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Search results

1000 results found for “Visfatin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    Lysostaphin

    Description:

    Lysostaphin Recombinant

    Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.

    Product # :

    ENZ-269

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • Citations

    Description

    Lysostaphin Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 26.92 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized without any additives.

    Purity

    98% as determined by RP-HPLC.

    Biological Activity

    Assessed by the decrease in turbidity of a suspension of heat-killed Staphylococcus aureus at pH-8, 30°C.  Lysostaphin is a zinc enzyme therefore EDTA is an inhibitory factor.

    Citations

    More Info

    • Introduction

      Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.

    • Synonyms

      Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Lyophilized Lysostaphin although stable at room temperature for 2 weeks, should be stored desiccated below -18°C. Upon reconstitution Lysostaphin can be stored at 4°C up to 3 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Lysostaphin in 20mM sodium acetate, pH 4.5 for optimal stability, which can then be further diluted.

    • Protein content

      Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 2.02 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis RP-HPLC, using a calibrated solution of Lysostaphin as a Reference standard.

    • Specific Activity

      Determined to be 3,540 units/mg.

    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.

    Lysostaphin
  • View Data Sheet

    Name :

    CST6 Human, Active

    Description:

    Cystatin E/M, BioActive Human Recombinant

    Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.

    Product # :

    PRO-2633

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    Description

    CST6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (29-149 a.a.) and having a molecular mass of 15.9kDa.CST6 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CST6 solution (0.5mg/1ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The IC50 value is < 10nM. The inhibitory function of Cystatin 6 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25˚C.

    Citations

    More Info

    • Introduction

      Cystatin E/M or CST6 is part of the cystatin type 2 family. Part of the cystatin type 2 family members can act as cysteine protease inhibitors, whereas cystatin E/M regulates cathepsin B inhibitors and not cathepsin C. cystatin E/M is a protein the when secreted, has an effect on osteogenesis and bone resorption, insulin regulation, response to systemic inflammation & hepatocyte growth factor receptors.

    • Synonyms

      Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MRPQERMVGE LRDLSPDDPQ VQKAAQAAVA SYNMGSNSIY YFRDTHIIKA QSQLVAGIKY FLTMEMGSTD CRKTRVTGDH VDLTTCPLAA GAQQEKLRCD FEVLVVPWQN SSQLLKHNCV QM

    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.

    Cst6 Protein
  • View Data Sheet

    Name :

    DCN Human, Sf9

    Description:

    Decorin Human Recombinant, Sf9

    Decorin, Decorin Proteoglycan, Bone Proteoglycan II, SLRR1B, PG-S2, CSCD, PG40, Dermatan Sulphate Proteoglycans II, Small Leucine-Rich Protein 1B, Proteoglycan Core Protein, DSPG2, PGII, PGS2, Decorin, Bone proteoglycan II, PG-S2, , PG40.

    Product # :

    PRO-2232

    Price :

    Quantity :

    Shipping Method :

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    Description

    DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 335 amino acids (31-359a.a.) and having a molecular mass of 37.1kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). DCN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    DCN protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.

    • Synonyms

      Decorin, Decorin Proteoglycan, Bone Proteoglycan II, SLRR1B, PG-S2, CSCD, PG40, Dermatan Sulphate Proteoglycans II, Small Leucine-Rich Protein 1B, Proteoglycan Core Protein, DSPG2, PGII, PGS2, Decorin, Bone proteoglycan II, PG-S2, , PG40.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      DEASGIGPEV PDDRDFEPSL GPVCPFRCQC HLRVVQCSDL GLDKVPKDLP PDTTLLDLQN NKITEIKDGD FKNLKNLHAL ILVNNKISKV SPGAFTPLVK LERLYLSKNQ LKELPEKMPK TLQELRAHEN EITKVRKVTF NGLNQMIVIE LGTNPLKSSG IENGAFQGMK KLSYIRIADT NITSIPQGLP PSLTELHLDG NKISRVDAAS LKGLNNLAKL GLSFNSISAV DNGSLANTPH LRELHLDNNK LTRVPGGLAE HKYIQVVYLH NNNISVVGSS DFCPPGHNTK KASYSGVSLF SNPVQYWEIQ PSTFRCVYVR SAIQLGNYKH HHHHH.

    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.

    Dcn Human Sf9
  • View Data Sheet

    Name :

    SEPX1 Human

    Description:

    Selenoprotein X 1 Human Recombinant

    Methionine-R-sulfoxide reductase B1, MsrB1, Selenoprotein X, SelX, SEPX1, SELR, SELX, HSPC270, MGC3344.

    Product # :

    PRO-260

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
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    • Citations

    Description

    SEPX1 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 136 amino acids (1-116 a.a.) and having a molecular mass of 14.8kDa. In bacteria, the selenocystein (Sec/U) element is positioned directly following the UGA codon within the reading frame for the selenoprotein so we mutated Sec-95 to Cys. The SEPX1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SEPX1 solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5), 1mM DTT, 0.1mM PMSF, 2mM EDTA and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Methionine sulfoxide reductase B1 (SEPX1 or MSRB1), is a selenoprotein that contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that usually signals translation termination. SEPX1 is a member of the methionine sulfoxide reductase B (MsrB) family, and is expressed in an assortment of adult and fetal tissues. MSRs (Methionine sulfoxide reductases) catalyze the reduction of free and protein-bound methionine sulfoxides to corresponding methionines. The oxidation of methionine by ROS creates a diastereomeric mixture of methionine-S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO). Two separate enzyme families evolved for reduction of these sulfoxides, with methionine-S-sulfoxide reductase (MsrA) being stereospecific for Met-S-SO and methionine-R-sulfoxide reductase (MsrB) for Met-R-SO.

    • Synonyms

      Methionine-R-sulfoxide reductase B1, MsrB1, Selenoprotein X, SelX, SEPX1, SELR, SELX, HSPC270, MGC3344.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSFCSFFGGE VFQNHFEPGV YVCAKCGYEL FSSRSKYAHS SPWPAFTETI HADSVAKRPE HNRSEALKVS CGKCGNGLGH EFLNDGPKPG QSRFCIFSSS LKFVPKGKET SASQGH.

    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.

    Sepx1 Human
  • View Data Sheet

    Name :

    SOST Human

    Description:

    Sclerostin Human Recombinant

    Sclerostin, SOST, CDD, VBCH.

    Product # :

    PRO-1601

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    SOST Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 24-213) containing 200 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 22.8kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    SOST filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.03M Acetate buffer pH-4.0.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

    • Synonyms

      Sclerostin, SOST, CDD, VBCH.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. SOST is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASQGWQAFKNDA TEIIPELGEY PEPPPELENN KTMNRAENGG RPPHHPFETK DVSEYSCREL HFTRYVTDGP CRSAKPVTEL VCSGQCGPAR LLPNAIGRGK WWRPSGPDFR CIPDRYRAQR VQLLCPGGEA PRARKVRLVA SCKCKRLTRF HNQSELKDFG TEAARPQKGR KPRPRARSAK ANQAELENAY.

    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.

    Sost Human
  • View Data Sheet

    Name :

    NRGN Human

    Description:

    Neurogranin Human Recombinant

    hng, RC3, Neurogranin, Ng, NRGN.

    Product # :

    CYT-293

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    Description

    NRGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a.) and having a molecular mass of 10.0kDa (molecular size on SDS-PAGE will appear higher). NRGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NRGN protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH7.0), 30% glycerol 0.1mM PMSF and 1mM EDTA.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Neurogranin (NRGN) is a calmodulin-binding protein which is expressed solely in the brain, mainly in dendritic spines. NRGN is also taking part in the protein kinase C signaling pathway by being a "third messenger" substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. NRGN binds to calmodulin in the absence of calcium. NRGN protein’s phosphorylation by protein kinase C lowers its binding ability.

    • Synonyms

      hng, RC3, Neurogranin, Ng, NRGN.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMDCCTEN ACSKPDDDIL DIPLDDPGAN AAAAKIQASF RGHMARKKIK SGERGRKGPG PGGPGGAGVA RGGAGGGPSG D.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Nrgn Human
  • View Data Sheet

    Name :

    Epigen Human, Sf9

    Description:

    Epigen Human Recombinant, Sf9

    Epithelial mitogen,  EPG, Epithelial Mitogen Homolog (Mouse), Epithelial Mitogen Homolog, ALGV3072, PRO9904, Epigen, EPGN.

    Product # :

    CYT-1038

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    • Citations

    Description

    EPGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 97 amino acids (23-110a.a.) and having a molecular mass of 10.8kDa.EPGN is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    EPGN protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    Epigen-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.

    • Synonyms

      Epithelial mitogen, EPG, Epithelial Mitogen Homolog (Mouse), Epithelial Mitogen Homolog, ALGV3072, PRO9904, Epigen, EPGN.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE KHHHHHH.

    • Background

      What is the molecular weight/Mw of EPIGEN Protein?
      EPIGEN Protein has a total Mw of 10.8kDa.

      What is the source or expression system of EPIGEN Protein?
      Sf9, Insect cells.

      What is the Purity of EPIGEN Protein?
      EPIGEN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of EPIGEN Protein?
      The biological functionality of EPIGEN Protein will be determined in the future.

      What is the amino acid sequence of EPIGEN Protein?
      ADPAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE KHHHHHH.

      What applications can EPIGEN Protein be used in?
      EPIGEN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EPIGEN Protein?
      The endotoxin level is minimal, EPIGEN 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.

    Epgn
  • View Data Sheet

    Name :

    TFB1M Human

    Description:

    Transcription Factor B1, Mitochondrial Human Recombinant

    Dimethyladenosine transferase 1 mitochondrial, Mitochondrial 12S rRNA dimethylase 1, Mitochondrial transcription factor B1, h-mtTFB, h-mtTFB1, hTFB1M, mtTFB1, S-adenosylmethionine-6-N'-N'-adenosyl(rRNA) dimethyltransferase 1, TFB1M, CGI-75, CGI75, mtTFB.

    Product # :

    PRO-903

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    Description

    TFB1M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (28-346 a.a.) and having a molecular mass of 38.8kDa.TFB1M is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TFB1M protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TFB1M is a member of the methyltransferase superfamily. TFB1M is a dimethyltransferase which methylates mitochondrial 12S rRNA at the conserved stem loop. The TFB1M protein also is part of the basal mitochondrial transcription complex and is required for mitochondrial gene expression. TFB1M stimulates transcription independently of the methyltransferase activity.

    • Synonyms

      Dimethyladenosine transferase 1 mitochondrial, Mitochondrial 12S rRNA dimethylase 1, Mitochondrial transcription factor B1, h-mtTFB, h-mtTFB1, hTFB1M, mtTFB1, S-adenosylmethionine-6-N'-N'-adenosyl(rRNA) dimethyltransferase 1, TFB1M, CGI-75, CGI75, mtTFB.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQAAKQLSQN FLLDLRLTDK IVRKAGNLTN AYVYEVGPGP GGITRSILNA DVAELLVVEK DTRFIPGLQM LSDAAPGKLR IVHGDVLTFK VEKAFSESLK RPWEDDPPNV HIIGNLPFSV STPLIIKWLE NISCRDGPFV YGRTQMTLTF QKEVAERLAA NTGSKQRSRL SVMAQYLCNV RHIFTIPGQA FVPKPEVDVG VVHFTPLIQP KIEQPFKLVE KVVQNVFQFR RKYCHRGLRM LFPEAQRLES TGRLLELADI DPTLRPRQLS ISHFKSLCDV YRKMCDEDPQ LFAYNFREEL KRRKSKNEEK EEDDAENYRL.

    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.

    Tfb1M Human
  • View Data Sheet

    Name :

    Calumenin Human

    Description:

    Calumenin Human Recombinant

    CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.

    Product # :

    PRO-2465

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    Description

    Calumenin Human Recombinant produced in E. coli is a single polypeptide chain containing 297 amino acids (20-315) and having a molecular mass of 35kDa. Calumenin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Calumenin solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The IC50 value is < 2.0nM. The inhibitory function of Cystatin 5 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25C.

    Citations

    More Info

    • Introduction

      Calumenin is a calcium-binding protein located in the endoplasmic reticulum (ER) and sarcoplasmic reticulum (SR) of mammalian tissues which plays a role in ER functions as protein folding and sorting. Calumenin belongs to a family of multiple EF-hand proteins (CERC) that include reticulocalbin, ERC-55, and Cab45 and the product of this gene. Calumenin binds 7 calcium ions having low affinity and takes part in such ER functions as protein folding and sorting.

    • Synonyms

      CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MKPTEKKDRV HHEPQLSDKV HNDAQSFDYD HDAFLGAEEA KTFDQLTPEE SKERLGKIVS KIDGDKDGFV TVDELKDWIK FAQKRWIYED VERQWKGHDL NEDGLVSWEE YKNATYGYVL DDPDPDDGFN YKQMMVRDER RFKMADKDGD LIATKEEFTA FLHPEEYDYM KDIVVQETME DIDKNADGFI DLEEYIGDMY SHDGNTDEPE WVKTEREQFV EFRDKNRDGK MDKEETKDWI LPSDYDHAEA EARHLVYESD QNKDGKLTKE EIVDKYDLFV GSQATDFGEA LVRHDEF.

    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.

    Calumenin Human 2
  • View Data Sheet

    Name :

    GFRA1 Human

    Description:

    GDNF Family Receptor Alpha 1 Human Recombinant

    GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.

    Product # :

    CYT-1026

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    Description

    GFRA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 25-423) containing 409 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 46.0kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    GFRA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline pH 7.5 containing 5 % (w/v) trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.

    • Synonyms

      GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • 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. GFRA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.

    • Background

      What is the molecular weight/Mw of GFRA1 Protein?
      GFRA1 Protein has a total Mw of 46kDa.

      What is the source or expression system of GFRA1 Protein?
      HEK293 cells.
      What is the Purity of GFRA1 Protein?
      GFRA1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GFRA1 Protein?
      The biological functionality of GFRA1 Protein will be determined in the future.

      What is the amino acid sequence of GFRA1 Protein?
      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.

      What applications can GFRA1 Protein be used in?
      GFRA1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GFRA1 Protein?
      The endotoxin level is minimal, GFRA1 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.

    Gfra1 Human
  • View Data Sheet

    Name :

    CETN1 Human

    Description:

    Centrin-1 Human Recombinant

    Centrin EF-hand protein 1, calcium binding protein, Caltractin isoform 2, CETN.

    Product # :

    PRO-1104

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    Description

    CETN1 Human Recombinant produced E. coli is a single polypeptide chain containing 196 amino acids (1-172) and having a molecular mass of 22.1kDa.CETN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CETN1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CETN1 is an EF-hand type Ca2+-binding protein. CETN1 is localized to the centrosome of interphase cells, and reorganizes the region of the spindle poles during mitosis, reflecting the dynamic behavior of the centrosome during the cell cycle. CETN1 has a vital part in the determination of centrosome position and isolation, and in the course of microtubule separating.

    • Synonyms

      Centrin EF-hand protein 1, calcium binding protein, Caltractin isoform 2, CETN.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMASGFK KPSAASTGQK RKVAPKPELT EDQKQEVREA FDLFDVDGSG TIDAKELKVA MRALGFEPRK EEMKKMISEV DREGTGKISF NDFLAVMTQK MSEKDTKEEI LKAFRLFDDD ETGKISFKNL KRVANELGEN LTDEELQEMI DEADRDGDGE VNEEEFLRIM KKTSLY

    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.

    Cetn1 Human
  • View Data Sheet

    Name :

    CST3 Mouse, Active

    Description:

    Cystatin-C Mouse Recombinant, Active

    Cystatin-C, Cystatin-3,  Cst3,  CST3    

    Product # :

    PRO-2433

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    Description

    CST3 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 126 amino acids (21-140 a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).CST3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CST3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The IC50 value is < 1.0nM. The inhibitory function of Cystatin 3 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25°C.

    Citations

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3, Cst3, CST3

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA 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.

    Cst3 Mouse Active
  • View Data Sheet

    Name :

    AAMDC Human

    Description:

    Adipogenesis Associated, Mth938 Domain Containing Human Recombinant

    Adipogenesis Associated, Mth938 Domain Containing, Adipogenesis Associated Mth938 Domain-Containing Protein , C11orf67, Chromosome 11 Open Reading Frame 67, Mth938 Domain-Containing Protein, UPF0366 Protein C11orf67, PTD015, CK067,AAMDC.

    Product # :

    PRO-2116

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    Description

    AAMDC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-122 a.a) and having a molecular mass of 15.7 kDa.AAMDC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AAMDC protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adipogenesis Associated, Mth938 Domain Containing, also known as AAMDC is a member of the AAMDC family and takes part in preadipocyte differentiation andadipogenesis.

    • Synonyms

      Adipogenesis Associated, Mth938 Domain Containing, Adipogenesis Associated Mth938 Domain-Containing Protein , C11orf67, Chromosome 11 Open Reading Frame 67, Mth938 Domain-Containing Protein, UPF0366 Protein C11orf67, PTD015, CK067,AAMDC.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMTSPEIA SLSWGQMKVK GSNTTYKDCK VWPGGSRTWD WRETGTEHSP GVQPADVKEV VEKGVQTLVI GRGMSEALKV PSSTVEYLKK HGIDVRVLQT EQAVKEYNAL VAQGVRVGGV FHSTC.

    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.

    Aamdc Human
  • View Data Sheet

    Name :

    NDUFA4 Human

    Description:

    NADH Dehydrogenase1 Alpha Subcomplex 4 Human Recombinant

    NDUFA4, Mitochondrial Complex Associated, NADH-Ubiquinone Oxidoreductase MLRQ Subunit, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4, 9kDa, Complex I 9kDa Subunit, Complex I-MLRQ, CI-MLRQ, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4 (9kD, MLRQ), NADH Dehydrogenase [Ubiquinone] 1 Alpha Subcomplex Subunit 4, CI-9k, MLRQ, Cytochrome c oxidase subunit NDUFA4.

    Product # :

    ENZ-803

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    Description

    NDUFA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 104 amino acids (1-81 a.a) and having a molecular mass of 11.8kDa. NDUFA4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    NDUFA4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NADH Dehydrogenase1 Alpha Subcomplex 4 (NDUFA4) is a member of the complex I 9kDa subunit family. Mammalian complex I of mitochondrial respiratory chain is comprised of 45 different subunits. NDUFA4 protein has NADH dehydrogenase activity and oxidoreductase activity. NDUFA4 transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the NDUFA4 enzyme is assumed to be ubiquinone.

    • Synonyms

      NDUFA4, Mitochondrial Complex Associated, NADH-Ubiquinone Oxidoreductase MLRQ Subunit, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4, 9kDa, Complex I 9kDa Subunit, Complex I-MLRQ, CI-MLRQ, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4 (9kD, MLRQ), NADH Dehydrogenase [Ubiquinone] 1 Alpha Subcomplex Subunit 4, CI-9k, MLRQ, Cytochrome c oxidase subunit NDUFA4.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMLRQIIG QAKKHPSLIP LFVFIGTGAT GATLYLLRLA LFNPDVCWDR NNPEPWNKLG PNDQYKFYSV NVDYSKLKKE RPDF.

    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.

    Ndufa4 Human
  • View Data Sheet

    Name :

    ARL14 Human

    Description:

    ADP-Ribosylation Factor-Like 14 Human Recombinant

    ADP-ribosylation factor-like protein 14, ADP-ribosylation factor 7, ARL14, ARF7, FLJ22595.

    Product # :

    PRO-936

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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.

    Citations

    More Info

    • 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.

    • Synonyms

      ADP-ribosylation factor-like protein 14, ADP-ribosylation factor 7, ARL14, ARF7, FLJ22595.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Arl14 Human
  • View Data Sheet

    Name :

    EIF4H Human

    Description:

    Eukaryotic Translation Initiation Factor 4H Human Recombinant

    Eukaryotic translation initiation factor 4H, eIF-4H, Williams-Beuren syndrome chromosomal region 1 protein, EIF4H, KIAA0038, WBSCR1, WSCR1.

    Product # :

    PRO-1114

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    Description

    EIF4H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-248 a.a) and having a molecular mass of 29.9kDa.EIF4H is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EIF4H protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Eukaryotic translation initiation factor 4H (EIF4H) is a 248 amino acid protein which localizes to the perinuclear region of the cytoplasm and is expressed as 2 isoforms, termed short and long. EIF4H functions to stimulate the initiation of protein synthesis at the level of mRNA employment. EIF4H stimulates the RNA-dependent ATP hydrolysis catalyzed by EIF4A and EIF4B. EIF4H gene defects linked to Williams- Beuren syndrome (WBS), a rare developmental disorder characterized by cardiovascular and musculo-skeletal abnormalities and caused by the deletion of contiguous genes at 7q11.23.

    • Synonyms

      Eukaryotic translation initiation factor 4H, eIF-4H, Williams-Beuren syndrome chromosomal region 1 protein, EIF4H, KIAA0038, WBSCR1, WSCR1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMADFDT YDDRAYSSFG GGRGSRGSAG GHGSRSQKEL PTEPPYTAYV GNLPFNTVQG DIDAIFKDLS IRSVRLVRDK DTDKFKGFCY VEFDEVDSLK EALTYDGALL GDRSLRVDIA EGRKQDKGGF GFRKGGPDDR GMGSSRESRG GWDSRDDFNS
      GFRDDFLGGR GGSRPGDRRT GPPMGSRFRD GPPLRGSNMD FREPTEEERA QRPRLQLKPR TVATPLNQVA NPNSAIFGGA RPREEVVQKE QE.

    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.

    Eif4H Human
  • View Data Sheet

    Name :

    ENSA Human

    Description:

    Endosulfine Alpha Human Recombinant

    ARPP-19e, Alpha endosulfine isoform 3, Alpha-endosulfine, ENSA, MGC4319, MGC8394, MGC78563.

    Product # :

    PRO-772

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    Description

    ENSA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (1-121 a.a.) and having a molecular weight of 15.5kDa. The ENSA is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Endosulfine Alpha protein solution contains 20mM Tris, pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ENSA is an endogenous ligand for sulfonylurea receptor. ENSA reduces K(ATP) channel currents by inhibiting sulfonylurea from binding to the receptor and thus stimulates insulin secretion. Endosulfine Alpha is part of a conserved cAMP-regulated phosphoprotein (ARPP) family. Endosulfine Alpha is an endogenous ligand for the sulfonylurea receptor, ABCC8/SUR1. Endosulfine Alpha is an endogenous regulator of KATP channels. ENSA modulates insulin secretion through the interaction with KATP channel. ENSA is a candidate gene for type 2 diabetes. ENSA is expressed in a wide range of tissues including muscle, brain, and endocrine tissues.

    • Synonyms

      ARPP-19e, Alpha endosulfine isoform 3, Alpha-endosulfine, ENSA, MGC4319, MGC8394, MGC78563.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG SDFLMKRLQK GQKYFDSGDY NMAKAKMKNK QLPSAGPDKN LVTGDHIPTP QDLPQRKSSL VTSKLAGGQV E.

    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.

    Ensa Human
  • View Data Sheet

    Name :

    BDNF Human, His

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant, His Tag

    Brain-Derived Neurotrophic Factor, Neurotrophin, Abrineurin, ANON2, BULN2, Brain-derived neurotrophic factor.

    Product # :

    CYT-881

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    Description

    BDNF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (129-247 a.a) and having a molecular mass of 15.8kDa. BDNF is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BDNF protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    BDNF-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, Neurotrophin, Abrineurin, ANON2, BULN2, Brain-derived neurotrophic factor.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 15.8kDa.

      What is the source or expression system of BDNF Protein?
      Escherichia Coli.

      What is the Purity of BDNF Protein?
      BDNF Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of BDNF Protein?
      The biological functionality of BDNF Protein will be determined in the future.

      What is the amino acid sequence of BDNF Protein?
      MGSSHHHHHH SSGLVPRGSH MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

      What applications can BDNF Protein be used in?
      BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BDNF Protein?
      The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.

    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.

    Bdnf Human His
  • View Data Sheet

    Name :

    CCL24 Human

    Description:

    Eotaxin-2 Human Recombinant (CCL24)

    C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    Product # :

    CHM-238

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    Description

    CCL24 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 8.8 kDa. The CCL24 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL24 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM PBS pH-7.4 and 0.15M sodium chloride.

    Purity

    Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

    Citations

    More Info

    • Introduction

      Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
      CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3.

    • Synonyms

      C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CCL24 Human Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKGGVIFTTKKGQQFCG
      DPKQEWV QRYMKNLDAKQKKASPRARAVA.

    • Background

      What is the molecular weight/Mw of CCL24 HUMAN Protein?
      CCL24 HUMAN Protein has a total Mw of 8.8kDa.

      What is the source or expression system of CCL24 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL24 HUMAN Protein?
      CCL24 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL24 HUMAN Protein?
      The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

      What is the amino acid sequence of CCL24 HUMAN Protein?
      VVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKGGVIFTTKKGQQFCG
      DPKQEWV QRYMKNLDAKQKKASPRARAVA.

      What applications can CCL24 HUMAN Protein be used in?
      CCL24 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL24 HUMAN Protein?
      The endotoxin level is minimal, CCL24 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL24 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL24 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ccl24 Human
  • View Data Sheet

    Name :

    STIP1 Mouse

    Description:

    Stress-Induced-Phosphoprotein 1 Mouse Recombinant

    Hop, p60, Sti1, STI1, mSTI1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein.

    Product # :

    PRO-2396

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    Description

    STIP1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 563 amino acids (1-543) and having a molecular mass of 64.7kDa. STIP1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The STIP1 solution (1mg/ml) contains 20mM Tris-HCl(pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.

    • Synonyms

      Hop, p60, Sti1, STI1, mSTI1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MEQVNELKEK GNKALSAGNI DDALQCYSEA IKLDPQNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNLQLKE GLQNMEARLA ERKFMNPFNL PNLYQKLEND PRTRSLLSDP TYRELIEQLQ NKPSDLGTKL QDPRVMTTLS VLLGVDLGSM DEEEEAATPP PPPPPKKEPK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDKALKHYDR AKELDPTNMT YITNQAAVHF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PRDAKLYSNR AACYTKLLEF QLALKDCEEC IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR.

    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.

    Stip1 Mouse
  • View Data Sheet

    Name :

    CXCL14 Rat

    Description:

    BRAK (CXCL14) Rat Recombinant

    C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.

    Product # :

    CHM-021

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    Description

    CXCL14 Rat Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL14 was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.

    Citations

    More Info

    • Introduction

      CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.

    • Synonyms

      C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CXCL14 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.

    • Background

      What is the molecular weight/Mw of CXCL14 RAT Protein?
      CXCL14 RAT Protein has a total Mw of 9.4kDa.

      What is the source or expression system of CXCL14 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL14 RAT Protein?
      CXCL14 RAT Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL14 RAT Protein?
      Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.

      What is the amino acid sequence of CXCL14 RAT Protein?
      SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.

      What applications can CXCL14 RAT Protein be used in?
      CXCL14 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL14 RAT Protein?
      The endotoxin level is minimal, CXCL14 RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL14 RAT that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL14 RAT?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cxcl14 Rat
  • View Data Sheet

    Name :

    FAS Human, His

    Description:

    sFas Receptor Human Recombinant, His Tag

    CD95, CD-95, Tumor necrosis factor receptor superfamily member 6, FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95 antigen, FAS, APT1, FAS1, TNFRSF6, APO-1, FASTM, ALPS1A.

    Product # :

    PRO-594

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    Description

    Recombinant FAS antigen/ CD95 purified from E. coli is a single non-glycosilated polypeptide chain containing amino acids 157-335 of Fas antigen. The recombinant CD95 is fused to C-terminal 6-histidine amino acids. The FAS antigen is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    10mM Sodium Phosphate, pH 8.0.

    Purity

    Greater than 95% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FAS / CD95 is a 36kDa transmembrane type I receptor, which belongs to the NF/NGF receptor super-family. It is a potent inducer of apoptosis in cells of the immune system upon interaction with its natural ligand, CD95L. Although the CD95/CD95L system could play a role in tumor regression, tumor cells seem to down-regulate CD95 expression as a mechanism of resistance to CD95L-induced killing by T lymphocytes and NK cells. The Fas antigen is expressed on the surface of various cell types, including activated T and B lymphocytes and T lymphoblastoid cell line. CD95 is also expressed in a broad panel of non-transformed cells outside the immune system.

    • Synonyms

      CD95, CD-95, Tumor necrosis factor receptor superfamily member 6, FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95 antigen, FAS, APT1, FAS1, TNFRSF6, APO-1, FASTM, ALPS1A.

    • Physical Appearance

      Sterile liquid formulation.

    • Stability

      CD95 although stable at 10°C for 5 days, should be stored below -18°C. Please prevent freeze-thaw cycles.

    • Background

      What is the source or expression system of FAS Protein?
      Escherichia Coli.

      What is the Purity of FAS Protein?
      FAS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FAS Protein?
      The biological functionality of FAS Protein will be determined in the future.

      What is the amino acid sequence of FAS Protein?
      FAS Protein is composed from 179 amino acids.

      What applications can FAS Protein be used in?
      FAS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FAS Protein?
      The endotoxin level is minimal, FAS 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.

    Cd95 Human His
  • View Data Sheet

    Name :

    FGF 8 Mouse

    Description:

    Fibroblast Growth Factor-8 Mouse Recombinant

    Fibroblast growth factor 8, FGF-8, Androgen-induced growth factor, AIGF, Heparin-binding growth factor 8, HBGF-8, Fgf8.

    Product # :

    CYT-070

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • Citations

    Description

    FGF-8 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids and having a molecular mass of 28.1kDa.The FGF-8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGF-8 protein was lyophilized from a 0.2µm filtered concentrated solution in 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, as determined by the dose-dependent a cell proliferation assay using NR6R-3T3 mouse fibroblast cells is <25 ng/ml in the presence of 0.1 ug/ml heprin, corresponding to a specific activity of > 4.0×104 units/mg.

    Citations

    More Info

    • Introduction

      FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.

    • Synonyms

      Fibroblast growth factor 8, FGF-8, Androgen-induced growth factor, AIGF, Heparin-binding growth factor 8, HBGF-8, Fgf8.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized FGF-8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR.

    • Background

      What is the molecular weight/Mw of FGF8 Protein?
      FGF8 Protein has a total Mw of 28.1kDa.

      What is the source or expression system of FGF8 Protein?
      Escherichia Coli.

      What is the Purity of FGF8 Protein?
      FGF8 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF8 Protein?
      The ED50, as determined by the dose-dependent a cell proliferation assay using NR6R-3T3 mouse fibroblast cells is <25 ng/ml in the presence of 0.1 ug/ml heprin, corresponding to a specific activity of > 4.0×104 units/mg.

      What is the amino acid sequence of FGF8 Protein?
      QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR.

      What applications can FGF8 Protein be used in?
      FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF8 Protein?
      The endotoxin level is minimal, FGF8 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.

    Fgf 8 Mouse
  • View Data Sheet

    Name :

    TFF1 Human

    Description:

    Trefoil Factor-1 Human Recombinant

    TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.

    Product # :

    CYT-586

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • Citations

    Description

    TFF-1 Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 60 amino acids which includes a 40 amino acid trefoil motif containing 3 conserved intramolecular disulfide bonds and having a total molecular mass of 13.2 kDa. TFF-1 Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Human TFF1 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 150mM NaCl.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.

    Citations

    More Info

    • Introduction

      The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.

    • Synonyms

      TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized TFF1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFY
      PNTIDVPPEEECEF.

    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.

    Tff1 Human
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