPCGTASWD AAVTWRVNGT DLAPDLLNGS QLILRSLELG HSGLYACFHR DSWHLRHQVL LHVGLPPREP VLSCRSNTYP KGFYCSWHLS APTYIPNTFN VTVLHGSKMM VCEKDPALKN RCHIRYMHLF STIKYKVSIS VSNALGHNTT AITFDEFTIV KPDPPENVVA RPVPSNPRRL EVTWQTPSTW PDPESFPLKF FLRYRPLILD QWQHVELSNG TAHTITDAYA GKEYIIQVAA KDNEIGTWSD WSVAAHATPW TEEPRHLTTE AQAPETTTST TSSLAPPPTT KICDPGELSS LEHHHHHH.
What applications can CNTFR Protein be used in?
CNTFR Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTFR Protein?
The endotoxin level is minimal, CNTFR 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 :
MCAM HumanDescription:
Melanoma Cell Adhesion Molecule Human Recombinant
Cell surface glycoprotein MUC18, Cell surface glycoprotein P1H12, Melanoma cell adhesion molecule, Melanoma-associated antigen A32, Melanoma-associated antigen MUC18, S-endo 1 endothelial-associated antigen, CD146, MCAM, MUC18, Cell Surface Glycoprotein MUC18, Melanoma Adhesion Molecule, CD146 Antigen, CD146, Melanoma Cell Adhesion Molecule, S-Endo 1 Endothelial-Associated Antigen, Melanoma-Associated Antigen MUC18, Cell Surface Glycoprotein P1H12, Melanoma-Associated Antigen A32, Gicerin.
Product # :
PRO-2503Price :
Quantity :
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Shipped with Ice Packs
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Description
MCAM produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 547 amino acids (24-559 a.a.) and having a molecular mass of 61.0kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).MCAM is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
MCAM protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cell surface glycoprotein MUC18 (MCAM), is an integral membrane glycoprotein which is part of the immunoglobulin superfamily. MCAM is related with a variety of carcinomas such as tumor progression, metastasis and is also implicated in embryonic neural development. In Addition, MCAM takes part in cell adhesion, as well as in cohesion of the endothelial monolayer at the intercellular junctions in vascular tissue.
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Synonyms
Cell surface glycoprotein MUC18, Cell surface glycoprotein P1H12, Melanoma cell adhesion molecule, Melanoma-associated antigen A32, Melanoma-associated antigen MUC18, S-endo 1 endothelial-associated antigen, CD146, MCAM, MUC18, Cell Surface Glycoprotein MUC18, Melanoma Adhesion Molecule, CD146 Antigen, CD146, Melanoma Cell Adhesion Molecule, S-Endo 1 Endothelial-Associated Antigen, Melanoma-Associated Antigen MUC18, Cell Surface Glycoprotein P1H12, Melanoma-Associated Antigen A32, Gicerin.
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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
VPGEAEQPAP ELVEVEVGST ALLKCGLSQS QGNLSHVDWF SVHKEKRTLI FRVRQGQGQS EPGEYEQRLS LQDRGATLAL TQVTPQDERI FLCQGKRPRS QEYRIQLRVY KAPEEPNIQV NPLGIPVNSK EPEEVATCVG RNGYPIPQVI WYKNGRPLKE EKNRVHIQSS QTVESSGLYT LQSILKAQLV KEDKDAQFYC ELNYRLPSGN HMKESREVTV PVFYPTEKVW LEVEPVGMLK EGDRVEIRCL ADGNPPPHFS ISKQNPSTRE AEEETTNDNG VLVLEPARKE HSGRYECQGL DLDTMISLLS EPQELLVNYV SDVRVSPAAP ERQEGSSLTL TCEAESSQDL EFQWLREETG QVLERGPVLQ LHDLKREAGG GYRCVASVPS IPGLNRTQLV NVAIFGPPWM AFKERKVWVK ENMVLNLSCE ASGHPRPTIS WNVNGTASEQ DQDPQRVLST LNVLVTPELL ETGVECTASN DLGKNTSILF LELVNLTTLT PDSNTTTGLS TSTASPHTRA NSTSTERKLP EPESRGAAAL 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.
- View Data Sheet
Name :
PTH (7-84) HumanDescription:
Parathyroid Hormone (7-84) Human Recombinant
Parathyrin, PTH, Parathormone.
Product # :
HOR-011Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PTH (7-84) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids, having an MW of 8.8kDa. The PTH (7-84) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calcium in the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptor in three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone. In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb. In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylation of 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
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Synonyms
Parathyrin, PTH, Parathormone.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PTH (7-84) although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PTH (7-84) 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 PTH (7-84) 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
LMHNLGKHLN SMERVEWLRK KLQDVHNFVA LGAPLAPRDA GSQRPRKKED NVLVESHEKS LGEADKADVN VLTKAKSQ.
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 :
CTLA4 Human, IgG-His, ActiveDescription:
CTLA4 Human Recombinant, igG-His Tag, Active
CTLA4, ALPS5, CD, CD152, CELIAC3, CTLA-4, GRD4, GSE, IDDM12, CD152, Cytotoxic T-Lymphocyte Associated Antigen-4, igG-His Tag.
Product # :
CYT-1144Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CTLA4 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 368 amino acids (36-161aa) and having a molecular mass of 40.8kDa.CTLA4 is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CTLA4 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Determined by the IL-2 ELISA in a using Jurkat human acute T cell leukemia cells. ED50 range for this is ≤ 150 ng/ml with Human B7 1/CD80.
More Info
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Introduction
Cytotoxic T-lymphocyte-associated protein 4 or CTLA4 or CD152 is a receptor that takes part in the immune checkpoint and inhibits immune response. This protein is fundamentally found in regulatory T cells; however, it acts as an enhancer in regular T cells following its activation, this is eminent in cancers. CTLA4 bounds to CD80 or CD86 on the membrane of antigen presenting cells and downregulates transductions.
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Synonyms
CTLA4, ALPS5, CD, CD152, CELIAC3, CTLA-4, GRD4, GSE, IDDM12, CD152, Cytotoxic T-Lymphocyte Associated Antigen-4, igG-His Tag.
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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
ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG
NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI
DPEPCPDSDL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD
VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN
KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG
QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH -
Background
What is the molecular weight/Mw of CTLA4 Protein?
CTLA4 Protein has a total Mw of 40.8kDa.
What is the source or expression system of CTLA4 Protein?
Sf9, Baculovirus cells.
What is the Purity of CTLA4 Protein?
CTLA4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CTLA4 Protein?
Determined by the IL-2 ELISA in a using Jurkat human acute T cell leukemia cells. ED50 range for this is ≤ 150 ng/ml with Human B7 1/CD80.
What is the amino acid sequence of CTLA4 Protein?
ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG
NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI
DPEPCPDSDL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD
VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN
KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG
QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH
What applications can CTLA4 Protein be used in?
CTLA4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTLA4 Protein?
The endotoxin level is minimal, CTLA4 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 :
CXCL16 HumanDescription:
CXCL16 Human Recombinant
Chemokine (C-X-C Motif) Ligand 16, Scavenger Receptor For Phosphatidylserine And Oxidized Low Density Lipoprotein, Transmembrane Chemokine CXCL16, Small-Inducible Cytokine B16, CXC Chemokine Ligand 16, SR-PSOX, SRPSOX, C-X-C Motif Chemokine 16, CXCLG16, SCYB16, CXCL16.
Product # :
CHM-029Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
CXCL16 Human Recombinant (30-118 a.a.) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 89 amino acids and having a molecular mass of 10kDa.The CXCL16 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL16 protein was lyophilized from a 0.2µm filtered solution in PBS.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to chemoattract mouse CXCR6-transfected mouse BaF3 cells, is less than 12ng/ml.More Info
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Introduction
CXC chemokine ligand 16 (CXCL16) is a type I membrane protein, which contains a non-ELR motif-containing CXC chemokine domain in its extracellular region. Human and Mouse CXCL16 share a 70% a.a. sequence similarity within their chemokine domains and 49% overall a.a. sequence identity. Functional CXCL16 can be dropped from the cell surface as an approximately 35kDa soluble protein. CXCR6 is the functional receptor for CXCL16. CXCL16 functions as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), proposing that CXCL16 may be involved in pathophysiology such as atherogenesis. In addition, CXCL16 induces a strong chemotactic response and calcium mobilization. CXCL16 binds to CXCR6/Bonzo.
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Synonyms
Chemokine (C-X-C Motif) Ligand 16, Scavenger Receptor For Phosphatidylserine And Oxidized Low Density Lipoprotein, Transmembrane Chemokine CXCL16, Small-Inducible Cytokine B16, CXC Chemokine Ligand 16, SR-PSOX, SRPSOX, C-X-C Motif Chemokine 16, CXCLG16, SCYB16, CXCL16.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL16 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 CXCL16 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
NEGSVTGSCY CGKRISSDSP PSVQFMNRLR KHLRAYHRCL YYTRFQLLSW SVCGGNKDPW VQELMSCLDL KECGHAYSGI VAHQKHLLP.
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Background
What is the molecular weight/Mw of CXCL16 HUMAN Protein?
CXCL16 HUMAN Protein has a total Mw of 10kDa.
What is the source or expression system of CXCL16 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL16 HUMAN Protein?
CXCL16 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL16 HUMAN Protein?
The ED50, as measured by its ability to chemoattract mouse CXCR6-transfected mouse BaF3 cells, is less than 12ng/ml.
What is the amino acid sequence of CXCL16 HUMAN Protein?
NEGSVTGSCY CGKRISSDSP PSVQFMNRLR KHLRAYHRCL YYTRFQLLSW SVCGGNKDPW VQELMSCLDL KECGHAYSGI VAHQKHLLP.
What applications can CXCL16 HUMAN Protein be used in?
CXCL16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL16 HUMAN Protein?
The endotoxin level is minimal, CXCL16 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 :
ARL14 HumanDescription:
ADP-Ribosylation Factor-Like 14 Human Recombinant
ADP-ribosylation factor-like protein 14, ADP-ribosylation factor 7, ARL14, ARF7, FLJ22595.
Product # :
PRO-936Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARL14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-192 a.a.) and having a molecular mass of 23.8kDa (Molecular weight on SDS-PAGE will appear higher).ARL14 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARL14 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 40% glycerol, 200mM NaCl and 1mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ADP-ribosylation factor-like 14 (ARL14) is a developmentally regulated member of the ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of Ras-related GTPases. ARL14 is GTPase which recruits MYO1E to MHC class II-containing vesicles via the effector protein C11orf46/ARF7EP and thus controls the movement of these vesicles along the actin cytoskeleton in dendritic cells. MHC-II transport was controlled by the GTPase ARL14/ARF7, which recruits the motor myosin 1E via an effector protein ARF7EP.
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Synonyms
ADP-ribosylation factor-like protein 14, ADP-ribosylation factor 7, ARL14, ARF7, FLJ22595.
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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 MGSLGSKNPQ TKQAQVLLLG LDSAGKSTLL YKLKLAKDIT TIPTIGFNVE MIELERNLSL TVWDVGGQEK MRTVWGCYCE NTDGLVYVVD STDKQRLEES QRQFEHILKN EHIKNVPVVL LANKQDMPGA LTAEDITRMF KVKKLCSDRN WYVQPCCALT GEGLAQGFRK LTGFVKSHMK SRGDTLAFFK QN.
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 :
Noggin MouseDescription:
Noggin Mouse Recombinant
Noggin, SYM1, SYNS1, NOG.
Product # :
CYT-600Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
- More Info
Description
Noggin Mouse Recombinant produced in E.Coli is a non-glycosylated, disulfide-linked protein consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.4 kDa (each chain 23.2 kDa).
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered solution in 30% acetonitrile, 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by inhibiting BMP-4-induced alkaline phosphatase production of murine ATDC5 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg in the presence of 5ng/ml BMP-4.More Info
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Introduction
The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
Noggin, SYM1, SYNS1, NOG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Mouse Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYD
PGFMATSPPEDRPGGGGGPAGGAEDLAELDQLLRQRPSGAMPSEIKG
LEFSEGLAQGKKQRLSKKLRRKLQMWLWSQTFCPVLYAWNDLGSRF
WPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHLTVLRWRCQRRGQR
CGWIPIQYPIISECKCSC.
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 :
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 :
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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 :
CXCL8 Human, HisDescription:
Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8), His Tag
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-345Price :
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Description
Interleukin-8 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 77 amino acids fragment (23-99) and having a total molecular mass of 13.7kDa with an amino-terminal hexahistidine tag. The IL-8 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL8 His is supplied in 10mM Tris-HCl pH 8, 250mM NaCl and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
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 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.
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Background
What is the molecular weight/Mw of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein has a total Mw of 13.7kDa.
What is the source or expression system of CXCL8 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN, HIS Protein?
The biological functionality of CXCL8 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein is composed from 77 amino acids.
What applications can CXCL8 HUMAN, HIS Protein be used in?
CXCL8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL8 HUMAN, HIS 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 :
TFPI HumanDescription:
Tissue Factor Pathway Inhibitor Human Recombinant
Tissue Factor Pathway Inhibitor (Lipoprotein-Associated Coagulation Inhibitor), Extrinsic Pathway Inhibitor, Tissue Factor Pathway Inhibitor, anti-convertin, TFPI1, EPI, LACI, TFI.
Product # :
PRO-1702Price :
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Description
TFPI Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (29-304) and having a molecular mass of 34.3kDa.TFPI is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TFPI solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
TFPI is a protease inhibitor which controls the tissue factor (TF)-dependent pathway of blood coagulation. The coagulation process starts with the creation of a factor VIIa-TF complex, that proteolytically triggers additional proteases (factors IX and X) and eventually results in a fibrin clot. TFPI inhibits the activated factor X and VIIa-TF proteases in an autoregulatory loop. TFPI is glycosylated and predominantly located in the vascular endothelium and plasma in both free forms and complexed with plasma lipoproteins. A number of alternatively spliced transcript variants of this gene have are known, however the full-length nature of several of these variants were not yet established.
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Synonyms
Tissue Factor Pathway Inhibitor (Lipoprotein-Associated Coagulation Inhibitor), Extrinsic Pathway Inhibitor, Tissue Factor Pathway Inhibitor, anti-convertin, TFPI1, EPI, LACI, TFI.
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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 MGSDSEEDEE HTIITDTELP PLKLMHSFCA FKADDGPCKA IMKRFFFNIF TRQCEEFIYG GCEGNQNRFE SLEECKKMCT RDNANRIIKT TLQQEKPDFC FLEEDPGICR GYITRYFYNN QTKQCERFKY GGCLGNMNNF ETLEECKNIC EDGPNGFQVD NYGTQLNAVN NSLTPQSTKV PSLFEFHGPS WCLTPADRGL CRANENRFYY NSVIGKCRPF KYSGCGGNEN NFTSKQECLR ACKKGFIQRI SKGGLIKTKR KRKKQRVKIA YEEIFVKNM.
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 :
PFN1 RatDescription:
Profilin-1 Rat Recombinant
Profilin-1, Profilin I.
Product # :
PRO-2231Price :
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Description
PFN1 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-140 a.a) and having a molecular mass of 17.5kDa. PFN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PFN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Profilin-1 also known as Pfn1 is a ubiquitous actin monomer-binding protein which is a member of the profilin family. Pfn1 significantly enhances skin wound healing in-vitro as well as in-vivo which is mediated by purinergic receptors. Furthermore, Pfn1 is also active in endothelial cell migration and vessel sprouting. Pfn1 is considered to regulate actin polymerization in response to extracellular signals.
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Synonyms
Profilin-1, Profilin I.
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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 MGSHMAGWNA YIDSLMADGT CQDAAIVGYK DSPSVWAAVP GKTFVSITPA EVGVLVGKDR SSFFVNGLTL GGQKCSVIRD SLLQDGEFTM DLRTKSTGGA PTFNVTVTMT AKTLVLLMGK EGVHGGLINK KCYEMASHLR RSQY.
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 :
CARD17 HumanDescription:
Caspase Recruitment Domain Family, Member 17 Human Recombinant
CARD17, Caspase Recruitment Domain Family, Member 17, Caspase recruitment domain-containing protein 17, INCA, Caspase-1 inhibitor INCA, Inhibitory caspase recruitment domain protein.
Product # :
PRO-1688Price :
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Description
CARD17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (1-110) and having a molecular mass of 14.3 kDa.CARD17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CARD17 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Caspase Recruitment Domain Family, Member 17 (CARD17) is a regulator of procaspase-1/CASP1 activation involved in the regulation of the proteolytic maturation of pro-IL-1beta/IL1B and its release throughout inflammation. CARD17 inhibits the release of IL1B in reaction to LPS in monocytes. Though, unlike CASP1, CARD17 do not induce NF-kappa-B activation.
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Synonyms
CARD17, Caspase Recruitment Domain Family, Member 17, Caspase recruitment domain-containing protein 17, INCA, Caspase-1 inhibitor INCA, Inhibitory caspase recruitment domain protein.
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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 MGSMADKVLK EKRKQFIRSV GEGTINGLLG ELLETRVLSQ EEIEIVKCEN ATVMDKARAL LDSVIRKGAP ACQICITYIC EEDSHLAGTL GLSAGPTSGN HLTTQDSQIV LPS.
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 :
GTSF1 HumanDescription:
Gametocyte Specific Factor 1 Human Recombinant
Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.
Product # :
PRO-561Price :
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Description
GTSF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167) and having a molecular mass of 21.7 kDa.GTSF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GTSF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Gametocyte Specific Factor 1 (GTSF1) is a member of the UPF0224 (FAM112) family and contains 1 CHHC-type zinc finger. A key paralog of the GTSF1 gene is GTSF1L.
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Synonyms
Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.
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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 MGSMEETYTD SLDPEKLLQC PYDKNHQIRA CRFPYHLIKC RKNHPDVASK LATCPFNARH QVPRAEISHH ISSCDDRSCI EQDVVNQTRS LRQETLAEST WQCPPCDEDW DKDLWEQTST PFVWGTTHYS DNNSPASNIV TEHKNNLASG MRVPKSLPYV LPWKNNGNAQ.
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 :
MAP1LC3B HumanDescription:
Microtubule-Associated Protein 1 Light Chain 3 Beta Human Recombinant
Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.
Product # :
PRO-076Price :
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Description
MAP1LC3B produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-120a.a.) and having a molecular mass of 16.2kDa.MAP1LC3B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAP1LC3B protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
1mM DTT, 100mM NaCl and 20% glycerol.Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
MAP1LC3B is a member of the MAP1 LC3 family. MAP1LC3B is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, that are involved in microtubule assembly and important for neurogenesis. In addition, MAP1LC3B takes part in formation of autophagosomal vacuoles and is expressed mainly in heart, testis, brain and skeletal muscle.
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Synonyms
Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.
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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 MPSEKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SEKDEDGFLY MVYASQETFG
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 :
RAC2 Human, 189a.aDescription:
Ras-Related C3 Botulinum Toxin Substrate 2 (1-189) Human Recombinant
Ras-related C3 botulinum toxin substrate 2, p21-Rac2, Small G protein, GX, RAC2, HSPC022, EN-7.
Product # :
PRO-719Price :
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Description
RAC2 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 209 amino acids (1- 189 a.a.) and having a molecular mass of 23.3kDa.The RAC2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RAC2 solution contains 20mM Tris-HCl buffer (pH 8.0), 20% Glycerol, 2mM EDTA, 2mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
RAC2 is a small signaling G protein/GTPase which is part of the RAS superfamily of small GTP-binding proteins which regulate cell growth, actin cytoskeletal organization, cell proliferation, survival, cell cycle progression, gene transcription rgulation and the activation of protein kinases. RAC2 cycles between an active gtp-bound and inactive gdp-bound state. In active state, RAC2 binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. RAC2 is involved in the regulation of the nadph oxidase.
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Synonyms
Ras-related C3 botulinum toxin substrate 2, p21-Rac2, Small G protein, GX, RAC2, HSPC022, EN-7.
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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 MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDSKP VNLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVSPASY ENVRAKWFPE VRHHCPSTPI ILVGTKLDLR DDKDTIEKLK EKKLAPITYP QGLALAKEID SVKYLECSAL TQRGLKTVFD EAIRAVLCPQ PTRQQKRAC.
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 :
RELM a MouseDescription:
RELM-alpha Mouse Recombinant
Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.
Product # :
CYT-309Price :
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Shipping Method :
Shipped at Room temp
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Description
Mouse RELM-alpha Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10 kDa. The Mouse RELM-alpha is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Sterile filtered and lyophilized from 0.5mg/ml in 10mM sodium phosphate buffer, pH 7.5.
Purity
Greater than 98% as determined by SDS-PAGE & RP-HPLC.
More Info
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Introduction
Bronchoalveolar lavage fluid from mice with experimentally induced allergic pulmonary inflammation contains a novel 9.4 kDa cysteine-rich secreted protein, RELM-alpha (FIZZ1, found in inflammatory zone). RELM-alpha is a secreted protein that has a restricted tissue distribution with highest levels in adipose tissue stroma. Murine RELM-alpha (FIZZ1) is the founding member of a new gene family including two other murine genes expressed, respectively, in intestinal crypt epithelium (RELM-beta) and white adipose tissue (Resistin), and two related human genes.
RELMalpha inhibits the differentiation of 3T3-L1 preadipocytes into adipocytes but has no effect on proliferation of 3T3-L1 preadipocytes. RELMalpha is able to form heterooligomers with resistin but not RELMbeta. Since RELMalpha is expressed by adipose tissue and it is a secreted factor, our findings suggest that RELMalpha may be involved in the control of the adipogenesis as well as in the process of muscle differentiation.
In the lung, RELM-alpha is induced by hypoxia and was renamed as hypoxia-induced mitogenic factor (HIMF). HIMF strongly activated Akt phosphorylation. The phosphatidylinositol 3-kinase (PI3K) inhibitor LY294002 (10 micromol/L) inhibited HIMF-activated Akt phosphorylation. It also inhibited HIMF stimulated RPSM proliferation. Thus, the PI3K/Akt pathway, at least in part, mediates the proliferative effect of HIMF. Further studies showed that HIMF had angiogenic and vasoconstrictive properties. HIMF increased pulmonary arterial pressure and vascular resistance. Further studies suggest that HIMF regulates apoptosis and may participate in lung alveolarization and maturation. -
Synonyms
Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.
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Physical Appearance
Sterile 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
At 0.1mg/ml of deionized sterile water.
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Amino Acid Sequence
MDETIEIIVE NKVKELLANP ANYPSTVTKT LSCTSVKTMN RWASCPAGMT ATGCACGFAC GSWEIQSGDT CNCLCLLVDW TTARCCQLS.
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 :
s100bb BovineDescription:
s100bb Bovine homodimer
Product # :
PRO-2796Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
s100bb Bovine is suitable for use as a standard in immunoassay and as an immunogen for antiserum production.
Source
Bovine brain tissue.
Formulation
s100bb was lyophilized from 5mM Tris-HCl, pH 7.5, 2mM EDTA and 5mM 2-mercaptoethanol.
Purity
Greater than 95.0% .
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized s100bb homodimer although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution s100bb 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 s100bb in sterile 18MΩ-cm H2O containing 5mM 2- mercaptoethanol not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
S100BB, a member of the S100 family of proteins, is a calcium-binding protein that plays a significant role in various cellular processes, particularly in the central nervous system (CNS). Initially identified as a brain-specific protein, S100BB has captured the attention of researchers due to its involvement in neurological signaling, brain development, and its potential implications in neurological disorders. This research delves into the enigmatic world of S100BB, aiming to uncover its diverse functions, regulatory mechanisms, and its relevance in health and disease.
Discovery and Structural Insights:
S100BB was first discovered in the brain, primarily localized in astrocytes, a type of glial cell in the CNS. Structurally, S100BB is characterized by its EF-hand motifs, allowing it to bind calcium ions, a property crucial for its function. These calcium-binding abilities enable S100BB to participate in intricate cellular signaling pathways, making it a vital player in the dynamic communication within the CNS.
Neurological Signaling and Plasticity:
Within the CNS, S100BB has been implicated in neuronal signaling and synaptic plasticity. It interacts with several target proteins, modulating their activities and influencing processes like neurotransmitter release and neuronal differentiation. Furthermore, S100BB participates in the regulation of intracellular calcium levels, a key factor in neuronal excitability and synaptic transmission. Understanding these roles is vital for unraveling the complexities of neurological function and plasticity.
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 :
NPPA HumanDescription:
Natriuretic Peptide A Human Recombinant
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
Product # :
CYT-1028Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
NPPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-123) containing 106 amino acids including an 8 a.a N-terminal His tag. The total molecular mass is 11.7kDa (calculated).
Source
Escherichia Coli.
Formulation
NPPA filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Natriuretic Peptide A (NPPA) is a part of the natriuretic peptide family and is involved in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. NPPA is synthesized as a great precursor which releases a peptide from the N-terminus with similarity to vasoactive peptide, cardiodilatin, and another peptide from the C-terminus with natriuretic-diuretic activity. In female pregnancy, NPPA is promoting trophoblast invasion and spiral artery remodeling in uterus.
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Synonyms
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
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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
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. NPPA is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHNP MYNAVSNADL MDFKNLLDHL EEKMPLEDEV VPPQVLSEPN EEAGAALSPL PEVPPWTGEV SPAQRDGGAL GRGPWDSSDR SALLKSKLRA LLTAPR.
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 :
SARS Nucleocapsid, 1-49 a.a.Description:
SARS-Associated Coronavirus Nuclecapsid (1-49 a.a.), Recombinant
Product # :
SARS-005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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Description
The E.coli derived recombinant protein contains the Nucleocapsid protein 1-49 amino acids immunodominant regions.
Source
Escherichia Coli.
Formulation
SARS Nucleocaspid protein solution is supplied in PBS.
Purity
Protein is >90% pure as determined SDS-PAGE.
More Info
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Introduction
The SARS Nucleocaspid is a protein that has a crucial structural importance, by making the virions associates with the RNA genome and therefore create a nucleocapsid that has the specific helical form. There has been found 3 different domain structures to the nucleocapsid antigen. This protein contains 3 outer structural proteins, the membrane (M), envelope (E), and spike (S) proteins.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Protein is shipped on ice packs. Upon arrival, Store at -20°C.
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Specificity
Immunoreactive with sera of SARS-infected individuals.
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Purification Method
Purified by proprietary chromatographic technique.
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 :
SPOCK3 MouseDescription:
Sparc/Osteonectin 3 Mouse Recombinant
Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.
Product # :
PRO-2328Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
SPOCK3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 423 amino acids (22-436 a.a.) and having a molecular mass of 47.9kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).SPOCK3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SPOCK3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Testican-3 (Spock3) is a nervous system-expressed heparan sulfate proteoglycan belonging to a subgroup of the BM-40/SPARC/osteonectin family, whose role of in brain development is unclear. Spock3 inhibits the processing of pro-matrix metalloproteinase 2(MMP-2) by MT1-MMP and MT3-MMP. Spock3 is mostly confined to the developmental stage of the brain.
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Synonyms
Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.
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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
AAAAVAVAGG RSDGGNFLDE KQWLTTISQY DKEVGQWNKF RDEVEDDYFR TWNPGKPFDQ ALDPAKDPCL KTKCSRHKVC ITQDAQTALC ISHRRLTHSM KEVGGSHKQW RGLPSSTCKP CPIAYASPVC GSDGHSYSSQ CKLEYQACVL GKQISIKCEG RCPCPSDKSM NIGRNVKRAC
SDLEFREVAN RLRDWFKALH ESGSQNKKTK ALLRPERSRF DTSILPICKD SLGWMFNRLD TNYDLLLDQS ELGSIYLDKN EQCTKAFFNS CDTYKDSLIS NNEWCYCFQR QQDPPCHTEL SNIQKRQGIK KLLGQYIPLC DEDGYYKPTQ CHGSVGQCWC VDRYGNEVVG SRINGVADCA
IDFEISGDFA SGDFREWTDD EGEEDDIMND KDDIEDDDED EGDDDDDGDV HDGYILEHHH HHH
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 :
PDCL HumanDescription:
Phosducin-Like Human Recombinant
Phosducin-like protein, PHLP, DKFZp564M1863.
Product # :
PRO-1141Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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Description
PDCL Human Recombinant produced in E. coli is a single polypeptide chain containing 325 amino acids (1-301) and having a molecular mass of 36.8 kDa.PDCL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PDCL solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Phosducin-like protein (PDCL) is a member of the phosducin family. PDCL is a putative modulator of heterotrimeric G proteins. PDCL shares broad amino acid sequence homology with phosducin, a phosphoprotein expressed in the retina and pineal gland. Both PDCL and phosphoducin regulate G-protein signaling by binding to the beta-gamma subunits of G proteins.
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Synonyms
Phosducin-like protein, PHLP, DKFZp564M1863.
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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 MGSHMTTLDD KLLGEKLQYY YSSSEDEDSD HEDKDRGRCA PASSSVPAEA ELAGEGISVN TGPKGVINDW RRFKQLETEQ REEQCREMER LIKKLSMTCR SHLDEEEEQQ KQKDLQEKIS GKMTLKEFAI MNEDQDDEEF LQQYRKQRME EMRQQLHKGP QFKQVFEISS GEGFLDMIDK EQKSIVIMVH IYEDGIPGTE AMNGCMICLA AEYPAVKFCK VKSSVIGASS QFTRNALPAL LIYKGGELIG NFVRVTDQLG DDFFAVDLEA FLQEFGLLPE KEVLVLTSVR NSATCHSEDS DLEID
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 :
ITGB1BP3 HumanDescription:
Integrin Beta 1 Binding Protein 3 Human Recombinant
Nicotinamide riboside kinase 2, Ribosylnicotinamide kinase 2, Ribosylnicotinic acid kinase 2, ITGB1BP3, MIBP, NRK2, NmR-K 2.
Product # :
PRO-1177Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ITGB1BP3 Human Recombinant produced in E. coli is a single polypeptide chain containing 253 amino acids (1-230) and having a molecular mass of 28.4 kDa.ITGB1BP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ITGB1BP3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Nicotinamide riboside kinase 2 (ITGB1BP3) is a member of the uridine kinase family and NRK subfamily. ITGB1BP3 catalyzes the phosphorylation of nicotinic acid riboside and nicotinamide riboside to create nicotinic acid mononucleotide and nicotinamide mononucleotide. ITGB1BP3 reduces laminin matrix deposition and cell adhesion to laminin, but not to fibronectin. ITGB1BP3 is involved in the regulation of PXN at the protein level and of PXN tyrosine phosphorylation. ITGB1BP3 also has a role in the regulation of terminal myogenesis.
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Synonyms
Nicotinamide riboside kinase 2, Ribosylnicotinamide kinase 2, Ribosylnicotinic acid kinase 2, ITGB1BP3, MIBP, NRK2, NmR-K 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 MGSMKLIVGI GGMTNGGKTT LTNSLLRALP NCCVIHQDDF FKPQDQIAVG EDGFKQWDVL ESLDMEAMLD TVQAWLSSPQ KFARAHGVSV QPEASDTHIL LLEGFLLYSY KPLVDLYSRR YFLTVPYEEC KWRRSTRNYT VPDPPGLFDG HVWPMYQKYR QEMEANGVEV VYLDGMKSRE ELFREVLEDI QNSLLNRSQE SAPSPARPAR TQGPGRGCGH RTARPAASQQ DSM
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 :
CCL13 Human, HisDescription:
Monocyte Chemotactic Protein-4 Human Recombinant (CCL13), His-Tag
CKb10, MCP-4, NCC-1, NCC1, SCYA1, SCYL1, CK-beta-10, Small-inducible cytokine A13.
Product # :
CHM-275Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
MCP4 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 96 amino acids (24-98) and having a molecular mass of 10.8 kDa. The MCP-4 is fused to 21 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The His Tag 0.25mg/ml MCP4 protein solution contains PBS pH-7.4, 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CCL13 chemokine is part of the CC chemokine family (TARC). CCL13 protein induces chemotaxis in monocytes, eosinophils, T lymphocytes, and basophils by binding cell surface G-protein linked chemokine receptors such as CCR2, CCR3 and CCR5. CCL13 is induced by the inflammatory cytokines IL1 & TNFA.
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Synonyms
CKb10, MCP-4, NCC-1, NCC1, SCYA1, SCYL1, CK-beta-10, Small-inducible cytokine A13.
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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. Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQPDALNVPS TCCFTFSSKK ISLQRLKSYV ITTSRCPQKA VIFRTKLGKE ICADPKEKWV QNYMKHLGRK
.AHTLKT -
Background
What is the molecular weight/Mw of CCL13 HUMAN, HIS Protein?
CCL13 HUMAN, HIS Protein has a total Mw of 10.8kDa.
What is the source or expression system of CCL13 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL13 HUMAN, HIS Protein?
CCL13 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL13 HUMAN, HIS Protein?
The biological functionality of CCL13 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL13 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQPDALNVPS TCCFTFSSKK ISLQRLKSYV ITTSRCPQKA VIFRTKLGKE ICADPKEKWV QNYMKHLGRK
.AHTLKT
What applications can CCL13 HUMAN, HIS Protein be used in?
CCL13 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL13 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL13 HUMAN, HIS 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.