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    CTACK (CCL27)

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Search results

1000 results found for “Cytokeratin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    CTACK Human

    Description:

    CTACK Human Recombinant (CCL27)

    ALP, CTACK, ESKINE, ILC, PESKY, SCYA27, CCL27, C-C motif chemokine 27, Small-inducible cytokine A27, IL-11 R-alpha-locus chemokine, Skinkine, ESkine, Cutaneous T-cell-attracting chemokine.

    Product # :

    CHM-373

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    • SDS-PAGE

    Description

    CTACK Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 89 amino acids (25-112 a.a.) and having a molecular mass of 10.3kDa. CTACK protein is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    CTACK Human solution containing 10mM sodium citrate pH-3.5 & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    SDS-PAGE

    CTACK Human-SDS-PAGE - Product image 1

    More Info

    • Introduction

      CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.

    • Synonyms

      ALP, CTACK, ESKINE, ILC, PESKY, SCYA27, CCL27, C-C motif chemokine 27, Small-inducible cytokine A27, IL-11 R-alpha-locus chemokine, Skinkine, ESkine, Cutaneous T-cell-attracting chemokine.

    • 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

      MFLLPPSTAC CTQLYRKPLS DKLLRKVIQV ELQEADGDCH LQAFVLHLAQ RSICIHPQNP SLSQWFEHQE RKLHGTLPKL NFGMLRKMG.

    • Background

      What is the molecular weight/Mw of CTACK HUMAN Protein?
      CTACK HUMAN Protein has a total Mw of 10.3kDa.

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

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

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

      What is the amino acid sequence of CTACK HUMAN Protein?
      MFLLPPSTAC CTQLYRKPLS DKLLRKVIQV ELQEADGDCH LQAFVLHLAQ RSICIHPQNP SLSQWFEHQE RKLHGTLPKL NFGMLRKMG.

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

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

    Ctack Human
  • View Data Sheet

    Name :

    FANK1 Human

    Description:

    Fibronectin Type III And Ankyrin Repeat Domains 1 Human Recombinant

    Fibronectin Type 3 And Ankyrin Repeat Domains 1, 1700007B22Rik.

    Product # :

    PRO-1768

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    Description

    FANK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-345 a.a) and having a molecular mass of 40.7kDa.FANK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FANK1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT, 0.1mM PMSF and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      FANK1 was localized in the nuclei of identical cells in the seminiferous epithelium. Depending on its nuclear localization, a gene ontology analysis proposes that FANK1 has a DNA binding activity therefor operates as a transcription factor. The extremely controlled expression of FANK1, suggests that it takes part in regulating gene expression in the transition from the meiotic phase to the haploid phase throughout spermatogenesis.

    • Synonyms

      Fibronectin Type 3 And Ankyrin Repeat Domains 1, 1700007B22Rik.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMEPQKIM PPSKPHPPVV GKVTHHSIEL YWDLEKKAKR QGPQEQWFRF SIEEEDPKMH TYGIIYTGYA TKHVVEGLEP RTLYRFRLKV TSPSGECEYS PLVSVSTTRE PISSEHLHRA VSVNDEDLLV RILQGGRVKV DVPNKFGFTA LMVAAQKGYT RLVKILVSNG TDVNLKNGSG KDSLMLACYA GHLDVVKYLR RHGASWQARD LGGCTALHWA ADGGHCSVIE WMIKDGCEVD VVDTGSGWTP LMRVSAVSGN QRVASLLIDA GANVNVKDRN GKTPLMVAVL NNHEELVQLL LDKGADASVK NEFGKGVLEM ARVFDRQSVV SLLEERKKKQ RPKKSCVC

    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.

    Fank1 Human
  • View Data Sheet

    Name :

    TBCEL Human

    Description:

    Tubulin Folding Cofactor E-Like Human Recombinant

    Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.

    Product # :

    PRO-030

    Price :

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    • More Info

    Description

    TBCEL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids and having a molecular mass of 50.6kDa. The TBCEL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TBCEL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.

    • Synonyms

      Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.

    • 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 MGSMDQPSGR SFMQVLCEKY SPENFPYRRG PGMGVHVPAT PQGSPMKDRL NLPSVLVLNS CGITCAGDEK EIAAFCAHVS ELDLSDNKLE DWHEVSKIVS NVPQLEFLNL SSNPLNLSVL ERTCAGSFSG VRKLVLNNSK ASWETVHMIL QELPDLEELF LCLNDYETVS CPSICCHSLK LLHITDNNLQ DWTEIRKLGV MFPSLDTLVL ANNHLNAIEE PDDSLARLFP NLRSISLHKS GLQSWEDIDK LNSFPKLEEV RLLGIPLLQP YTTEERRKLV IARLPSVSKL NGSVVTDGER EDSERFFIRY YVDVPQEEVP FRYHELITKY GKLEPLAEVD LRPQSSAKVE VHFNDQVEEM SIRLDQTVAE LKKQLKTLVQ LPTSNMLLYY FDHEAPFGPE EMKYSSRALH SFGIRDGDKI YVESKTK.

    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.

    Tbcel Human
  • View Data Sheet

    Name :

    CKS2 Human

    Description:

    CDC28 Protein Kinase 2 Human Recombinant

    CDC28, CKSHS2, CKS2, CDC28 Protein Kinase 2.

    Product # :

    PKA-258

    Price :

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    • description
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    • More Info

    Description

    CKS2 Human Recombinant fused to T7-Tag produced in E.Coli is a single, non- glycosylated polypeptide chain containing 94 amino acids and having a molecular mass of 11 kDa.

    Source

    Escherichia Coli.

    Formulation

    The CKS2 protein solution contains 20mM Tris-HCl pH-7.5 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CKS2 protein binds to the catalytic subunit of the cyclin dependent kinases and is necessary for their biological function. The CKS2 mRNA is expressed in various patterns through the cell cycle in HeLa cells, which shows spcific role for the encoded protein. CKS2 (CDC28) Protein kinase 2 binds to the catalytic subunit of cyclin-dependent kinases and has thus in involved in cell cycle regulation. CKS2 is required for the first metaphase/anaphase transition during the meiosis. An increase in expression of CKS2 protects the cells from apoptosis. CKS2 is essential during early embryogenesis and cell cycle progression in somatic cells.

    • Synonyms

      CDC28, CKSHS2, CKS2, CDC28 Protein Kinase 2.

    • 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

      MASMTGGQQM GRGSHMAHKQ IYYSDKYFDE HYEYRHVMLP RELSKQVPKT HLMSEEEWRRLGVQQSLGWV HYMIHEPEPH ILLFRRPLPK DQQ.

    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.

    Cks2 Human
  • View Data Sheet

    Name :

    DYNLT3 Human

    Description:

    Dynein, Light Chain, Tctex-Type 3 Human Recombinant

    Dynein light chain Tctex-type 3, t-complex-associated-testis-expressed 1-like, TCTE1XL, Protein 91/23, TCTEX1L, TCTE1L, RP3.

    Product # :

    PRO-1197

    Price :

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    • description
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    • More Info

    Description

    DYNLT3 Human Recombinant produced in E. coli is a single polypeptide chain containing 139 amino acids (1-116) and having a molecular mass of 15.5 kDa.DYNLT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DYNLT3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      DYNLT3 belongs to a subclass of dynein light chains. The DYNLT3 protein homodimerizes and forms the light chain component of the cytoplasmic dynein motor protein complex. DYNLT3 functions as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex which are believed to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. DYNLT3 may also work independently of dynein as a transcriptional modulator. DYNLT3 is required for the effective progression through mitosis.

    • Synonyms

      Dynein light chain Tctex-type 3, t-complex-associated-testis-expressed 1-like, TCTE1XL, Protein 91/23, TCTEX1L, TCTE1L, RP3.

    • 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 MGSMEEYHRH CDEVGFNAEE AHNIVKECVD GVLGGEDYNH NNINQWTASI VEQSLTHLVK LGKAYKYIVT CAVVQKSAYG FHTASSCFWD TTSDGTCTVR WENRTMNCIV NVFAIAIVL

    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.

    Dynlt3 Human
  • View Data Sheet

    Name :

    CHI3L2 Human

    Description:

    Chitinase 3-Like 2 Recombinant

    Chitinase 3-Like 2, Chondrocyte Protein 39, YKL-39, YKL39, Chitinase-3-Like Protein 2, CHIL2, CHI3L2.

    Product # :

    ENZ-811

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    Description

    CHI3L2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Tyr27-Leu390) containing 374 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 42.1kDa.

    Source

    Escherichia Coli.

    Formulation

    CHI3L2 was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 30mM acetate buffer, pH 4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chitinase 3-Like 2 (CHI3L2) is similar to bacterial chitinases but lacks chitinase activity. CHI3L2 protein is secreted and is involved in cartilage biogenesis. CHI3L2 is a lectin, which binds chitooligosaccharides and other glycans with high affinity.

    • Synonyms

      Chitinase 3-Like 2, Chondrocyte Protein 39, YKL-39, YKL39, Chitinase-3-Like Protein 2, CHIL2, CHI3L2.

    • 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 4.0 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.CHI3L2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASYKLVCYFTNW SQDRQEPGKF TPENIDPFLC SHLIYSFASI ENNKVIIKDK SEVMLYQTIN SLKTKNPKLK ILLSIGGYLF GSKGFHPMVD SSTSRLEFIN SIILFLRNHN FDGLDVSWIY PDQKENTHFT VLIHELAEAF QKDFTKSTKE RLLLTAGVSA GRQMIDNSYQ VEKLAKDLDF INLLSFDFHG SWEKPLITGH NSPLSKGWQD RGPSSYYNVE YAVGYWIHKG MPSEKVVMGI PTYGHSFTLA SAETTVGAPA SGPGAAGPIT ESSGFLAYYE ICQFLKGAKI TRLQDQQVPY AVKGNQWVGY DDVKSMETKV QFLKNLNLGG AMIWSIDMDD FTGKSCNQGP YPLVQAVKRS LGSL.

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    Chi3L2 Human
  • View Data Sheet

    Name :

    CKBB Human

    Description:

    Creatine Kinase Brain Human Recombinant

    Creatine kinase B-type, B-CK, BCK, CKBB, HEL-211, HEL-S-29, CKB, EC 2.7.3.2, Creatine kinase B chain, CKB, CKBB, CKBBI.

    Product # :

    PKA-089

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    Description

    CKBB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-381a.a) and having a molecular mass of 42.6kDa. CKB is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CKBB solution (1mg/ml) contains 20mM Tris-Hcl Buffer (pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    CKBB purity was found to be greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Creatine Kinase BB is a cytoplasmic enzyme involved in energy homeostasis. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in brain as well as in other tissues, and as a heterodimer with a similar muscle isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. A pseudogene of this gene has been characterized.

    • Synonyms

      Creatine kinase B-type, B-CK, BCK, CKBB, HEL-211, HEL-S-29, CKB, EC 2.7.3.2, Creatine kinase B chain, CKB, CKBB, CKBBI.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire CKBB 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

      MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K.

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    Human Ckb
  • View Data Sheet

    Name :

    MAEA Human

    Description:

    Macrophage Erythroblast Attacher Human Recombinant

    Macrophage Erythroblast Attacher, GID Complex Subunit 9 FYV10 Homolog, Lung Cancer-Related Protein 10, Proliferation-Inducing Gene 5, Human Lung Cancer Oncogene 10 Protein, Cell Proliferation-Inducing Gene 5 Protein, Erythroblast Macrophage Protein, FYV10 Homolog (S. Cerevisiae), GID Complex Subunit 9, EMLP, GID9, PIG5, HLC-10, EMP.

    Product # :

    PRO-1634

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    Description

    MAEA Human Recombinant (isoform 1) produced in E.coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (1-396) and having a molecular mass of 47.7kDa.MAEA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAEA solution contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAEA is a 396aa widely expressed adhesion protein which has 5 alternatively spliced isoforms. MAEA holds one CTLH domain and one LisH domain. MAEA forms a complex with F-actin, which takes part in regulating actin distribution in erythroblasts and macrophages and is known to assist in cell division and nuclear architecture. MAEA is confined with condensed chromatin at prophase, nuclear spindle poles at metaphase and in the contractile ring throughout cytokinesis phase and telophase.

    • Synonyms

      Macrophage Erythroblast Attacher, GID Complex Subunit 9 FYV10 Homolog, Lung Cancer-Related Protein 10, Proliferation-Inducing Gene 5, Human Lung Cancer Oncogene 10 Protein, Cell Proliferation-Inducing Gene 5 Protein, Erythroblast Macrophage Protein, FYV10 Homolog (S. Cerevisiae), GID Complex Subunit 9, EMLP, GID9, PIG5, HLC-10, EMP.

    • 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 MGSMAVQESA AQLSMTLKVQ EYPTLKVPYE TLNKRFRAAQ KNIDRETSHV TMVVAELEKT LSGCPAVDSV VSLLDGVVEK LSVLKRKAVE SIQAEDESAK LCKRRIEHLK EHSSDQPAAA SVWKRKRMDR MMVEHLLRCG YYNTAVKLAR QSGIEDLVNI EMFLTAKEVE ESLERRETAT CLAWCHDNKS RLRKMKSCLE FSLRIQEFIE LIRQNKRLDA VRHARKHFSQ AEGSQLDEVR QAMGMLAFPP DTHISPYKDL LDPARWRMLI QQFRYDNYRL HQLGNNSVFT LTLQAGLSAI KTPQCYKEDG SSKSPDCPVC SRSLNKLAQP LPMAHCANSR LVCKISGDVM NENNPPMMLP NGYVYGYNSL LSIRQDDKVV CPRTKEVFHF SQAEKVYIM

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    Maea Human
  • View Data Sheet

    Name :

    Vimentin Antibody

    Description:

    Vimentin, Mouse Anti Human Antibody

    Product # :

    ANT-245

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    Formulation

    1mg/ml in PBS (after reconstitution).

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    • Introduction

      Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines.

    • Solubility

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

    • Immunogen

      Purified Human Vimentin.

    • Ig Subclass

      mouse IgG1.

    • Clone

      hVimentin.

    • Applications

      Direct ELISA, Western Blot, Immuneprecipitation, immunohistochemistry.

    • Cross reactivity

      Vimentin antibody will recognize most mammalian Vimentin except mouse and rat.

    • Titer

      For intra-cellular staining, use 5-10µl/1,000,000 cells. Wash twice with PBS/Azide before adding the appropriate amount of secondary fluorescent reagent.

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Available Conjugates

      This antibody is also available conjugated to biotin and FITC.

    • Type

      Mouse Anti Human Monoclonal Antibody.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.

    • Purification Method

      Ion exchange column.

    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.

    Vimentin Antibody
  • View Data Sheet

    Name :

    ANKRA2 Human

    Description:

    Ankyrin Repeat Family A2 Human Recombinant

    Ankyrin Repeat, Family A (RFXANK-Like), 2, ANKRA, RFXANK-Like Protein 2, Ankyrin Repeat Family A Protein 2, ANKRA2.

    Product # :

    PRO-2062

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    Description

    ANKRA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313a.a) and having a molecular mass of 36.7kDa. ANKRA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ANKRA2 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ankyrin Repeat Family A2, also known as ANKRA2 contains 5 ANK repeats. ANKRA2 assist endocytosis by linking megalin to components of the cytoskeleton or endocytic machinery.

    • Synonyms

      Ankyrin Repeat, Family A (RFXANK-Like), 2, ANKRA, RFXANK-Like Protein 2, Ankyrin Repeat Family A Protein 2, ANKRA2.

    • 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 MGSMDTSTNL DIGAQLIVEE CPSTYSLTGM PDIKIEHPLD PNSEEGSAQG VAMGMKFILP NRFDMNVCSR FVKSLNEEDS KNIQDQVNSD LEVASVLFKA ECNIHTSPSP GIQVRHVYTP STTKHFSPIK QSTTLTNKHR GNEVSTTPLL ANSLSVHQLA AQGEMLYLAT RIEQENVINH TDEEGFTPLM WAAAHGQIAV VEFLLQNGAD PQLLGKGRES ALSLACSKGY TDIVKMLLDC GVDVNEYDWN GGTPLLYAVH GNHVKCVKML LESGADPTIE TDSGYNSMDL AVALGYRSVQ QVIESHLLKL LQNIKE.

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    Ankra2 Human
  • View Data Sheet

    Name :

    CHI3L1 (22-383) Human

    Description:

    Chitinase 3-Like 1 (22-383 a.a) Human Recombinant

    Chitinase 3 Like 1, Chitinase 3-Like 1 (Cartilage Glycoprotein-39), Cartilage Glycoprotein 39, 39 KDa Synovial Protein, HCGP-39, CGP-39, YKL-40, GP-39 , Chitinase-3-Like Protein 1, Cartilage Glycoprotein-39, HC-Gp39, HCGP-3P, YYL-40, ASRT7, YKL40.

    Product # :

    ENZ-975

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    Description

    CHI3L1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 370 amino acids (22-383 a.a.) and having a molecular mass of 41.4kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).CHI3L1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CHI3L1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chitinase 3-Like 1 (CHI3L1) catalyze the hydrolysis of chitin that is an abundant glycopolymer present in insect exoskeletons and fungal cell walls. The glycoside hydrolase 18 family of chitinases comprises 8 human family members. CHI3L1 belongs to the glycosyl hydrolase 18 family. CHI3L1 lacks chitinase activity and is secreted by activated macrophages, chondrocytes, neutrophils and synovial cells. CHI3L1 takes part in the process of inflammation and tissue remodeling.

    • Synonyms

      Chitinase 3 Like 1, Chitinase 3-Like 1 (Cartilage Glycoprotein-39), Cartilage Glycoprotein 39, 39 KDa Synovial Protein, HCGP-39, CGP-39, YKL-40, GP-39 , Chitinase-3-Like Protein 1, Cartilage Glycoprotein-39, HC-Gp39, HCGP-3P, YYL-40, ASRT7, YKL40.

    • 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

      YKLVCYYTSW SQYREGDGSC FPDALDRFLC THIIYSFANI SNDHIDTWEW NDVTLYGMLN TLKNRNPNLK TLLSVGGWNF GSQRFSKIAS NTQSRRTFIK SVPPFLRTHG FDGLDLAWLY PGRGDKQHFT TLIKEMKAEF IKEAQPGKKQ LLLSAALSAG KVTIDSSYDI AKISQHLDFI SIMTYDFHGA WRGTTGHHSP LFRGQEDASP DRFSNTDYAV GYMLRLGAPA SKLVMGIPTF GRSFTLASSE TGVGAPISGP GIPGRFTKEA GTLAYYEICD FLRGATVHRI LGQQVPYATK GNQWVGYDDQ ESVKSKVQYL KDRQLAGAMV WALDLDDFQG SFCGQDLRFP LTNAIKDALA ATLEHHHHHH.

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    Chi3L1 22 383 Human
  • View Data Sheet

    Name :

    CCL14 Human, His

    Description:

    HCC-1 (CCL14) Human Recombinant, His Tag

    Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

    Product # :

    CHM-253

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    Description

    HCC-1 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids (20-93 a.a.) and having a molecular mass of 10.9kDa. The HCC-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HCC-1 solution (0.5 mg/ml) contains Phosphate Buffered Saline pH7.4 containing 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.

    • Synonyms

      Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

    • 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 MTKTESSSRG PYHPSECCFT YTTYKIPRQR IMDYYETNSQ CSKPGIVFIT KRGHSVCTNP SDKWVQDYIK DMKEN.

    • Background

      What is the molecular weight/Mw of CCL14 HUMAN, HIS Protein?
      CCL14 HUMAN, HIS Protein has a total Mw of 10.9kDa.

      What is the source or expression system of CCL14 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL14 HUMAN, HIS Protein?
      CCL14 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL14 HUMAN, HIS Protein?
      The biological functionality of CCL14 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL14 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MTKTESSSRG PYHPSECCFT YTTYKIPRQR IMDYYETNSQ CSKPGIVFIT KRGHSVCTNP SDKWVQDYIK DMKEN.

      What applications can CCL14 HUMAN, HIS Protein be used in?
      CCL14 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL14 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL14 HUMAN, HIS Protein was purified using conventional chromatography techniques.


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    Hcc 1 Human His
  • View Data Sheet

    Name :

    CST3 Protein, His

    Description:

    Cystatin-C Human Recombinant, His Tag

    Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    Product # :

    PRO-656

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    Description

    Cystatin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 129 amino acids and having a molecular mass of 14.5 kDa. The protein contains an extra His tag at N-terminus. The Cystatin-C amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q6FGW9 amino acids 28–146.The Cystatin-C is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS PAGE.

    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, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. 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

      Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

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    Cystatin C Human Recombinant
  • View Data Sheet

    Name :

    CTSE Human

    Description:

    Cathepsin-E Human Recombinant

    Cathepsin E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving Proteinase, EC 3.4.23.

    Product # :

    ENZ-776

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    Description

    CTSE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (57-363 a.a) and having a molecular mass of 35.4kDa.CTSE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Cathepsin-E also known as CTSE is a gastric aspartyl protease which functions as a disulfide-linked homodimer. CTSE belongs to the peptidase C1 family; furthermore it has specificity similar to pepsin A and cathepsin D. CTSE is an intracellular proteinase which does not seem to be involved in the digestion of dietary protein and is found in the uppermost concentration in the surface of epithelial mucus-producing cells of the stomach. CTSE is the first aspartic proteinaseexpressed in the fetal stomach and is discovered in more than half of gastric cancers. For that reason CTSE is anoncofetal antigen. In addition, transcript variants utilizing alternative polyadenylation signals and two transcript variantsencoding different isoforms exist for this gene.

    • Synonyms

      Cathepsin E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving Proteinase, EC 3.4.23.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSTESCSMD QSAKEPLINY LDMEYFGTIS IGSPPQNFTV IFDTGSSNLW VPSVYCTSPA CKTHSRFQPS QSSTYSQPGQ SFSIQYGTGS LSGIIGADQV SVEGLTVVGQ QFGESVTEPG QTFVDAEFDG ILGLGYPSLA VGGVTPVFDN MMAQNLVDLP MFSVYMSSNP EGGAGSELIF GGYDHSHFSG SLNWVPVTKQ AYWQIALDNM LWSVPTLTSC RMSPSPLTES PIPSAQLPTP YWTSWMECSS AAVAFKDLTS TLQLGPSGSW GMSSFDSFTQ SLTVGITVWD WPQQSPKEGP CVCACLSDRP

    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.

    Ctse Human
  • View Data Sheet

    Name :

    SOSTDC1 Human

    Description:

    Sclerostin Domain Containing 1 Human Recombinant

    Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.

    Product # :

    PRO-426

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    Description

    SOSTDC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (24-206 a.a) and having a molecular mass of 23kDa.SOSTDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SOSTDC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sclerostin Domain Containing 1 (SOSTDC1) belongs to the sclerostin family and an N-glycosylated, secreted protein with a C-terminal cystine knot-like domain. The SOSTDC1 protein acts as a bone morphogenetic protein (BMP) antagonist. Specifically, SOSTDC1 directly associates with BMPs, prohibiting them from binding their receptors, thus regulating BMP signaling throughout cellular proliferation, differentiation, and programmed cell death. SOSTDC1 may also be involved in the onset of endometrial receptivity for implantation/sensitization for the decidual cell reaction Enhances Wnt signaling and hinders TGF-beta signaling. In addition, SOSTDC1 directly antagonizes the activity of BMP2, BMP4, BMP6 and BMP7 in a dose-dependent manner.

    • Synonyms

      Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.

    • 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 MGSFKNDATE ILYSHVVKPV PAHPSSNSTL NQARNGGRHF SNTGLDRNTR VQVGCRELRS TKYISDGQCT SISPLKELVC AGECLPLPVL PNWIGGGYGT KYWSRRSSQE WRCVNDKTRT QRIQLQCQDG STRTYKITVV TACKCKRYTR QHNESSHNFE SMSPAKPVQH HRERKRASKS SKHSMS.

    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.

    Sostdc1 Human
  • View Data Sheet

    Name :

    TTC32 Human

    Description:

    Tetratricopeptide Repeat Domain 32 Human Recombinant

    Tetratricopeptide Repeat Domain 32, Tetratricopeptide Repeat Protein 32, TPR Repeat Protein 32.

    Product # :

    PRO-1246

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    Description

    TTC32 Human Recombinant produced in E. coli is a single polypeptide chain containing 174 amino acids (1-151) and having a molecular mass of 19.7 kDa. TTC32 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TTC32 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TTC32 contains 3 TPR repeats. The tetratricopeptide repeat (TPR) is a structural motif. TPR is observed in organized 3–16 motifs, which form scaffolds to mediate protein–protein interactions and frequently the assembly of multiprotein complexes. TPR-containing proteins include the anaphase-promoting complex subunits cdc16, cdc23 and cdc27, the NADPH oxidase subunit p67-phox, hsp90-binding immunophilins, transcription factors, the major receptor for peroxisomal matrix protein import PEX5, the PKR protein kinase inhibitor and mitochondrial import proteins.

    • Synonyms

      Tetratricopeptide Repeat Domain 32, Tetratricopeptide Repeat Protein 32, TPR Repeat Protein 32.

    • 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 MGSMEGQRQE SHATLTLAQA HFNNGEYAEA EALYSAYIRR CACAASSDES PGSKCSPEDL ATAYNNRGQI KYFRVDFYEA MDDYTSAIEV QPNFEVPYYN RGLILYRLGY FDDALEDFKK VLDLNPGFQD ATLSLKQTIL DKEEKQRRNV AKNY.

    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.

    Ttc32 Human
  • View Data Sheet

    Name :

    EREG Human

    Description:

    Epiregulin Human Recombinant

    EREG, Epiregulin, ER.

    Product # :

    CYT-609

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    Description

    Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.

    Purity

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

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

    More Info

    • Introduction

      Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

    • Synonyms

      EREG, Epiregulin, ER.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 5.6kDa.

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

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

      What is the Biological Activity of EREG Protein?
      The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

      What is the amino acid sequence of EREG Protein?
      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

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

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

    Epiregulin Human
  • View Data Sheet

    Name :

    CST4 Human, sf9

    Description:

    Cystatin 4 Human Recombinant, sf9

    Cystatin S, Salivary Acidic Protein 1, Cystatin-SA-III, Cystatin-4, Cystatin 4, Cystatin-S.

    Product # :

    PRO-2250

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    Description

    CST4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 131 amino acids (21-141 a.a.) and having a molecular mass of 15.4kDa (Migrates at 13.5-18kDa on SDS-PAGE under reducing conditions). CST4 is expressed with a 10 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CST4 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CST4 is a member of the cystatin superfamily which contains proteins that hold multiple cystatin-like sequences. Several family members are active cysteine protease inhibitors, whereas others have lost or possibly never attained this inhibitory activity. CST4 strongly inhibits papain (non-competitively) and ficin, partially inhibits stem bromelain and bovine cathepsin C, however does not inhibit porcine cathepsin B or clostripain.

    • Synonyms

      Cystatin S, Salivary Acidic Protein 1, Cystatin-SA-III, Cystatin-4, Cystatin 4, Cystatin-S.

    • 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

      ADPMSSSKEE NRIIPGGIYD ADLNDEWVQR ALHFAISEYN KATEDEYYRR PLQVLRAREQ TFGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WEDRMSLVNS RCQEAHHHHH H.

    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.

    Cst4 Human Sf9
  • View Data Sheet

    Name :

    CTF1 Mouse

    Description:

    Cardiotrophin-1 Mouse Recombinant

    CTF1, CT1, CT-1, Cardiophin 1.

    Product # :

    CYT-151

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    Description

    CTF1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 202 amino acids and having a molecular mass of 21.3kDa.The CTF1 Mouse is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of TF-1 cells was < 1.0ng/ml, corresponding to a specific activity of > 1,000,000units/mg.

    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.

    • 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 CTF1 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 CTF1 in sterile 4mM HCl to a concentration of 0.1-0.5 mg/ml. Stock solutions should be apportioned into working aliquots and stored at <-200C. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      SQREGSLEDH QTDSSISFLP HLEAKIRQTH NLARLLTKYA EQLLEEYVQQ QGEPFGLPGF SPPRLPLAGL SGPAPSHAGL PVSERLRQDA AALSVLPALL DAVRRRQAEL NPRAPRLLRS LEDAARQVRA LGAAVETVLA ALGAAARGPG PEPVTVATLF TANSTAGIFS AKVLGFHVCG LYGEWVSRTE GDLGQLVPGG VA

    • Background

      What is the molecular weight/Mw of CTF1 Protein?
      CTF1 Protein has a total Mw of 21.3kDa.

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

      What is the Purity of CTF1 Protein?
      CTF1 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTF1 Protein?
      The ED50 as determined by the dose-dependent proliferation of TF-1 cells was < 1.0ng/ml, corresponding to a specific activity of > 1,000,000units/mg.

      What is the amino acid sequence of CTF1 Protein?
      SQREGSLEDH QTDSSISFLP HLEAKIRQTH NLARLLTKYA EQLLEEYVQQ QGEPFGLPGF SPPRLPLAGL SGPAPSHAGL PVSERLRQDA AALSVLPALL DAVRRRQAEL NPRAPRLLRS LEDAARQVRA LGAAVETVLA ALGAAARGPG PEPVTVATLF TANSTAGIFS AKVLGFHVCG LYGEWVSRTE GDLGQLVPGG VA

      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.

    Ct 1 Mouse
  • View Data Sheet

    Name :

    Activin A Human Plant

    Description:

    Activin A Human Recombinant, Plant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-052

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    Description

    Activin A human Recombinant produced in Nicotiana benthamiana plant is a disulfide-linked homodimers of two betaA chains, each containing 116 amino residues (molecular formula C600H911N173O174S13) and 6-His-tag at the N-terminal having the total molecular mass of 27.4kDa.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in Tris HCl 0.05M buffer at pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different ? subunit isoforms, part of the TGF? family. Mature Activin A has two 116 amino acids residues betaA subunits (bA-bA). 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

      Sterile Filtered White 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

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

    • Amino Acid Sequence

      HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 27.4 kDa.
      What is the source or expression system of Activin A Protein?
      Nicotinia

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

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

      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?
      HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS

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

    • Serological Identification

      The protein was electrophoresed under reducing condition on a 15% SDS-polyacrylamide gel, transferred by electroblotting to a NC membrane and visualized by immune-detection with specific antibody Activin 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.

    Activin A Human Plant
  • View Data Sheet

    Name :

    SPINK7 Human

    Description:

    Serine Peptidase Inhibitor Kazal Type 7 Human Recombinant

    Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.

    Product # :

    PRO-1507

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    Description

    SPINK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 89 amino acids (20-85) and having a molecular mass of 9.6 kDa.SPINK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPINK7 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serine peptidase inhibitor Kazal type 7 (SPINK7) which includes one Kazal-like domain is most likely serine protease inhibitor. Diseases linked with SPINK7 include esophageal cancer, and oral squamous cell carcinoma

    • Synonyms

      Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.

    • 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 MGSSEAASLS PKKVDCSIYK KYPVVAIPCP ITYLPVCGSD YITYGNECHL CTESLKSNGR VQFLHDGSC.

    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.

    Spink7 Human
  • View Data Sheet

    Name :

    BTC Human, HEK

    Description:

    Betacellulin Human Recombinant, HEK

    Betacellulin isoform 1, Probetacellulin, Betacellulin, BTC

    Product # :

    CYT-1188

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    Description

    BTC Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (32-111 a.a) containing 86 amino acids and having a molecular mass of 9.8kDa.BTC is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    ED50 range is ≤ 0.5ng/ml. It is measured by cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.

    More Info

    • Introduction

      BTC is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are mediated by the EGF receptor and other related receptors.

    • Synonyms

      Betacellulin isoform 1, Probetacellulin, Betacellulin, BTC

    • 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

      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY HHHHHH

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 9.8kDa.

      What is the source or expression system of BETACELLULIN Protein?
      HEK293 cells.

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

      What is the Biological Activity of BETACELLULIN Protein?
      ED50 range is ≤ 0.5ng/ml. It is measured by cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.

      What is the amino acid sequence of BETACELLULIN Protein?
      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY HHHHHH

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

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

    Betacellulin Protein
  • View Data Sheet

    Name :

    FSTL1 Human, HEK

    Description:

    Follistatin Like 1 Human Recombinant, HEK

    Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1, MIR198.

    Product # :

    CYT-1027

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    • More Info

    Description

    FSTL1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-308) containing 296 amino acids including a 8 a.a C-terminal His tag. The total molecular mass is 33.8kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    FSTL1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline and 5 % (w/v) trehalose, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      FSTL1 protein resembles follistatin, an activin-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.

    • Synonyms

      Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1, MIR198.

    • 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 one week 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. FSTL1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEIHH HHHHHH.

    • Background

      What is the molecular weight/Mw of FSTL1 HUMAN, HEK Protein?
      FSTL1 HUMAN, HEK Protein has a total Mw of 33.8kDa.

      What is the source or expression system of FSTL1 HUMAN, HEK Protein?
      HEK293 cells.

      What is the Purity of FSTL1 HUMAN, HEK Protein?
      FSTL1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FSTL1 HUMAN, HEK Protein?
      The biological functionality of FSTL1 HUMAN, HEK Protein will be determined in the future.

      What is the amino acid sequence of FSTL1 HUMAN, HEK Protein?
      EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEIHH HHHHHH.

      What applications can FSTL1 HUMAN, HEK Protein be used in?
      FSTL1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FSTL1 HUMAN, HEK Protein?
      The endotoxin level is minimal, FSTL1 HUMAN, HEK 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.

    Fstl1 Protein
  • View Data Sheet

    Name :

    KIAA0101 Human

    Description:

    KIAA0101 Human Recombinant

    KIAA0101, L5, NS5ATP9, OEATC, OEATC-1, OEATC1, p15(PAF), p15/PAF, p15PAF, PAF, PAF15, PCNA-associated factor, Hepatitis C virus NS5A-transactivated protein 9, HCV NS5A-transactivated protein 9, Overexpressed in anaplastic thyroid carcinoma 1, PCNA-associated factor of 15 kDa.

    Product # :

    PRO-1683

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    KIAA0101 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (1-111) and having a molecular mass of 14.4 kDa.KIAA0101 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KIAA0101 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KIAA0101 is a PCNA-binding protein which performs as a regulator of DNA repair all through DNA replication. Subsequent to DNA mutilation, the collaboration with PCNA is interrupted, enabling the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, assisting the bypass of replication-fork-blocking lesions. Additionally, KIAA0101 performs as a controller of centrosome number.

    • Synonyms

      KIAA0101, L5, NS5ATP9, OEATC, OEATC-1, OEATC1, p15(PAF), p15/PAF, p15PAF, PAF, PAF15, PCNA-associated factor, Hepatitis C virus NS5A-transactivated protein 9, HCV NS5A-transactivated protein 9, Overexpressed in anaplastic thyroid carcinoma 1, PCNA-associated factor of 15 kDa.

    • 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 MGSMVRTKAD SVPGTYRKVV AARAPRKVLG SSTSATNSTS VSSRKAENKY AGGNPVCVRP TPKWQKGIGE FFRLSPKDSE KENQIPEEAG SSGLGKAKRK ACPLQPDHTN DEKE.

    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.

    Kiaa0101 Human
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