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1000 results found for “gremlin”
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Name :
IGF1 RatDescription:
IGF-1 Rat Recombinant
Somatomedin C, IGF-I, IGFIA, IGF1.
Product # :
CYT-289Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IGF-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.7kDa. IGF-I is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with a 0.2µm filtered concentrated solution in 20mM PBS, pH 7.0.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by a cell proliferation assay using FDC-P1 cells is less than 2.0ng/ml, corresponding to a specific activity of >500,000units/mg.More Info
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Introduction
The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
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Synonyms
Somatomedin C, IGF-I, IGFIA, IGF1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IGF-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFI 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 IGF1 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
GPETLCGAEL VDALQFVCGP RGFYFNKPTG YGSSIRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPTKSA.
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Background
What is the molecular weight/Mw of IGF1 RAT Protein?
IGF1 RAT Protein has a total Mw of 7.7kDa.
What is the source or expression system of IGF1 RAT Protein?
Escherichia Coli.
What is the Purity of IGF1 RAT Protein?
IGF1 RAT Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IGF1 RAT Protein?
The ED50 as determined by a cell proliferation assay using FDC-P1 cells is less than 2.0ng/ml, corresponding to a specific activity of >500,000units/mg.
What is the amino acid sequence of IGF1 RAT Protein?
GPETLCGAEL VDALQFVCGP RGFYFNKPTG YGSSIRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPTKSA.
What applications can IGF1 RAT Protein be used in?
IGF1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGF1 RAT Protein?
The endotoxin level is minimal, IGF1 RAT 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 :
sRANKL (158-316) MouseDescription:
Soluble RANK Ligand (158-316 a.a) Mouse Recombinant
Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf.
Product # :
CYT-958Price :
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Shipped with Ice Packs
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Description
sRANKL Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (158-316 a.a.) and having a molecular mass of 17.9kDa. sRANKL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
sRANKL protein solution (1mg/ml) containing Tris-Hcl buffer pH-8.5 and 0.1M NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to induce osteoclast differentiation of RAW 264.7 mouse monocyte/macrophage cells, is less than 2ng/ml.More Info
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Introduction
RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.
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Synonyms
Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf.
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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
MKPEAQPFAH LTINAASIPS GSHKVTLSSW YHDRGWAKIS NMTLSNGKLR VNQDGFYYLY ANICFRHHET SGSVPTDYLQ LMVYVVKTSI KIPSSHNLMK GGSTKNWSGN SEFHFYSINV GGFFKLRAGE EISIQVSNPS LLDPDQDATY FGAFKVQDID
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 :
ITGB3BP HumanDescription:
Integrin Beta 3 Binding Protein Human Recombinant
CENP-R, CENPR, HSU37139, NRIF3, TAP20, Centromere protein R, Beta-3-endonexin, Integrin beta-3-binding protein, Nuclear receptor-interacting factor 3, ITGB3BP.
Product # :
PRO-1435Price :
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Shipped with Ice Packs
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Description
ITGB3BP Human Recombinant produced in E. coli is a single polypeptide chain containing 239 amino acids (1-216) and having a molecular mass of 27.1kDa. ITGB3BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ITGB3BP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Integrin Beta 3 Binding Protein (ITGB3BP1) is a broadly expressed protein which contains a DD1 or RepD1 domain and an LXXLL motif. ITGB3BP1 functions as a nuclear receptor coactivator while induced by estrogen. ITGB3BP1 is also relates with the CENP-A-CAD complex that is engaged in mitotic progression, the assembly of kinetochore proteins and chromosome segregation. ITGB3BP1 behave s as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit by interfering with the transactivation domain of NFKB1.
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Synonyms
CENP-R, CENPR, HSU37139, NRIF3, TAP20, Centromere protein R, Beta-3-endonexin, Integrin beta-3-binding protein, Nuclear receptor-interacting factor 3, ITGB3BP.
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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 MGSMPFAPVA QARVQWHDFR SLQHLLPAFK RFSCLSLGSS WDYSVKRSLK LDGLLEENSF DPSKITRKKS VITYSPTTGT CQMSLFASPT SSEEQKHRNG LSNEKRKKLN HPSLTESKES TTKDNDEFMM LLSKVEKLSE EIMEIMQNLS SIQALEGSRE LENLIGISCA SHFLKREMQK TKELMTKVNK QKLFEKSTGL PHKASRHLDS YEFLKAILN.
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 :
EGF RatDescription:
Epidermal Growth Factor Rat Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-669Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Epidermal Growth Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6151 Dalton. The Rat EGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Rat EGF was lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.More Info
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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. -
Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Rat EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat EGF 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 Rat EGF in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.
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Background
Pioneering Insights into Epidermal Growth Factor Rat Recombinant: Unraveling Signaling Dynamics and Therapeutic Implications
Abstract:
This research paper delves into the unexplored landscape of Epidermal Growth Factor Rat Recombinant (EGF-RR), delving into its intricate molecular attributes, signaling pathways, and potential therapeutic applications. By employing advanced methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the complex interplay between EGF-RR and cellular responses, offering a new perspective for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) holds a key role in cellular regulation. This paper navigates the intricacies of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and its potential therapeutic implications.
Protein Expression and Purification:
The paper delves into the meticulous engineering of EGF-RR, involving gene optimization for enhanced expression. Protein purification strategies, such as affinity chromatography, are employed to obtain highly purified EGF-RR for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Advanced receptor binding assays elucidate the interaction of EGF-RR with its cognate receptor. By quantifying binding affinities and kinetic rates, the study unveils the nuances of EGF-RR's engagement with its receptor, shedding light on potential structural determinants.
Cellular Signaling Pathways and Functional Responses:
Through in vitro cellular assays, the study unravels the intricate signaling pathways initiated by EGF-RR. Quantitative phosphoproteomic analyses expose the dynamic phosphorylation events triggered by EGF-RR, providing insights into its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Molecular Modeling:
Utilizing advanced bioinformatics tools, molecular dynamics simulations provide a deeper understanding of EGF-RR's interactions with its receptor and potential downstream effectors. Structural modeling unveils the conformational changes driving signaling cascades.
Therapeutic Prospects and Novel Avenues:
The molecular insights into EGF-RR's signaling dynamics open avenues for therapeutic exploration. Targeted interventions harnessing EGF-RR's potential in wound healing and tissue regeneration, as well as its role in modulating cancer microenvironments, emerge as promising prospects.
Challenges and Future Directions:
Despite progress, challenges such as deciphering context-dependent signaling responses remain. Future research should focus on unraveling the intricate cross-talk between different signaling pathways and exploring EGF-RR's role in specific disease contexts.
Conclusion:
In a convergence of advanced methodologies and visionary insights, Epidermal Growth Factor Rat Recombinant emerges as a captivating subject. Its distinctive molecular attributes and complex cellular interplay offer potential avenues for therapeutic interventions, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.1kDa.
What is the source or expression system of EGF RAT Protein?
Escherichia Coli.
What is the Purity of EGF RAT Protein?
EGF RAT Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF RAT Protein?
The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.
What is the amino acid sequence of EGF RAT Protein?
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.
What applications can EGF RAT Protein be used in?
EGF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF RAT Protein?
The endotoxin level is minimal, EGF RAT 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 :
GM-CSF Poricne, HisDescription:
Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant, His Tag
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim
Product # :
CYT-1160Price :
Quantity :
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Shipped with Ice Packs
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Description
GMCSF Poricne Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids (18-144a.a.) and having a molecular mass of 16.6kDa.GMCSF is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GMCSF protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.
More Info
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Introduction
The hematopoietic growth factor GM-CSF or granulocyte macrophage colony-stimulating factor, stimulates the development of neutrophils & macrophages, enhance proliferation and development of early erythroid megakaryocytic & eosinophilic progenitor cells. GM-CSF is secreted from the fibroblasts, monocytes, T-lymphocytes & endothelial cells. This protein blocks the migration of neutrophils & induces the biological activity of mature end-cells.
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Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim
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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 MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK
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Background
What is the molecular weight/Mw of GM-CSF PORCINE, HIS Protein?
GM-CSF PORCINE, HIS Protein has a total Mw of 16.6kDa.
What is the source or expression system of GM-CSF PORCINE, HIS Protein?
Escherichia Coli.
What is the Purity of GM-CSF PORCINE, HIS Protein?
GM-CSF PORCINE, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF PORCINE, HIS Protein?
The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.
What is the amino acid sequence of GM-CSF PORCINE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK
What applications can GM-CSF PORCINE, HIS Protein be used in?
GM-CSF PORCINE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF PORCINE, HIS Protein?
The endotoxin level is minimal, GM-CSF PORCINE, 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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Description:
Treponema pallidum p15 (Partial) Recombinant, His Tag
Product # :
TRP-247Price :
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- sds-page
Description
The E.Coli derived recombinant 6xHis tag fusion protein is a multimer having a molecular mass of 15kDa and contains the Trp. Pallidum p15 immunodominant regions and six histidines fused at the C- terminus.
Source
Escherichia Coli.
Formulation
70mM Tris-HCl pH 8.0, 50mM NaCl, 50% Glycerol, 1.5 M Urea.
Purity
Treponema Pallidum protein is >95% pure as determined by SDS- PAGE.
sds-page
More Info
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Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
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Stability
Treponema Pallidum protein should be stored at 2-8°C. Do NOT freeze.
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Specificity
Immunoreactive with sera of Trp. Pallidum infected individuals.
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Purification Method
Treponema Pallidum protein was 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 :
MFGE8 MouseDescription:
Milk Fat Globule-EGF Factor 8 Protein Mouse Recombinant
Milk fat globule-EGF factor 8 protein, isoform CRA_a, Putative uncharacterized protein, Mfge8, mCG_6301.
Product # :
CYT-1000Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MFGE8 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (23-426a.a.) and having a molecular mass of 46kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).MFGE8 is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
MFGE8 protein solution (0.25mg/ml) contains 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
Milk fat globule-EGF factor 8 protein (Mfge8) is pleiotropic secreted glycoprotein which promotes mammary gland morphogenesis, angiogenesis, and tumor progression. Mfge8 has also an imperative role in tissue homeostasis and the prevention of inflammation. Mfge8 functions as a bridge between phosphatidylserine on apoptotic cells and Integrin alpha V beta 3 on phagocytes, leading to the clearance of apoptotic debris.
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Synonyms
Milk fat globule-EGF factor 8 protein, isoform CRA_a, Putative uncharacterized protein, Mfge8, mCG_6301.
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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
ADLASGDFCD SSLCLNGGTC LTGQDNDIYC LCPEGFTGLV CNETERGPCS PNPCYNDAKC LVTLDTQRGD IFTEYICQCP VGYSGIHCET GCSTQLGMEG GAIADSQISA SSVYMGFMGL QRWGPELARL YRTGIVNAWT ASNYDSKPWI QVNLLRKMRV SGVMTQGASR AGRAEYLKTF KVAYSLDGRK FEFIQDESGG DKEFLGNLDN NSLKVNMFNP TLEAQYIKLY PVSCHRGCTL RFELLGCELH GCSEPLGLKN NTIPDSQMSA SSSYKTWNLR AFGWYPHLGR LDNQGKINAW TAQSNSAKEW LQVDLGTQRQ VTGIITQGAR DFGHIQYVAS YKVAHSDDGV QWTVYEEQGS SKVFQGNLDN NSHKKNIFEK PFMARYVRVL PVSWHNRITL RLELLGCHHH HHH.
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Background
An Insight into Milk Fat Globule-EGF Factor 8 Protein (Mouse Recombinant): Characteristics, Applications, and Future Directions
Abstract
The Milk Fat Globule-EGF Factor 8 (MFG-E8) protein, particularly in its mouse recombinant form, has emerged as a pivotal player in multiple physiological processes. This paper aims to elucidate its unique characteristics, delve into current methodologies employed in its study, and chart the trajectory for future research directions.
Introduction
Milk Fat Globule-EGF Factor 8 (MFG-E8) is a glycoprotein known for its vital role in several cellular processes, including cell signaling, apoptosis, and phagocytosis. The recombinant form of MFG-E8 derived from mouse models offers a valuable tool for researchers in deciphering its biological relevance.
Characteristics of MFG-E8 (Mouse Recombinant)
1. Structural Profile: The MFG-E8 protein harbors EGF-like domains, which enable its participation in numerous cellular signaling events.
2. Expression Spectrum: While originally identified in mammary epithelial cells, its expression spectrum extends to macrophages, dendritic cells, and other tissues.
3. Biochemical Activity: It plays a key role in facilitating the phagocytic clearance of apoptotic cells by bridging these cells to phagocytes.
Methodologies Employed in MFG-E8 Research
1. Production of Recombinant MFG-E8: Using bacterial expression systems, such as E. coli, mouse MFG-E8 DNA is introduced, followed by protein purification techniques like gel filtration chromatography.
2. Assays: The phagocytosis assays employing fluorescently tagged apoptotic cells and phagocytes enable researchers to quantify MFG-E8's effectiveness in apoptotic cell clearance.
3. Immunoblotting: Through SDS-PAGE and Western blotting, the expression and purification of MFG-E8 can be monitored and validated.
4. Knockout Models: MFG-E8 knockout mice models help decipher its in vivo significance, especially concerning its immune-regulatory roles.
Original Ideas & Implications
The potential for MFG-E8, particularly in its mouse recombinant form, to serve as a therapeutic agent in autoimmune disorders remains a tantalizing prospect. Considering its role in apoptotic cell clearance, dysregulation in MFG-E8 might be implicated in the etiology of autoimmune disorders. Thus, targeting this protein therapeutically may pave the way for innovative treatments.
Conclusions & Future Directions
While the recombinant MFG-E8 protein has elucidated much about the biological implications of this protein, the horizon is rife with potential. Future research might focus on its therapeutic potential, particularly in autoimmunity and inflammation.
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 :
vMIP-IIDescription:
MIP-2 Viral Recombinant
MIP-2 Viral, Viral MIP-2, MIP2 Viral, Viral MIP2, Viral Macrophage inflammatory Protein-2.
Product # :
CHM-376Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MIP-2 Viral Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.9 kDa. The MIP-2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 1mg/ml solution containing 20mM Phospahte Buffer, pH 7.4 % 0.15M NaCl.
Purity
Greater than 97.0% as determined by RP-HPLC & SDS-PAGE.
Biological Activity
Determined by the inhibitory effect on monocyte migration response to human MIP1A using a concentration range of 1µg-10µg/ml of viral MIP2 which will inhibit 25ng/ml of human MIP1A.More Info
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Introduction
Viral MIP-2 is closely related to MIP-1α, show amino acid sequence similarity of about 41%. At the amino acid sequence level, Viral MIP-1 and Viral MIP-2 share 48% similarity. Viral MIP-1 and Viral MIP-2 are more closely linked to one another phylogenetically than to other human chemokines, signifying that they have gene duplication within the virus rather than by two independent gene aquisitions. Viral MIP-2 binds to the CCR3 chemokine receptor through which eotaxin and other β chemokines activate eosinophils. Viral MIP-2 activates and chemoattract human eosinphils.
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Synonyms
MIP-2 Viral, Viral MIP-2, MIP2 Viral, Viral MIP2, Viral Macrophage inflammatory Protein-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-2 Viral protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 CXCL2 Viral 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
LGASWHRPDK CCLGYQKRPL PQVLLSSWYP TSQLCSKPGV IFLTKRGRQV
CADKSKDWVK KLMQQLPVTA. -
Background
What is the molecular weight/Mw of VMIP-II Protein?
VMIP-II Protein has a total Mw of 7.9kDa.
What is the source or expression system of VMIP-II Protein?
Escherichia Coli.
What is the Purity of VMIP-II Protein?
VMIP-II Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of VMIP-II Protein?
Determined by the inhibitory effect on monocyte migration response to human MIP1A using a concentration range of 1µg-10µg/ml of viral MIP2 which will inhibit 25ng/ml of human MIP1A.
What is the amino acid sequence of VMIP-II Protein?
LGASWHRPDK CCLGYQKRPL PQVLLSSWYP TSQLCSKPGV IFLTKRGRQV
CADKSKDWVK KLMQQLPVTA.
What applications can VMIP-II Protein be used in?
VMIP-II Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for VMIP-II Protein?
The endotoxin level is minimal, VMIP-II 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 :
SDF 1a Mouse, HisDescription:
Stromal Cell-Derived Factor-1 alpha (CXCL12), Mouse Recombinant, His Tag
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.
Product # :
CHM-323Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SDF 1a Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (22-89 a.a) and having a molecular mass of 10.4kDa. SDF 1a is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SDF 1a protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively. -
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.
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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 MGSKPVSLSY RCPCRFFESH IARANVKHLK ILNTPNCALQ IVARLKNNNR QVCIDPKLKW IQEYLEKALN 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.
- View Data Sheet
Name :
SEMA7A HumanDescription:
Semaphorin 7A Human Recombinant
Semaphorin-7A, CDw108, JMH blood group antigen, John-Milton-Hargen human blood group Ag, Semaphorin-K1, Sema K1, Semaphorin-L, Sema L, CD108.
Product # :
PRO-2506Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SEMA7A produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 846 amino acids (45-648 a.a.) and having a molecular mass of 95.7kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).SEMA7A is expressed with an 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
SEMA7A protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
SEMA7A (semaphorin-7A isoform 1), is a membrane-bound semaphorin which is linked with cell surfaces via a glycosylphosphatidylinositol (GPI) linkage. SEMA7A encourages formation of focal adhesion complexes, activation of the protein kinase PTK2/FAK1 and subsequent phosphorylation of MAPK3 & MAPK1. SEMA7A takes a vital part in integrin-mediated signaling and functions in regulating cell migration as well as immune responses. In addition, SEMA7A promotes the production of proinflammatory cytokines by macrophages & monocytes.
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Synonyms
Semaphorin-7A, CDw108, JMH blood group antigen, John-Milton-Hargen human blood group Ag, Semaphorin-K1, Sema K1, Semaphorin-L, Sema L, CD108.
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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
ADPQGHLRSG PRIFAVWKGH VGQDRVDFGQ TEPHTVLFHE PGSSSVWVGG RGKVYLFDFP EGKNASVRTV NIGSTKGSCL DKRDCENYIT LLERRSEGLL ACGTNARHPS CWNLVNGTVV PLGEMRGYAP FSPDENSLVL FEGDEVYSTI RKQEYNGKIP RFRRIRGESE LYTSDTVMQN PQFIKATIVH QDQAYDDKIY YFFREDNPDK NPEAPLNVSR VAQLCRGDQG GESSLSVSKW NTFLKAMLVC SDAATNKNFN RLQDVFLLPD PSGQWRDTRV YGVFSNPWNY SAVCVYSLGD IDKVFRTSSL KGYHSSLPNP RPGKCLPDQQ PIPTETFQVA DRHPEVAQRV EPMGPLKTPL FHSKYHYQKV AVHRMQASHG ETFHVLYLTT DRGTIHKVVE PGEQEHSFAF NIMEIQPFRR AAAIQTMSLD AERRKLYVSS QWEVSQVPLD LCEVYGGGCH GCLMSRDPYC GWDQGRCISI YSSERSVLQS INPAEPHKEC PNPKPDKAPL QKVSLAPNSR YYLSCPMESR HATYSWRHKE NVEQSCEPGH QSPNCILFIE NLTAQQYGHY FCEAQEGSYF REAQHWQLLP EDGIMAEHLL GHACALALEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
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 :
ANGPTL3 Human, HEKDescription:
Angiopoietin Like Protein 3 Human Recombinant, HEK
Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.
Product # :
CYT-766Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
ANGPTL3 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 17-460) containing a total of 450 amino acids, having a molecular mass of 52.6kDa (calculated) and fused to a 6 aa His tag at C-Terminus.The Human ANGPTL3 is purified by proprietary chromatographic techniques.
Source
HEK 293.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ANGPTL3 and ANGPTL4 are angiopoietin-like proteins secreted and expressed mainly by the liver, their role being the regulation of triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins. During different nutritional states (feeding/fasting) the levels of the circulating triglycerides are regulated by Angptl3 and Angptl4 through differential inhibition of Lipoprotein lipase (LPL) as shown by the experimental data. The molecular structure of ANGPTL3 is similar to that of the angiopoietins (vascular endothelial growth factors). Deletion mutants of human Angiopoietin 5 were used in order to demonstrate that the N-terminal domain (fragment 17-207) and not the C-terminal fibrinogen-like domain (fragment 207-460) increased the plasma triglyceride levels in mice.
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Synonyms
Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.
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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.
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Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product 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
SRIDQDNSSF DSLSPEPKSR FAMLDDVKIL ANGLLQLGHG LKDFVHKTKG QINDIFQKLN IFDQSFYDLS LQTSEIKEEE KELRRTTYKL QVKNEEVKNM SLELNSKLES LLEEKILLQQ KVKYLEEQLT NLIQNQPETP EHPEVTSLKT FVEKQDNSIK DLLQTVEDQY KQLNQQHSQI KEIENQLRRT SIQEPTEISL SSKPRAPRTT PFLQLNEIRN VKHDGIPAEC TTIYNRGEHT SGMYAIRPSN SQVFHVYCDV ISGSPWTLIQ HRIDGSQNFN ETWENYKYGF GRLDGEFWLG LEKIYSIVKQ SNYVLRIELE DWKDNKHYIE YSFYLGNHET NYTLHLVAIT GNVPNAIPEN KDLVFSTWDH KAKGHFNCPE GYSGGWWWHD ECGENNLNGK YNKPRAKSKP ERRRGLSWKS QNGRLYSIKS TKMLIHPTDS ESFEHHHHHH.
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Background
What is the molecular weight/Mw of ANGPTL3 Protein?
ANGPTL3 Protein has a total Mw of 52.6kDa.
What is the source or expression system of ANGPTL3 Protein?
HEK 293.
What is the Purity of ANGPTL3 Protein?
ANGPTL3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPTL3 Protein?
The biological functionality of ANGPTL3 Protein will be determined in the future.
What is the amino acid sequence of ANGPTL3 Protein?
SRIDQDNSSF DSLSPEPKSR FAMLDDVKIL ANGLLQLGHG LKDFVHKTKG QINDIFQKLN IFDQSFYDLS LQTSEIKEEE KELRRTTYKL QVKNEEVKNM SLELNSKLES LLEEKILLQQ KVKYLEEQLT NLIQNQPETP EHPEVTSLKT FVEKQDNSIK DLLQTVEDQY KQLNQQHSQI KEIENQLRRT SIQEPTEISL SSKPRAPRTT PFLQLNEIRN VKHDGIPAEC TTIYNRGEHT SGMYAIRPSN SQVFHVYCDV ISGSPWTLIQ HRIDGSQNFN ETWENYKYGF GRLDGEFWLG LEKIYSIVKQ SNYVLRIELE DWKDNKHYIE YSFYLGNHET NYTLHLVAIT GNVPNAIPEN KDLVFSTWDH KAKGHFNCPE GYSGGWWWHD ECGENNLNGK YNKPRAKSKP ERRRGLSWKS QNGRLYSIKS TKMLIHPTDS ESFEHHHHHH.
What applications can ANGPTL3 Protein be used in?
ANGPTL3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPTL3 Protein?
The endotoxin level is minimal, ANGPTL3 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 :
ANKRA2 HumanDescription:
Ankyrin Repeat Family A2 Human Recombinant
Ankyrin Repeat, Family A (RFXANK-Like), 2, ANKRA, RFXANK-Like Protein 2, Ankyrin Repeat Family A Protein 2, ANKRA2.
Product # :
PRO-2062Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANKRA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313a.a) and having a molecular mass of 36.7kDa. ANKRA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ANKRA2 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Ankyrin Repeat Family A2, also known as ANKRA2 contains 5 ANK repeats. ANKRA2 assist endocytosis by linking megalin to components of the cytoskeleton or endocytic machinery.
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Synonyms
Ankyrin Repeat, Family A (RFXANK-Like), 2, ANKRA, RFXANK-Like Protein 2, Ankyrin Repeat Family A Protein 2, ANKRA2.
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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 MGSMDTSTNL DIGAQLIVEE CPSTYSLTGM PDIKIEHPLD PNSEEGSAQG VAMGMKFILP NRFDMNVCSR FVKSLNEEDS KNIQDQVNSD LEVASVLFKA ECNIHTSPSP GIQVRHVYTP STTKHFSPIK QSTTLTNKHR GNEVSTTPLL ANSLSVHQLA AQGEMLYLAT RIEQENVINH TDEEGFTPLM WAAAHGQIAV VEFLLQNGAD PQLLGKGRES ALSLACSKGY TDIVKMLLDC GVDVNEYDWN GGTPLLYAVH GNHVKCVKML LESGADPTIE TDSGYNSMDL AVALGYRSVQ QVIESHLLKL LQNIKE.
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 :
DGCR6L HumanDescription:
DiGeorge Syndrome Critical Region Gene 6-Like Human Recombinant
Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.
Product # :
PRO-1454Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DGCR6L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a) and having a molecular mass of 27.3kDa.DGCR6L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DGCR6L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 1mM DTT and 250mM Imidazole.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
DiGeorge syndrome critical region 6-like protein (DGCR6L) shares homology with the Drosophila gonadal protein, it is expressed in gonadal tissues and germ cells, and with the human laminin gamma-1 chain which functions in cell attachment and migration. DGCR6L is located in a region of chromosome 22 involved in the DiGeorge syndrome, one aspect of a wider collection of anomalies referred to as the CATCH 22 syndrome. Moreover, it is one of two functional genes encoding nearly identical proteins which have analogous expression patterns.
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Synonyms
Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.
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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 MGSMERYAAA LEEVADGARQ QERHYQLLSA LQSLVKELPS SFQQRLSYTT LSDLALALLD GTVFEIVQGL LEIQHLTEKS LYNQRLRLQN EHRVLRQALR QKHQEAQQAC RPHNLPVVQA AQQRELEAVE HRIREEQRAM DQKIILELDR KVADQQSTLE KAGVAGFYVT TNPQELMLQM NLLELIRKLQ QRGCRAGNAA LGLGGPWQSP AAQCDQKGSP VPP.
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 :
FGF 1 HumanDescription:
Fibroblast Growth Factor-Acidic Human Recombinant
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Product # :
CYT-264Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Fibroblast Growth Factor-acidic Human Recombinant (FGF-1) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids and having a molecular mass of approximately 15.8kDa.The FGF acidic is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of mouse BALB/c 3T3 cells is <0.5 ng/ml, corresponding to a specific activity of > 2,000,000IU/mg.More Info
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Introduction
Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis.
Three alternatively spliced variants encoding different isoforms have been described.
The hep-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors. -
Synonyms
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fibroblast Growth Factor-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-a 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 Fibroblast Growth Factor-acidic in sterile 18MΩ-cm H2O at 4 degrees Celsius at a concentration of 0.1mg-0.25mg per 1ml. Allow sample to sit for 5 min. at 4 degrees, spin to remove precipitant.
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Amino Acid Sequence
MFNLPPGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SVGEVYIKST ETGQYLAMDT DGLLYGSQTP NEECLFLERL EENHYNTYIS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.
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Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 15.8kDa.
What is the source or expression system of FGF 1 Protein?
Escherichia Coli.
What is the Purity of FGF 1 Protein?
FGF 1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF 1 Protein?
The ED50, calculated by the dose-dependant proliferation of mouse BALB/c 3T3 cells is <0.5 ng/ml, corresponding to a specific activity of > 2,000,000IU/mg.
What is the amino acid sequence of FGF 1 Protein?
MFNLPPGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SVGEVYIKST ETGQYLAMDT DGLLYGSQTP NEECLFLERL EENHYNTYIS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.
What applications can FGF 1 Protein be used in?
FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF 1 Protein?
The endotoxin level is minimal, FGF 1 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 :
FSTL1 HumanDescription:
Follistatin Like 1 Human Recombinant
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1.
Product # :
CYT-792Price :
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Shipped with Ice Packs
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- sds-page
Description
FSTL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 309 amino acids (21-308) and having a molecular mass of 34.9 kDa.FSTL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The FSTL1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
FSTL1 protein resembles follistatin, an ACTV-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.
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Synonyms
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1.
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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 MEEELRSKSK ICANVFCGAG RECAVTEKGE PTCLCIEQCK PHKRPVCGSN GKTYLNHCEL HRDACLTGSK IQVDYDGHCK EKKSVSPSAS PVVCYQSNRD ELRRRIIQWL EAEIIPDGWF SKGSNYSEIL DKYFKNFDNG DSRLDSSEFL KFVEQNETAI NITTYPDQEN NKLLRGLCVD ALIELSDENA DWKLSFQEFL KCLNPSFNPP EKKCALEDET YADGAETEVD CNRCVCACGN WVCTAMTCDG KNQKGAQTQT EEEMTRYVQE LQKHQETAEK TKRVSTKEI.
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Background
What is the molecular weight/Mw of FSTL1 HUMAN Protein?
FSTL1 HUMAN Protein has a total Mw of 34.9kDa.
What is the source or expression system of FSTL1 HUMAN Protein?
Escherichia Coli.
What is the Purity of FSTL1 HUMAN Protein?
FSTL1 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of FSTL1 HUMAN Protein?
The biological functionality of FSTL1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of FSTL1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MEEELRSKSK ICANVFCGAG RECAVTEKGE PTCLCIEQCK PHKRPVCGSN GKTYLNHCEL HRDACLTGSK IQVDYDGHCK EKKSVSPSAS PVVCYQSNRD ELRRRIIQWL EAEIIPDGWF SKGSNYSEIL DKYFKNFDNG DSRLDSSEFL KFVEQNETAI NITTYPDQEN NKLLRGLCVD ALIELSDENA DWKLSFQEFL KCLNPSFNPP EKKCALEDET YADGAETEVD CNRCVCACGN WVCTAMTCDG KNQKGAQTQT EEEMTRYVQE LQKHQETAEK TKRVSTKEI.
What applications can FSTL1 HUMAN Protein be used in?
FSTL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FSTL1 HUMAN Protein?
The endotoxin level is minimal, FSTL1 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 :
GAP43 HumanDescription:
Growth Associated Protein 43 Human Recombinant
Growth associated protein 43, Axonal membrane protein GAP-43, Neural phosphoprotein B-50, calmodulin-binding protein P-57, nerve growth-related peptide GAP43, neuromodulin, protein F1, pp46, B-50.
Product # :
PRO-1126Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GAP43 Human Recombinant produced in E. coli is a single polypeptide chain containing 262 amino acids (1-238) and having a molecular mass of 27.3kDa (Molecular size on SDS-PAGE will appear higher).GAP43 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GAP43 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GAP43 is a phosphoprotein of the presynaptic membrane that takes part in synaptic reorganization and neural development. GAP43 is found in large quantities in neuronal growth cones all through the development and axonal regeneration. Additionally, GAP43 is involved in specific regions of the normal adult nervous system and has a vital part in the conservation mechanism of long-term potentiation (LTP).
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Synonyms
Growth associated protein 43, Axonal membrane protein GAP-43, Neural phosphoprotein B-50, calmodulin-binding protein P-57, nerve growth-related peptide GAP43, neuromodulin, protein F1, pp46, B-50.
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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 MGSHMLCCMR RTKQVEKNDD DQKIEQDGIK PEDKAHKAAT KIQASFRGHI TRKKLKGEKK DDVQAAEAEA NKKDEAPVAD GVEKKGEGTT TAEAAPATGS KPDEPGKAGE TPSEEKKGEG DAATEQAAPQ APASSEEKAG SAETESATKA STDNSPSSKA EDAPAKEEPK QADVPAAVTA AAATTPAAED AAAKATAQPP TETGESSQAE ENIEAVDETK PKESARQDEG KEEEPEADQE HA
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 :
TPM2 HumanDescription:
Tropomyosin-2 Human Recombinant
Tropomyosin 2 (beta), DA1, TMSB, DA2B, AMCD1, NEM4, Arthrogryposis Multiplex Congenital Distal-Type 1, beta-Tropomyosin.
Product # :
PRO-069Price :
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Shipping Method :
Shipped with Ice Packs
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Description
TPM2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (1-284a.a.) and having a molecular mass of 35.1kDa(molecular weight on SDS-PAGE will appear higher).TPM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TPM2 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 100mM NaCl and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Tropomyosin beta chain isoform 2 is affiliate to the actin filament binding protein family which primarily expressed in slow, type 1 muscle fibers. Mutations in TPM2 can change the expression of other sarcomeric tropomyosin proteins, and cause cap disease, nemaline myopathy and distal arthrogryposis syndromes.
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Synonyms
Tropomyosin 2 (beta), DA1, TMSB, DA2B, AMCD1, NEM4, Arthrogryposis Multiplex Congenital Distal-Type 1, beta-Tropomyosin.
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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 MDAIKKKMQM LKLDKENAID RAEQAEADKK QAEDRCKQLE EEQQALQKKL KGTEDEVEKY SESVKEAQEK LEQAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA DESERGMKVI ENRAMKDEEK MELQEMQLKE AKHIAEDSDR KYEEVARKLV ILEGELERSE ERAEVAESRA RQLEEELRTM DQALKSLMAS EEEYSTKEDK YEEEIKLLEE KLKEAETRAE FAERSVAKLE KTIDDLEETL ASAKEENVEI HQTLDQTLLE LNNL.
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 :
Leptin Human, HisDescription:
Leptin Human Recombinant, His Tag
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-287Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing amino acids 48-167 and having a total molecular mass of 19 kDa including the 4 kDa His tag.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Leptin is a protein hormone with important effects in regulating body weight, metabolism and reproductive function. The protein is approximately~16 kDa in mass and encoded by the obese (ob)gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus known to be important in regulating body weight, as well as in T lymphocytes and vascular endothelial cells.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature, should be stored desiccated below 0°C. Reconstituted Leptin is best stored refrigerated at 4°C.Please avoid freeze-thaw cycles.
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Solubility
The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.
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 :
GLTPD1 HumanDescription:
Glycolipid Transfer Protein Domain Containing 1 Human Recombinant
Ceramide-1-Phosphate Transfer Protein, Glycolipid Transfer Protein Domain-Containing Protein 1, Glycolipid Transfer Protein Domain Containing 1, GLTP Domain-Containing Protein 1, GLTPD1, GLTPD1, Ceramide-1-phosphate transfer protein, CPTP.
Product # :
PRO-2093Price :
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Description
GLTPD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-214 a.a) and having a molecular mass of 26.8kDa. GLTPD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GLTPD1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 50% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Glycolipid Transfer Protein Domain Containing 1 (GLTPD1) belongs to the GLTP family. GLTPD1 mediates the intracellular transfer of ceramide-1-phosphate between organelle membranes and the cell membrane. GLTPD1 is essential for normal structure of the Golgi stacks. In addition, GLTPD1 is able to bind phosphoceramides with a diversity of aliphatic chains, however GLTPD1 has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains. Moreover, GLTPD1 is inefficient with phosphoceramides which contains lignoceryl (C24:0). GLTPD1 participates in the regulation of the cellular levels of ceramide-1-phosphate, and in that way contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid.
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Synonyms
Ceramide-1-Phosphate Transfer Protein, Glycolipid Transfer Protein Domain-Containing Protein 1, Glycolipid Transfer Protein Domain Containing 1, GLTP Domain-Containing Protein 1, GLTPD1, GLTPD1, Ceramide-1-phosphate transfer protein, CPTP.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDDSETG FNLKVVLVSF KQCLDEKEEV LLDPYIASWK GLVRFLNSLG TIFSFISKDV VSKLRIMERL RGGPQSEHYR SLQAMVAHEL SNRLVDLERR SHHPESGCRT VLRLHRALHW LQLFLEGLRT SPEDARTSAL CADSYNASLA AYHPWVVRRA VTVAFCTLPT REVFLEAMNV GPPEQAVQML GEALPFIQRV YNVSQKLYAE HSLLDLP.
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 :
GSTP2 Mouse, HisDescription:
Glutathione S-Transferase pi 2 Mouse Recombinant, His Tag
Glutathione S-transferase P 2 (EC:2.5.1.18), Gst P2, GST YF-YF, GST class-pi, GST-piA, Gstp2, Gstpia.
Product # :
ENZ-928Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GSTP2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 25.9kDa. GSTP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GSTP2 protein solution (1mg/ml) containing 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
Gltathione S-transferase PI 2, also known as GSTP2 is multifunctional enzyme which is involved in theprotection of cellular components against anti-cancer drugs or peroxidative stress. Furthermore, down regulation of GSTP2induces an increase of oxidative damage in the pyramidal cells of the CA1&CA3 regions as well as in the granular layer ofthe dentate gyrus, which at the end leads to structural and functional damage.
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Synonyms
Glutathione S-transferase P 2 (EC:2.5.1.18), Gst P2, GST YF-YF, GST class-pi, GST-piA, Gstp2, Gstpia.
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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 MGSMPPYTIV YFPSPGRCEA MRMLLADQGQ SWKEEVVTID TWMQGLLKPT CLYGQLPKFE DGDLTLYQSN AILRHLGRSL GLYGKNQREA AQVDMVNDGV EDLRGKYGTM IYRNYENGKN DYVKALPGHL KPFETLLSQN QGGKAFIVGD QISFADYNLL DLLLIHQVLA PGCLDNFPLL SAYVARLSAR PKIKAFLSSP EHVNRPINGN GKQ.
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 :
ZMAT3 HumanDescription:
Zinc Finger, Matrin-Type 3 Human Recombinant
Zinc Finger Matrin-Type 3, Zinc Finger Protein WIG1, P53-Activated Gene 608 Protein, P53 Target Zinc Finger Protein, WIG1.
Product # :
PRO-1635Price :
Quantity :
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Shipped with Ice Packs
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Description
ZMAT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 312 amino acids (1-289) and having a molecular mass of 34.4kDa.ZMAT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ZMAT3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
ZMAT3 is a protein with a nuclear localization signal and 3 zinc finger domains. The mRNA and the protein of this gene are upregulated by wildtype p53. When overexpressed, ZMAT3 can produce tumor cell growth, indicating that ZMAT3 takes part in the p53-dependent growth regulatory pathway. Alternative splicing of ZMAT3 produce two transcript variants encoding two isoforms differing in only one amino acid.
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Synonyms
Zinc Finger Matrin-Type 3, Zinc Finger Protein WIG1, P53-Activated Gene 608 Protein, P53 Target Zinc Finger Protein, WIG1.
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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 MGSMILLQHA VLPPPKQPSP SPPMSVATRS TGTLQLPPQK PFGQEASLPL AGEEELSKGG EQDCALEELC KPLYCKLCNV TLNSAQQAQA HYQGKNHGKK LRNYYAANSC PPPARMSNVV EPAATPVVPV PPQMGSFKPG GRVILATEND YCKLCDASFS SPAVAQAHYQ GKNHAKRLRL AEAQSNSFSE SSELGQRRAR KEGNEFKMMP NRRNMYTVQN NSAGPYFNPR SRQRIPRDLA MCVTPSGQFY CSMCNVGAGE EMEFRQHLES KQHKSKVSEQ RYRNEMENLG YV
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 :
Leptin Human, PEGDescription:
Leptin Human Recombinant, PEG
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1108Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Pegylated Leptin Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Leptin Human Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Biological Activity is < than 0.1% as determined by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It’s in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo it has profound weight reducing effect, resulting mainly from reduced food intake.
More Info
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Introduction
Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pegylated leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution leptin N82K 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 Pegylated leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RHOD HumanDescription:
Ras Homolog Gene Family Member D Human Recombinant
Rho-related GTP-binding protein RhoD, Rho-related protein HP1, RhoHP1, RHOD, ARHD, Rho, RHOM.
Product # :
PRO-190Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RHOD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (18-207 a.a.) and having a molecular mass of 23.8kDa.RHOD is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RHOD solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 50% glycerol, 200mM NaCl, 2mM EDTA and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Rho-related GTP-binding protein (RhoD) is a member of the small GTPase superfamily. The small GTPase Rho D promotes the rearrangement of the actin cytoskeleton and cell surface and also regulates endosome motility and distribution.
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Synonyms
Rho-related GTP-binding protein RhoD, Rho-related protein HP1, RhoHP1, RHOD, ARHD, Rho, RHOM.
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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 MVKVVLVGDG GCGKTSLLMV FADGAFPESY TPTVFERYMV NLQVKGKPVH LHIWDTAGQD DYDRLRPLFY PDASVLLLCF DVTSPNSFDN IFNRWYPEVN HFCKKVPIIV VGCKTDLRKD KSLVNKLRRN GLEPVTYHRG QEMARSVGAV AYLECSARLH
DNVHAVFQEA AEVALSSRGR NFWRRITQGF 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.
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Name :
SPA, HisDescription:
Staphylococcal Protein-A Recombinant, His Tag
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-1925Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SPA Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with 6×His tag at C-terminus. SPA is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 306 amino acids and having a molecular mass of 34.7kDa containing little or no carbohydrate. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding.
Source
Escherichia Coli.
Formulation
SPA protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by:
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA 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 SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE HHHHHH.
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.