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Search results

1000 results found for “asfv”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    CD40 Antibody

    Description:

    CD40, Mouse Anti-Human

    p50, Bp50, CDW40, MGC9013, TNFRSF5, CD40.

    Product # :

    ANT-263

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • formulation
    • More Info
    • Citations

    Formulation

    1mg/ml in PBS (after reconstitution).

    Citations

    More Info

    • Introduction

      CD40 is part of the TNF-receptor superfamily. CD40 is a necessary mediator for vast range of immune and inflammatory responses together with T cell-dependent immunoglobulin class switching, memory B cell growth, and germinal center formation. The transcription factor AKNA regulates the expression of CD40 and its ligand, which is vital for homotypic cell interactions. Adaptor protein TNFR2 interacts with CD40 and serves as a mediator of the signal transduction. The interaction of CD40 and its ligand is crucial for amyloid-beta-induced microglial activation, and thus is thought to be an early event in Alzheimer disease pathogenesis. CD40 is the receptor for TNFSF5/CD40L.

    • Synonyms

      p50, Bp50, CDW40, MGC9013, TNFRSF5, CD40.

    • Solubility

      Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      Activated Human B cells.

    • Ig Subclass

      Mouse IgG1.

    • Clone

      hCD40.

    • Applications

      Staining antibody. For staining, use 10µl/1,000,000 cells.

    • Available Conjugates

      This antibody is also available conjugated to biotin and FITC. For staining with biotin or FITC-conjugated antibody use 5-10µl/106 cells.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.

    • Purification Method

      Protein-A.

    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.

    Cd40 Antibody
  • View Data Sheet

    Name :

    Protein-A/G/L-Cys

    Description:

    Protein A/G/L-Cys Recombinant

    Product # :

    PRO-1934

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    Description

    Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 806 amino acids in total and having a molecular mass of 89.3kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein- A/G/L was lyophilized without any additives.

    Purity

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

    Citations

    More Info

    • Introduction

      The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEE PRARPGSGSG KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAGC.

    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.

    Protein A G L Cys
  • View Data Sheet

    Name :

    ABO Human

    Description:

    ABO Blood Group Human Recombinant

    Histo-blood group ABO system transferase, Fucosylglycoprotein 3-alpha-galactosyltransferase, Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-galactosyltransferase, Histo-blood group A transferase, A transferase, Histo-blood group B transferase, B transferase, NAGAT, ABO, GTB, A3GALNT, A3GALT1.

    Product # :

    ENZ-167

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

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    More Info

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

    Description

    ABO Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (54-354 a.a) and having a molecular mass of 37.4kDa.ABO is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ABO protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 200mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NAGAT (ABO) is a member of the glycosyltransferase 6 family. The ABO protein is the basis of the ABO blood group system and related to the first discovered blood group system, ABO. The allele that is present in an individual determines the blood group. The histo-blood group ABO is comprised of 3 carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity which converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals are deficient of such activity.

    • Synonyms

      Histo-blood group ABO system transferase, Fucosylglycoprotein 3-alpha-galactosyltransferase, Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-galactosyltransferase, Histo-blood group A transferase, A transferase, Histo-blood group B transferase, B transferase, NAGAT, ABO, GTB, A3GALNT, A3GALT1.

    • 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 MAVREPDHLQ RVSLPRMVYP QPKVLTPCRK DVLVVTPWLA PIVWEGTFNI DILNEQFRLQ NTTIGLTVFA IKKYVAFLKL FLETAEKHFM VGHRVHYYVF TDQPAAVPRV TLGTGRQLSV LEVRAYKRWQ DVSMRRMEMI SDFCERRFLS EVDYLVCVDV DMEFRDHVGV EILTPLFGTL HPGFYGSSRE AFTYERRPQS QAYIPKDEGD FYYLGGFFGG SVQEVQRLTR ACHQAMMVDQ ANGIEAVWHD ESHLNKYLLR HKPTKVLSPE YLWDQQLLGW PAVLRKLRFT AVPKNHQAVR NP.

    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.

    Abo Human
  • View Data Sheet

    Name :

    CSTF1 Human, sf9

    Description:

    Cleavage Stimulation Factor 1 Human Recombinant, sf9

    Cleavage Stimulation Factor Subunit 1, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, 50kD, Cleavage Stimulation Factor 50 KDa Subunit, CF-1 50 KDa Subunit, CSTF 50 KDa Subunit, CstF-50, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, 50kDa, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, CstFp50.

    Product # :

    PRO-2436

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

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

    Description

    CSTF1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 437 amino acids (1-431a.a.) and having a molecular mass of 49.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CSTF1 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CSTF1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cleavage stimulation factor subunit 1 (CSTF1) is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. The CSTF1 gene encodes one of three subunits which merge to produce cleavage stimulation factor (CSTF). Like the mammalian G protein beta subunits, CSTF1 contains transducin-like repeats. CSTF1 is one of the numerous factors necessary for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. CSTF1 is responsible for the interaction of CSTF with other factors to create a stable complex on the pre-mRNA.

    • Synonyms

      Cleavage Stimulation Factor Subunit 1, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, 50kD, Cleavage Stimulation Factor 50 KDa Subunit, CF-1 50 KDa Subunit, CSTF 50 KDa Subunit, CstF-50, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, 50kDa, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, CstFp50.

    • 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

      MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR ARFWYRRSTT DHHHHHH.

    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.

    Cstf1 Human Sf9
  • View Data Sheet

    Name :

    CTF1 Human

    Description:

    Cardiotrophin-1 Human Recombinant

    CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.

    Product # :

    CYT-944

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    Description

    Cardiotrophin-1 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids and having a molecular mass of 21.2kDa.The CTF1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CTF-1 protein 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

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 IU/mg.

    Citations

    More Info

    • Introduction

      Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
      CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
      Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
      Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.

    • Synonyms

      CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CTF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF-1 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 CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.

    • Background

      Title: Cardiotrophin-1 Human Recombinant: A Potential Therapeutic Target for Cardiovascular Diseases

      Abstract:


      Cardiotrophin-1 (CT-1) is a cytokine that plays a crucial role in cardiac development and homeostasis. This research paper provides a comprehensive analysis of human recombinant CT-1, focusing on its production, characterization, and potential therapeutic implications in cardiovascular diseases. The paper discusses the significance of CT-1 in cardiac cell survival, hypertrophy, and regeneration. Furthermore, it elucidates the ongoing research and clinical trials exploring the therapeutic potential of recombinant CT-1 in cardiovascular disorders. The information presented in this paper aims to enhance the understanding of human recombinant CT-1 and its utility as a research tool and a potential therapeutic agent for cardiovascular diseases.

      Introduction:


      Cardiotrophin-1 (CT-1) is a member of the interleukin-6 cytokine family, primarily produced by cardiac cells. It exerts its effects by binding to the CT-1 receptor complex, leading to the activation of various signaling pathways. Human recombinant CT-1, produced through genetic engineering techniques, provides researchers with a valuable tool to explore its biological functions and therapeutic potential.

      Production and Characterization:


      Recombinant CT-1 is typically produced using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CT-1.

      Role in Cardiovascular Physiology:


      CT-1 plays a critical role in cardiac cell survival, hypertrophy, and regeneration. It promotes cardiomyocyte growth and survival, contributing to the adaptation of the heart to stress and injury. CT-1 also exhibits angiogenic properties, stimulating the formation of new blood vessels in the heart. These functions make recombinant CT-1 an important tool for studying cardiac physiology and exploring potential therapeutic interventions.

      Therapeutic Implications:


      The dysregulation of CT-1 signaling has been implicated in various cardiovascular diseases, including heart failure, myocardial infarction, and cardiac hypertrophy. Recombinant CT-1 holds promise as a potential therapeutic agent for these conditions. Clinical trials are underway to evaluate the safety and efficacy of CT-1-based therapies, including recombinant CT-1 administration and gene therapy approaches.

      Conclusion:


      Human recombinant CT-1 is a valuable research tool and a potential therapeutic target for cardiovascular diseases. Its production, characterization, and applications in cardiac cell signaling contribute to our understanding of cardiovascular physiology and the development of novel treatments. Continued research and clinical trials exploring the therapeutic potential of recombinant CT-1 hold promise for improving outcomes in patients with cardiovascular disorders.

      What is the molecular weight/Mw of CTF1 Protein?
      CTF1 Protein has a total Mw of 21.2kDa.

      What is the source or expression system of CTF1 Protein?
      Escherichia Coli.

      What is the Purity of CTF1 Protein?
      CTF1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTF1 Protein?
      The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 IU/mg.

      What is the amino acid sequence of CTF1 Protein?
      MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.

      What applications can CTF1 Protein be used in?
      CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTF1 Protein?
      The endotoxin level is minimal, CTF1 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.

    Ctf1 Human
  • View Data Sheet

    Name :

    Activin-A Mouse

    Description:

    Activin-A Mouse Recombinant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-146

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    Description

    Active form Activin-A Murine Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Mouse Activin-A lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.

    Citations

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

      Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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

      Murine INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 26.2 kDa.

      What is the source or expression system of Activin A Protein?
      Ecoli

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

      What is the Biological Activity of Activin A Protein?
      Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000 units/mg.

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

      What is the amino acid sequence of ACTIVIN A Protein?
      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

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

    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.

    Inhba Mouse
  • View Data Sheet

    Name :

    CXCL17 Human, His

    Description:

    VEGF Co-regulated Chemokine 1, His Tag Human Recombinant

    Dcip1, DMC, MGC138300, UNQ473, VCC-1, VCC1, VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein.

    Product # :

    CHM-024

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    Description

    CXCL17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (22-119 a.a) and having a molecular mass of 13.7kDa.CXCL17 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL17 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    SDS-PAGE

    CXCL17 Human, His-SDS-PAGE - Product image 1

    Citations

    More Info

    • Introduction

      Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.

    • Synonyms

      Dcip1, DMC, MGC138300, UNQ473, VCC-1, VCC1, VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein.

    • 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 MSSLNPGVAR GHRDRGQASR RWLQEGGQEC ECKDWFLRAP RRKFMTVSGL PKKQCPCDHF KGNVKKTRHQ RHHRKPNKHS RACQQFLKQC QLRSFALPL.

    • Background

      What is the molecular weight/Mw of CXCL17 HUMAN, HIS Protein?
      CXCL17 HUMAN, HIS Protein has a total Mw of 13.7kDa.

      What is the source or expression system of CXCL17 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL17 HUMAN, HIS Protein?
      CXCL17 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL17 HUMAN, HIS Protein?
      The biological functionality of CXCL17 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL17 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MSSLNPGVAR GHRDRGQASR RWLQEGGQEC ECKDWFLRAP RRKFMTVSGL PKKQCPCDHF KGNVKKTRHQ RHHRKPNKHS RACQQFLKQC QLRSFALPL.

      What applications can CXCL17 HUMAN, HIS Protein be used in?
      CXCL17 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL17 HUMAN, HIS Protein?
      The endotoxin level is minimal, CXCL17 HUMAN, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL17 HUMAN, HIS that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL17 HUMAN, HIS?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Cxcl17 Human His
  • View Data Sheet

    Name :

    ARL6 Human

    Description:

    ADP-Ribosylation Factor-Like 6 Human Recombinant

    ADP-ribosylation factor-like 6, Bardet-Biedl syndrome 3 protein, BBS3, RP55, MGC32934.

    Product # :

    PRO-232

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    Description

    ARL6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-186a.a) and having a molecular mass of 23.2kDa.ARL6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARL6 protein solution (0.5mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.2M NaCl and 5mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARL6 is a member of the ARF family of GTP-binding proteins. ARL6 has a vital part in modulating membrane trafficking and cytoskeletal functions. Mutation in ARL6 is the source of Bardet-Biedl syndrome (BBS3) which is a pleiotropic genetic disorder that causes obesity, photoreceptor degeneration, polydactyly, hypogenitalism, renal abnor-malities and developmental delay.

    • Synonyms

      ADP-ribosylation factor-like 6, Bardet-Biedl syndrome 3 protein, BBS3, RP55, MGC32934.

    • 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 MGLLDRLSVL LGLKKKEVHV LCLGLDNSGK TTIINKLKPS NAQSQNILPT IGFSIEKFKS SSLSFTVFDM SGQGRYRNLW EHYYKEGQAI IFVIDSSDRL RMVVAKEELD TLLNHPDIKH RRIPILFFAN KMDLRDAVTS VKVSQLLCLE NIKDKPWHIC ASDAIKGEGL QEGVDWLQDQ IQTVKT.

    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.

    Arl6 Human
  • View Data Sheet

    Name :

    NRAS Human

    Description:

    Neuroblastoma RAS Viral Oncogene Homolog Human Recombinant

    GTPase NRas, HRAS1, ALPS4, N-ras, NRAS1, NS6, Transforming protein N-Ras.

    Product # :

    PRO-794

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    Description

    NRAS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-186 a.a.) and having a molecular mass of 20.8kDa. The NRAS is purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The NRAS protein solution contains 20mM Tris-HCl pH-7.5, 100mM NaCl, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NRAS binds GDP/GTP and has intrinsic GTPase activity. NRAS is a membrane protein that shuttles between the Golgi apparatus and the plasma membrane. This transport is regulated through palmitoylation and depalmitoylation by the ZDHHC9-GOLGA7 complex. NRAS is activated to a GTP-bound form by a GTPase activating protein and inactivated to a GDP-bound form by a guanine nucleotide-exchange factor. Defects in this NRAS gene result in juvenile myelomonocytic leukemia.

    • Synonyms

      GTPase NRas, HRAS1, ALPS4, N-ras, NRAS1, NS6, Transforming protein N-Ras.

    • 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

      MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG QEEYSAMRDQ YMRTGEGFLC VFAINNSKSF ADINLYREQI KRVKDSDDVP MVLVGNKCDL PTRTVDTKQA HELAKSYGIP FIETSAKTRQ GVEDAFYTLV REIRQYRMKK LNSSDDGTQG CMGLPC.

    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.

    Nras Human
  • View Data Sheet

    Name :

    ENHO Human

    Description:

    Energy Homeostasis Associated Human Recombinant

    Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

    Product # :

    PRO-1569

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    Description

    ENHO Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 34-76) containing 121 amino acids including extra 78 N-terminal amino acids. The total molecular mass is 13.05kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    ENHO filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Energy Homeostasis Associated (ENHO) participates in glucose homeostasis maintenance and lipid metabolism. ENHO is expressed in the liver and the brain. The role of ENHO in obesity or diabetes is studied.

    • Synonyms

      Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

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

    • Amino Acid Sequence

      MGGKSNGEKK YIVGFKQGFK SCAKKEDVIS EKGGKLQKCF KYVDAASATL NEKAVEELKK DPSVAYVEED KLFKALTSCHSRSADVDSLS ESSPNSSPGP CPEKAPPPQK PSHEGSYLLQ P.

    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.

    Enho Human
  • View Data Sheet

    Name :

    OSM Rat

    Description:

    Oncostatin-M Rat Recombinant

    Oncostatin-M, OSM, OncoM.

    Product # :

    CYT-169

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    Description

    OSM Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 214 amino acids and having a molecular mass of 24.3kDa.The OSM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, 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 stimulation of the proliferation of rat C6 cells is < 5.0 µg/ml, corresponding to a specific activity of > 200 units/mg.

    Citations

    More Info

    • Introduction

      Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

    • Synonyms

      Oncostatin-M, OSM, OncoM.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      KRGCSSSSPK LLSQLKSQAN ITGNTASLLE PYILHQNLNT LTLRAACTEH PVAFPSEDML RQLSKPDFLS TVHATLGRVW HQLGAFRQQF PKIQDFPELE RARQNIQGIR NNVYCMARLL HPPLEIPEPT QADSGTSRPT TTAPGIFQIK IDSCRFLWGY HRFMGSVGRV FEEWGDGSRR SR RHSPLWAW LKGDHRIRPS RSSQSAMLRS LVPR.

    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.

    Osm Rat
  • View Data Sheet

    Name :

    SVIP Human

    Description:

    Small VCP/P97-Interacting Protein Human Recombinant

    Small VCP/P97-Interacting Protein, SVIP.

    Product # :

    PRO-472

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    Description

    SVIP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 100 amino acids (1-77) and having a molecular mass of 10.8 kDa.SVIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SVIP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Small VCP/p97-interacting protein (SVIP) is involved in various cellular processes, including membrane fusion and ubiquitin-dependent protein degradation. SVIP functions as an inhibitor of the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. On the other hand, SVIP overexpression increased the levels of p62 protein and enhanced starvation-activated autophagy as well as stimulated sequestration of polyubiquitinated proteins and p62 in autophagosomes.

    • Synonyms

      Small VCP/P97-Interacting Protein, SVIP.

    • 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 MGSMGLCFPC PGESAPPTPD LEEKRAKLAE AAERRQKEAA SRGILDVQSV QEKRKKKEKI EKQIATSGPP PEGGLRWTVS.

    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.

    Svip Human
  • View Data Sheet

    Name :

    PDGF A Human

    Description:

    Platelet-Derived Growth Factor A Human Recombinant

    Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-A, PDGF-1.

    Product # :

    CYT-491

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    Description

    Platelet-Derived Growth Factor A Human Recombinant short chain produced in E.Coli is a non-glycosylated, polypeptide chain containing 110 amino acids fragment (87-196) and having a total Mw of 17.02kDa, with an amino-terminal hexahistidine tag. PDGF-A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Platelet-derived Growth Factor A is supplied in 25mM Na-Acetate, pH-4.8, 1mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The term ‘PDGF’ refers to a family of disulphide bond-linked dimeric isoforms that act as autocrine and paracrine growth factors and are produced by a variety of cell types other than platelets.
      They act as potent mitogens for almost all mesenchymally-derived cells. Aberrant expression is involved in certain cancers, fibroproliferative disorders and atherosclerosis. The protein also contributes to wound healing and neural regeneration. There are four members of the PDGF family – PDGF A, PDGF B, PDGF C and PDGF D. Two distinct types of PDGF-A exist – a short form that is soluble and a long form that is retained by the extracellular matrix.

    • Synonyms

      Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-A, PDGF-1.

    • 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. Please avoid freeze thaw cycles.

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

    Pdgf A Human
  • View Data Sheet

    Name :

    FGF22 Human

    Description:

    Fibroblast Growth Factor-22 Human Recombinant

    Fibroblast growth factor 22, FGF-22.

    Product # :

    CYT-428

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    Description

    Fibroblast Growth Factor-22 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids and having a molecular mass of 17.3 kDa. The FGF-22 is purified by chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile protein powder is lyophilized with no additives.

    Purity

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

    Citations

    More Info

    • Introduction

      FGF22 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. The mouse homolog of this gene was found to be preferentially expressed in the inner root sheath of the hair follicle, which suggested a role in hair development.

    • Synonyms

      Fibroblast growth factor 22, FGF-22.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized Fibroblast Growth Factor 22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-22 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 Fibroblast Growth Factor-22 sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MTPSASRGPR SYPHLEGDVR WRRLFSSTHF FLRVDPGGRV QGTRWRHGQD SILEIRSVHV GVVVIKAVSS GFYVAMNRRG RLYGSRLYTV DCRFRERIEE NGHNTYASQR WRRRGQPMFL ALDRRGGPRP GGRTRRYHLS AHFLPVLVS.

    • Background

      What is the molecular weight/Mw of FGF22 HUMAN Protein?
      FGF22 HUMAN Protein has a total Mw of 17.3kDa.

      What is the source or expression system of FGF22 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of FGF22 HUMAN Protein?
      FGF22 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF22 HUMAN Protein?
      The biological functionality of FGF22 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of FGF22 HUMAN Protein?
      MTPSASRGPR SYPHLEGDVR WRRLFSSTHF FLRVDPGGRV QGTRWRHGQD SILEIRSVHV GVVVIKAVSS GFYVAMNRRG RLYGSRLYTV DCRFRERIEE NGHNTYASQR WRRRGQPMFL ALDRRGGPRP GGRTRRYHLS AHFLPVLVS.

      What applications can FGF22 HUMAN Protein be used in?
      FGF22 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF22 HUMAN Protein?
      The endotoxin level is minimal, FGF22 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.

    Fgf22 Human
  • View Data Sheet

    Name :

    FGFBP Human

    Description:

    Fibroblast Growth Factor Binding Protein 1 Human Recombinant

    Fibroblast Growth Factor Binding Protein 1, FGFBP, HBP17, 17 KDa Heparin-Binding Growth Factor-Binding Protein, 17 KDa HBGF-Binding Protein, FGF-Binding Protein 1, FGF-BP1, FGFBP-1, FGF-BP, Heparin-Binding Growth Factor Binding Protein, Fibroblast Growth Factor-Binding Protein 1, Fibroblast growth factor-binding protein 1.

    Product # :

    CYT-860

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    • Citations

    Description

    FGFBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (24-234 a.a) and having a molecular mass of 26.2kDa. FGFBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGFBP protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    sds-page

    FGFBP Human - Product image 1

    Citations

    More Info

    • Introduction

      Fibroblast Growth Factor Binding Protein 1, also known as FGFBP1 is a secreted fibroblast growth factor carrier protein. FGFBP1 plays a vital part in cell proliferation, differentiation and migration by binding to fibroblast growth factors and potentiating their biological effects on target cells. In addition, FGFBP1 also takes part in tumor growth as an angiogenic switch molecule, furthermore an expression of FGFBP1 has been associated with more than a few types of cancer as well as pancreatic and colorectal adenocarcinoma.

    • Synonyms

      Fibroblast Growth Factor Binding Protein 1, FGFBP, HBP17, 17 KDa Heparin-Binding Growth Factor-Binding Protein, 17 KDa HBGF-Binding Protein, FGF-Binding Protein 1, FGF-BP1, FGFBP-1, FGF-BP, Heparin-Binding Growth Factor Binding Protein, Fibroblast Growth Factor-Binding Protein 1, Fibroblast growth factor-binding protein 1.

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSKKKVKNG LHSKVVSEQK DTLGNTQIKQ KSRPGNKGKF VTKDQANCRW AATEQEEGIS LKVECTQLDH EFSCVFAGNP TSCLKLKDER VYWKQVARNL RSQKDICRYS KTAVKTRVCR KDFPESSLKL VSSTLFGNTK PRKEKTEMSP REHIKGKETT PSSLAVTQTM ATKAPECVED PDMANQRKTA LEFCGETWSS LCTFFLSIVQ DTSC.

    • Background

      What is the molecular weight/Mw of CYT-860 Protein?
      CYT-860 Protein has a total Mw of 26.2kDa.

      What is the source or expression system of CYT-860 Protein?
      Escherichia Coli.

      What is the Purity of CYT-860 Protein?
      CYT-860 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CYT-860 Protein?
      The biological functionality of CYT-860 Protein will be determined in the future.

      What is the amino acid sequence of CYT-860 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSKKKVKNG LHSKVVSEQK DTLGNTQIKQ KSRPGNKGKF VTKDQANCRW AATEQEEGIS LKVECTQLDH EFSCVFAGNP TSCLKLKDER VYWKQVARNL RSQKDICRYS KTAVKTRVCR KDFPESSLKL VSSTLFGNTK PRKEKTEMSP REHIKGKETT PSSLAVTQTM ATKAPECVED PDMANQRKTA LEFCGETWSS LCTFFLSIVQ DTSC.

      What applications can CYT-860 Protein be used in?
      CYT-860 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CYT-860 Protein?
      The endotoxin level is minimal, CYT-860 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.

    Fgfbp Human
  • View Data Sheet

    Name :

    FGFR1 Human

    Description:

    Fibroblast Growth Factor Receptor 1 Fc Chimera Human Recombinant

    FGFR-1, bFGF-R, C-FGR, CD331, fms-related tyrosine kinase 2, Pfeiffer syndrome, CEK, FLG, FLT2, KAL2, BFGFR, FGFBR, HBGFR, FGFR1/FGFR1OP2 FUSION GENE, FGFR1/ZNF198 FUSION GENE, FLG FGFR1/BCR FUSION GENE, FLG protein, FMS-LIKE GENE, N-sam tyrosine kinase, basic fibroblast growth factor receptor 1.

    Product # :

    PKA-230

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    Description

    Soluble FGFR-1a (IIIc) Fc Chimera Human Recombinant fused with Xa cleavage site with the Fc part of human IgG1 produced in baculovirus is a heterodimeric, glycosylated, Polypeptide chain containing 601 amino acids and having a molecular mass of 170 kDa. The FGFR1 is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    CD331 was lyophilized from a concentrated (1 mg/ml) sterile solution containing 1xPBS.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by its ability to inhibit human FGF acidic-dependent proliferation on R1 cells. The ED50 for this effect is typically at 15.0-30.0 ng/ml.

    Citations

    More Info

    • Introduction

      Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.

    • Synonyms

      FGFR-1, bFGF-R, C-FGR, CD331, fms-related tyrosine kinase 2, Pfeiffer syndrome, CEK, FLG, FLT2, KAL2, BFGFR, FGFBR, HBGFR, FGFR1/FGFR1OP2 FUSION GENE, FGFR1/ZNF198 FUSION GENE, FLG FGFR1/BCR FUSION GENE, FLG protein, FMS-LIKE GENE, N-sam tyrosine kinase, basic fibroblast growth factor receptor 1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGFR1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGFR1 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 bFGF-R in sterile PBS not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      RPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQL AESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSS EDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFK CPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYT CIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYS DPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSF EDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEDPRRASIEG RGDPEEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCV VVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWL NGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLT CLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQ QGNVFSCSVMHEALHNHYTQKSLSLSPGK

    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.

    Fgfr1 Human
  • View Data Sheet

    Name :

    FGFR2 Human, His

    Description:

    Fibroblast Growth Factor Receptor-2 Human Recombinant, His Tag

    EC 2.7.10, FGFR-2, BFR-1, CD332, BBDS, CEK3, ECT1, TK14, TK25, CFD1, KSAM, JWS, Fibroblast Growth Factor Receptor 2, Keratinocyte Growth Factor Receptor, Bacteria-Expressed Kinase, EC 2.7.10.1, K-SAM, KGFR, BEK, Protein Tyrosine Kinase, Receptor Like 14, BEK Fibroblast Growth Factor Receptor, Craniofacial Dysostosis 1, Jackson-Weiss Syndrome, Pfeiffer Syndrome, Crouzon Syndrome, CD332 Antigen.

    Product # :

    PKA-098

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    Description

    FGFR2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 596 amino acids (22-378a.a.) and having a molecular mass of 66.6kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).FGFR2 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    FGFR2 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.

    • Synonyms

      EC 2.7.10, FGFR-2, BFR-1, CD332, BBDS, CEK3, ECT1, TK14, TK25, CFD1, KSAM, JWS, Fibroblast Growth Factor Receptor 2, Keratinocyte Growth Factor Receptor, Bacteria-Expressed Kinase, EC 2.7.10.1, K-SAM, KGFR, BEK, Protein Tyrosine Kinase, Receptor Like 14, BEK Fibroblast Growth Factor Receptor, Craniofacial Dysostosis 1, Jackson-Weiss Syndrome, Pfeiffer Syndrome, Crouzon Syndrome, CD332 Antigen.

    • 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

      RPSFSLVEDT TLEPEEPPTK YQISQPEVYV AAPGESLEVR CLLKDAAVIS WTKDGVHLGP NNRTVLIGEY LQIKGATPRD SGLYACTASR TVDSETWYFM VNVTDAISSG DDEDDTDGAE DFVSENSNNK RAPYWTNTEK MEKRLHAVPA ANTVKFRCPA GGNPMPTMRW LKNGKEFKQE HRIGGYKVRN QHWSLIMESV VPSDKGNYTC VVENEYGSIN HTYHLDVVER SPHRPILQAG LPANASTVVG GDVEFVCKVY SDAQPHIQWI KHVEKNGSKY GPDGLPYLKV LKHSGINSSN AEVLALFNVT EADAGEYICK VSNYIGQANQ SAWLTVLPKQ QAPGREKEIT ASPDYLELEP 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.

    Fgfr2 Protein
  • View Data Sheet

    Name :

    KGF 2 His Human

    Description:

    Keratinocyte Growth Factor-2 Human Recombinant, His Tag

    FGFA, FGF10, FGF-10, KGF-2, Fibroblast growth factor 10.

    Product # :

    CYT-129

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    Description

    KGF 2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (38-208) and having a molecular mass of 22.0kDa.KGF 2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The KGF 2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl 2mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      KGF-2 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. FGF-10 exhibits mitogenic activity for keratinizing epidermal cells, but essentially no activity for fibroblasts, which is similar to the biological activity of FGF7. Studies of the mouse homolog of suggested that this gene is required for embryonic epidermal morphogenesis including brain development, lung morphogenesis, and initiation of lim bud formation. This gene is also implicated to be a primary factor in the process of wound healing.

    • Synonyms

      FGFA, FGF10, FGF-10, KGF-2, Fibroblast growth factor 10.

    • 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 MGSHMQALGQ DMVSPEATNS SSSSFSSPSS AGRHVRSYNH LQGDVRWRKL FSFTKYFLKI EKNGKVSGTK KENCPYSILE ITSVEIGVVA VKAINSNYYL AMNKKGKLYG SKEFNNDCKL KERIEENGYN TYASFNWQHN GRQMYVALNG KGAPRRGQKT RRKNTSAHFL PMVVHS

    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.

    Kgf 2 His Human
  • View Data Sheet

    Name :

    TNF b Human, His

    Description:

    Tumor Necrosis Factor-Beta Human Recombinant, His Tag

    Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.

    Product # :

    CYT-495

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    Description

    TNF-b Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (35-205 a.a.) and having a molecular mass of 20.9kDa. TNF-b is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNF-b protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D. The ED50 for this effect is <0.3 ng/ml.

    Citations

    More Info

    • Introduction

      TNF-b is a potent multifunctional cytokine produced mainly by activated T and B lymphocytes. The protein has been shown to have a specific potent cytotoxic activity on tumor cells and a variety of other target cells as well as being a mediator of inflammation and immune function.

    • Synonyms

      Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.

    • 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 MLPGVGLTPS AAQTARQHPK MHLAHSTLKP AAHLIGDPSK QNSLLWRANT DRAFLQDGFS LSNNSLLVPT SGIYFVYSQV VFSGKAYSPK ATSSPLYLAH EVQLFSSQYP FHVPLLSSQK MVYPGLQEPW LHSMYHGAAF QLTQGDQLST HTDGIPHLVL SPSTVFFGAF AL.

    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.

    Tnf Beta Human His
  • View Data Sheet

    Name :

    TROVE2 Bovine

    Description:

    TROVE Domain Family, Member 2, Bovine

    60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

    Product # :

    PRO-111

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    Description

    TROVE2 is a natural protein having a molecular mass of 60kDa. TROVE2 is purified from bovine tissues by protein-chemical methods.

    Source

    Bovine tissues.

    Formulation

    TROVE2 is supplied in 20mM Tris/HCl buffer pH-7.5, 150mM NaCl, 2mM MgCl2, 0.2mM DTT, 0.1mM PMSF and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.

    • Synonyms

      60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.

    • coating concentration

      0.2-0.6 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.

    • Applications

      Western blot with SLE sera (secondary Sjogren’s syndrome).

    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.

    Trove2 Bovine
  • View Data Sheet

    Name :

    LIFR Mouse

    Description:

    Leukemia Inhibitory Factor Receptor Alpha Mouse Recombinant

    Leukemia inhibitory factor receptor, LIF receptor, LIF-R, D-factor/LIF receptor, CD118, CD antigen, leukemia inhibitory factor receptor isoform 1 precursor, Lifr.

    Product # :

    CYT-1170

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    Description

    LIFR Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 794 amino acids (44-828 aa) and having a molecular mass of 89.6kDa.LIFR is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    LIFR protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit proliferation using TF-1 human erythroleukemic cells. The ED50 range ≤ 1ug/ml with Mouse LIF.

    Citations

    More Info

    • Introduction

      Leukemia Inhibitory Factor Receptor Alpha or LIFR is a protein, part of the Interleukin-6 receptor group of proteins. As such, LIFR acts as a mediator for various proteins (IL-6, IL-11, IL-27, Oncostatin M etc). LIFR has many functions as a cytokine, he has an affect on the cell proliferation, differentiation and survival in the different stages of life. In different types of breast cancer LIFR is down regulated, and as such, can be used as a prognostic tool.

    • Synonyms

      Leukemia inhibitory factor receptor, LIF receptor, LIF-R, D-factor/LIF receptor, CD118, CD antigen, leukemia inhibitory factor receptor isoform 1 precursor, Lifr.

    • 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

      ADPLKRGVQD LKCTTNNMRV WDCTWPAPLG VSPGTVKDIC IKDRFHSCHP LETTNVKIPA LSPGDHEVTI NYLNGFQSKF TLNEKDVSLI PETPEILDLS ADFFTSSLLL KWNDRGSALP HPSNATWEIK VLQNPRTEPV ALVLLNTMLS GKDTVQHWNW TSDLPLQCAT HSVSIRWHID SPHFSGYKEW SDWSPLKNIS WIRNTETNVF PQDKVVLAGS NMTICCMSPT KVLSGQIGNT LRPLIHLYGQ TVAIHILNIP VSENSGTNII FITDDDVYGT VVFAGYPPDV PQKLSCETHD LKEIICSWNP GRITGLVGPR NTEYTLFESI SGKSAVFHRI EGLTNETYRL GVQMHPGQEI HNFTLTGRNP LGQAQSAVVI NVTERVAPHD PTSLKVKDIN STVVTFSWYL PGNFTKINLL CQIEICKANS KKEVRNATIR GAEDSTYHVA VDKLNPYTAY TFRVRCSSKT FWKWSRWSDE KRHLTTEATP SKGPDTWREW SSDGKNLIVY WKPLPINEAN GKILSYNVSC SLNEETQSVL EIFDPQHRAE IQLSKNDYII SVVARNSAGS SPPSKIASME IPNDDITVEQ AVGLGNRIFL TWRHDPNMTC DYVIKWCNSS RSEPCLLDWR KVPSNSTETV IESDQFQPGV RYNFYLYGCT NQGYQLLRSI IGYVEELAPI VAPNFTVEDT SADSILVKWD DIPVEELRGF LRGYLFYFQK GERDTPKTRS LEPHHSDIKL KNITDISQKT LRIADLQGKT SYHLVLRAYT HGGLGPEKSM FVVTKENSHH HHHH.

    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.

    Lifr Mouse
  • View Data Sheet

    Name :

    CLMP Human, SF9

    Description:

    CXADR-Like Membrane Protein, Sf9 Human Recombinant

    CXADR like membrane protein, ACAM, ASAM, CSBM, CSBS, Adipocyte adhesion molecule, Coxsackie- and adenovirus receptor-like membrane protein, CAR-like membrane protein.

    Product # :

    PRO-2519

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    Description

    CLMP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 226 amino acids (19-235a.a.) and having a molecular mass of 25.6kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CLMP is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CLMP protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4), 1mM DTT and 20%glycerol

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CXADR Like Membrane Protein or CLMP, part of the CTX family within the immunoglobulin superfamily, is a type 1 transmembrane peptide. CLMP is expressed in the placenta and small intensine, skeletal muscle, colon, lungs and heart. CLMP is located in junction complexes across endothelial and epithelial cells and can take part in cell adhesion. The protein has influence on development of obesity via adipocyte differentiation.

    • Synonyms

      CXADR like membrane protein, ACAM, ASAM, CSBM, CSBS, Adipocyte adhesion molecule, Coxsackie- and adenovirus receptor-like membrane protein, CAR-like membrane protein.

    • 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

      ADPTHTEIKR VAEEKVTLPC HHQLGLPEKD TLDIEWLLTD NEGNQKVVIT YSSRHVYNNL TEEQKGRVAF ASNFLAGDAS LQIEPLKPSD EGRYTCKVKN SGRYVWSHVI LKVLVRPSKP KCELEGELTE GSDLTLQCES SSGTEPIVYY WQRIREKEGE DERLPPKSRI DYNHPGRVLL
      QNLTMSYSGL YQCTAGNEAG KESCVVRVTV QYVQSIGMVA 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.

    Clmp Protein
  • View Data Sheet

    Name :

    VAT1 Human

    Description:

    Vesicle Amine Transport Protein 1 Homolog Human Recombinant

    Synaptic vesicle membrane protein VAT-1 homolog, VAT1, VATI.

    Product # :

    PRO-1011

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    Description

    VAT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 413 amino acids (1-393 a.a.) and having a molecular mass of 44.1kDa. VAT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    VAT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Synaptic vesicle membrane protein VAT-1 homolog (VAT1) is a member of the quinone oxidoreductase subfamily of zinc-containing alcohol dehydrogenase proteins. Synaptic vesicles are in charge of regulating the storage and release of neurotransmitters in the nerve terminal. VAT1 has an increased calcium ion-dependent expression in glioblastomas and on wounding, in basal keratinocytes. VAT1 is an abundant integral membrane protein of cholinergic synaptic vesicles and is believed to be involved in vesicular transport.

    • Synonyms

      Synaptic vesicle membrane protein VAT-1 homolog, VAT1, VATI.

    • 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 MSDEREVAEA ATGEDASSPP PKTEAASDPQ HPAASEGAAA AAASPPLLRC LVLTGFGGYD KVKLQSRPAA PPAPGPGQLT LRLRACGLNF ADLMARQGLY DRLPPLPVTP GMEGAGVVIA VGEGVSDRKA GDRVMVLNRS GMWQEEVTVP SVQTFLIPEA MTFEEAAALL VNYITAYMVL FDFGNLQPGH SVLVHMAAGG VGMAAVQLCR TVENVTVFGT ASASKHEALK ENGVTHPIDY HTTDYVDEIK KISPKGVDIV MDPLGGSDTA KGYNLLKPMG KVVTYGMANL LTGPKRNLMA LARTWWNQFS VTALQLLQAN RAVCGFHLGY LDGEVELVSG VVARLLALYN QGHIKPHIDS VWPFEKVADA MKQMQEKKNV GKVLLVPGPE KEN.

    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.

    Vat1 Human
  • View Data Sheet

    Name :

    CNTF Human, His Active

    Description:

    Ciliary Neurotrophic Factor Human Recombinant, His Tag Active

    Ciliary neurotrophic factor, CNTF, HCNTF.

    Product # :

    CYT-909

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    Description

    CNTF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-200 a.a) and having a molecular mass of 25kDa. CNTF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNTF protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 8.5), 1 mM DTT,30% Glycerol and 0.2M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 1 ug/ml.

    Citations

    More Info

    • Introduction

      CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
      CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

    • Synonyms

      Ciliary neurotrophic factor, CNTF, HCNTF.

    • 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 MAFTEHSPLT PHRRDLCSRS IWLARKIRSD LTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.

    • Background

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 25kDa.

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

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

      What is the Biological Activity of CNTF Protein?
      Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 1 ug/ml.

      What is the amino acid sequence of CNTF Protein?
      MGSSHHHHHH SSGLVPRGSH MAFTEHSPLT PHRRDLCSRS IWLARKIRSD LTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.

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

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

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

    Cntf Human His Active
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