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Search results

1000 results found for “Uroplakin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    MAPK14 Human

    Description:

    Mitogen-Activated Protein Kinase 14 Human Recombinant

    Mitogen-activated protein kinase 14, Mitogen-activated protein kinase p38 alpha, CSBP1, CSBP2, Mxi2, PRKM14, MAP kinase p38 alpha, MAX-interacting protein 2, EXIP, PRKM15, p38, Cytokine suppressive anti-inflammatory drug-binding protein, MAP kinase MXI2, Stress-activated protein kinase 2a, RK, CSAID binding protein, p38alpha Exip, SAPK2A, EC 2.7.11, EC 2.7.11.24.

    Product # :

    PKA-014

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    Description

    MAPK14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 383 amino acids (1-360 a.a.) and having a molecular mass of 43.7kDa.MAPK14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAPK14 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE analysis.

    More Info

    • Introduction

      MAPK14 belongs to the MAP kinase family and is most associated with p38 MAP kinases(MAPKs). MAPKs are activated mainly as a reaction to cellular stress and inflammatory cytokines, and inhibitors that target the MAPK14 and MAPK11 have demonstrated ability to cure inflammatory disease. The substrates of this kinase contain transcription regulator ATF2, MEF2C, and MAX, cell cycle regulator CDC25B, and tumor suppressor p53, which demonstrate the parts of MAPK14 in stress-related transcription, cell cycle regulation and genotoxic stress response.

    • Synonyms

      Mitogen-activated protein kinase 14, Mitogen-activated protein kinase p38 alpha, CSBP1, CSBP2, Mxi2, PRKM14, MAP kinase p38 alpha, MAX-interacting protein 2, EXIP, PRKM15, p38, Cytokine suppressive anti-inflammatory drug-binding protein, MAP kinase MXI2, Stress-activated protein kinase 2a, RK, CSAID binding protein, p38alpha Exip, SAPK2A, EC 2.7.11, EC 2.7.11.24.

    • 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 MGSMSQERPT FYRQELNKTI WEVPERYQNL SPVGSGAYGS VCAAFDTKTG LRVAVKKLSR PFQSIIHAKR TYRELRLLKH MKHENVIGLL DVFTPARSLE EFNDVYLVTH LMGADLNNIV KCQKLTDDHV QFLIYQILRG LKYIHSADII HRDLKPSNLA VNEDCELKIL DFGLARHTDD EMTGYVATRW YRAPEIMLNW MHYNQTVDIW SVGCIMAELL TGRTLFPGTD HIDQLKLILR LVGTPGAELL KKISSESARN YIQSLTQMPK MNFANVFIGA NPLAVDLLEK MLVLDSDKRI TAAQALAHAY FAQYHDPDDE PVADPYDQSF ESRDLLIDEW KSLTYDEVIS FVPPPLDQEE MES.

    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.

    Mapk14 Human
  • View Data Sheet

    Name :

    MAPK9 Human

    Description:

    Mitogen-Activated Protein Kinase 9 Human Recombinant

    Mitogen-activated protein kinase 9, MAP kinase 9, MAPK 9, JNK-55, Stress-activated protein kinase 1a, SAPK1a, Stress-activated protein kinase JNK2, c-Jun N-terminal kinase 2, MAPK9, JNK2, PRKM9, SAPK, p54a, JNK2A, JNK2B, JNK2BETA, p54aSAPK, JNK2ALPHA.

    Product # :

    PKA-039

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    Description

    MAPK9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-382 a.a) and having a molecular mass of 46.6kDa.MAPK9 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAPK9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitogen-activated protein kinase 9 (MAPK9) belongs to the MAP kinase family. MAP kinases function as an integration point for numerous biochemical signals, and are involved in a broad variety of cellular processes such as proliferation, differentiation, transcription regulation and development. MAPK9 targets specific transcription factors, and consequently mediates immediate-early gene expression in response to diverse cell stimuli. As an active dimer, MAPK9 can translocate to the nucleus and control transcription through its effects on c-Jun, ATF-2, and other transcription factors. MAPK9 blocks the ubiquitination of tumor suppressor p53, and so it increases the stability of p53 in nonstressed cells.

    • Synonyms

      Mitogen-activated protein kinase 9, MAP kinase 9, MAPK 9, JNK-55, Stress-activated protein kinase 1a, SAPK1a, Stress-activated protein kinase JNK2, c-Jun N-terminal kinase 2, MAPK9, JNK2, PRKM9, SAPK, p54a, JNK2A, JNK2B, JNK2BETA, p54aSAPK, JNK2ALPHA.

    • 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 MGSHMSDSKC DSQFYSVQVA DSTFTVLKRY QQLKPIGSGA QGIVCAAFDT VLGINVAVKK LSRPFQNQTH AKRAYRELVL LKCVNHKNII SLLNVFTPQK TLEEFQDVYL VMELMDANLC QVIHMELDHE RMSYLLYQML CGIKHLHSAG IIHRDLKPSN IVVKSDCTLK ILDFGLARTA CTNFMMTPYV VTRYYRAPEV ILGMGYKENV DIWSVGCIMG ELVKGCVIFQ GTDHIDQWNK VIEQLGTPSA EFMKKLQPTV RNYVENRPKY PGIKFEELFP DWIFPSESER DKIKTSQARD LLSKMLVIDP DKRISVDEAL RHPYITVWYD PAEAEAPPPQ IYDAQLEERE HAIEEWKELI YKEVMDWEER SKNGVVKDQP SAQMQQ.

    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.

    Mapk9 Human
  • View Data Sheet

    Name :

    RALY Human

    Description:

    RALY Human Recombinant

    RALY Heterogeneous Nuclear Ribonucleoprotein, RNA-Binding Protein (Autoantigenic, HnRNP-Associated With Lethal Yellow), HnRNP Associated With Lethal Yellow Protein Homolog, Heterogeneous Nuclear Ribonucleoprotein C-Like 2, HnRNP Core Protein C-Like 2, Autoantigen P542, HNRPCL2, P542, RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog (Mouse)), RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog), RNA-Binding Protein (Autoantigenic), RNA-Binding Protein Raly, RNA-binding protein Raly.

    Product # :

    PRO-2095

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    • description
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    Description

    RALY Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (1-306 a.a) and having a molecular mass of 34.9kDa. RALY is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RALY protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RALY belongs to the heterogeneous nuclear ribonucleoprotein (hnRNP) gene family. RALY takes part in pre-mRNA splicing and also in embryonic development. Moreover, alternate splicing results in multiple transcript variants have been found for RALY.

    • Synonyms

      RALY Heterogeneous Nuclear Ribonucleoprotein, RNA-Binding Protein (Autoantigenic, HnRNP-Associated With Lethal Yellow), HnRNP Associated With Lethal Yellow Protein Homolog, Heterogeneous Nuclear Ribonucleoprotein C-Like 2, HnRNP Core Protein C-Like 2, Autoantigen P542, HNRPCL2, P542, RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog (Mouse)), RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog), RNA-Binding Protein (Autoantigenic), RNA-Binding Protein Raly, RNA-binding protein Raly.

    • 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 MGSMSLKLQA SNVTNKNDPK SINSRVFIGN LNTALVKKSD VETIFSKYGR VAGCSVHKGY AFVQYSNERH ARAAVLGENG RVLAGQTLDI NMAGEPKPDR PKGLKRAASA IYSGYIFDYD YYRDDFYDRL FDYRGRLSPV PVPRAVPVKR PRVTVPLVRR VKTNVPVKLF ARSTAVTTSS AKIKLKSSEL QAIKTELTQI KSNIDALLSR LEQIAAEQKA NPDGKKKGDG GGAGGGGGGG GSGGGGSGGG GGGGSSRPPA PQENTTSEAG LPQGEARTRD DGDEEGLLTH SEEELEHSQD TDADDGALQ.

    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.

    Raly Human
  • View Data Sheet

    Name :

    RLBP1 Human

    Description:

    Retinaldehyde Binding Protein 1 Human Recombinant

    Retinaldehyde Binding Protein 1, Cellular Retinaldehyde-Binding Protein, CRALBP.

    Product # :

    PRO-1845

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    • description
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    Description

    RLBP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (1-317) and having a molecular mass of 38.9 kDa. RLBP1 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The RLBP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RLBP1 is a 36-kD water-soluble protein that transports 11-cis-retinal or 11-cis-retinaldehyde as physiologic ligands. RLBP1 is a functional element of the visual cycle. RLBP1 gene mutations cause retinitis punctata albescens, severe rod-cone dystrophy and Bothnia dystrophy (nonsyndromic autosomal recessive retinitis pigmentosa).

    • Synonyms

      Retinaldehyde Binding Protein 1, Cellular Retinaldehyde-Binding Protein, CRALBP.

    • 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 MGSMSEGVGT FRMVPEEEQE LRAQLEQLTT KDHGPVFGPC SQLPRHTLQK AKDELNEREE TREEAVRELQ EMVQAQAASG EELAVAVAER VQEKDSGFFL RFIRARKFNV GRAYELLRGY VNFRLQYPEL FDSLSPEAVR CTIEAGYPGV LSSRDKYGRV VMLFNIENWQ SQEITFDEIL QAYCFILEKL LENEETQING FCIIENFKGF TMQQAASLRT SDLRKMVDML QDSFPARFKA IHFIHQPWYF TTTYNVVKPF LKSKLLERVF VHGDDLSGFY QEIDENILPS DFGGTLPKYD GKAVAEQLFG PQAQAENTAF

    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.

    Rlbp1 Human
  • View Data Sheet

    Name :

    RPL11 Human

    Description:

    Ribosomal Protein L11 Human Recombinant

    Ribosomal Protein L11, Cell Growth-Inhibiting Protein 34, CLL-Associated Antigen KW-12, 60S Ribosomal Protein L11, DBA7, GIG34, L11.

    Product # :

    PRO-1561

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    Description

    RPL11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-178) and having a molecular mass of 22.6kDa.RPL11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RPL11 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT, 2mM EDTA, 250mM Imidazole and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribosomes are the organelles which catalyze protein synthesis, they’re comprised of a small 40S subunit and a large 60S subunit. Ribosomal Protein L11 (RPL11) is a member of the L5P family of ribosomal proteins. RPL11 is a ribosomal protein which is a component of the 60S subunit. RPL11 is found in the cytoplasm. The RPL11 protein most likely associates with the 5S rRNA.

    • Synonyms

      Ribosomal Protein L11, Cell Growth-Inhibiting Protein 34, CLL-Associated Antigen KW-12, 60S Ribosomal Protein L11, DBA7, GIG34, L11.

    • 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 MGSMAQDQGE KENPMRELRI RKLCLNICVG ESGDRLTRAA KVLEQLTGQT PVFSKARYTV RSFGIRRNEK IAVHCTVRGA KAEEILEKGL KVREYELRKN NFSDTGNFGF GIQEHIDLGI KYDPSIGIYG LDFYVVLGRP GFSIADKKRR TGCIGAKHRI SKEEAMRWFQ QKYDGIILPG K

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

    Rpl11 Human
  • View Data Sheet

    Name :

    DDAVP

    Description:

    Desmopressin

    Product # :

    HOR-270

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    Description

    Desmopressin also called ADH (Anti-Diuretic Hormone) has a molecular formula of C46H64N14O12S2 , Mpr-Tyr-Phe-Gln-Asn-Cys-Pro-D-Arg-Gly-NH2 having a Mw of 1069.23 Dalton.

    Formulation

    The Desmopressin peptide was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Desmopressin is the first vasopressin analog with a very high and very specific antidiuretic effect, has been widely used for different therapeutic purposes and is believed to be partly responsible for the formation of memories learning and memory processes. Desmopressin increases urine concentration and decreases urine production. Desmopressin is used to prevent and control excessive thirst, urination, and dehydration.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    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.

    Desmopressin
  • View Data Sheet

    Name :

    KRT14 Human

    Description:

    Cytokeratin 14 Human Recombinant

    Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.

    Product # :

    PRO-348

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    Description

    Cytokeratin 14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 51,530 Dalton. The KRT14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized after from a sterile solution containing 30mM Tris-HCl pH-8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokeratin 14 is a member of the keratin family, the most diverse group of intermediate filaments. Cytokeratin 14 is a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11.

    • Synonyms

      Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KRT14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KRT14 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 CK-14 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Reconstitution to filaments

      Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCI, 2mM dithiothreitol, 10mM Tris-HCI, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

    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.

    Krt14 Human
  • View Data Sheet

    Name :

    SPOP Human

    Description:

    Speckle-Type POZ Protein Human Recombinant

    Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.

    Product # :

    PRO-195

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    Description

    SPOP Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 394 amino acids (1-374 a.a.) and having a molecular mass of 44.3kDa. The SPOP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPOP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 50% glycerol, 0.2M NaCl and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Speckle-type POZ protein (SPOP) belongs to the Tdpoz family containing one N-terminal MATH (Meprin and TRAF homology) domain and one C-terminal BTB/POZ domain. SPOP inhibits IPF1/PDX1 transactivation of established target promoters, may be by recruiting a repressor complex. SPOP is involved in ubiquitinylation and protein degradation as a result of an interaction with CUL-3.

    • Synonyms

      Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.

    • Physical Appearance

      SPOP is supplied as a 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 MSRVPSPPPP AEMSSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE VIKSSTFSSG ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA KFKFSILNAK GEETKAMESQ RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE
      VSVVQDSVNI SGQNTMNMVK VPECRLADEL GGLWENSRFT DCCLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR VEINDVEPEV FKEMMCFIYT GKAPNLDKMA DDLLAAADKY ALERLKVMCE DALCSNLSVE NAAEILILAD LHSADQLKTQ AVDFINYHAS DVLETSGWKS MVVSHPHLVA EAYRSLASAQ CPFLGPPRKR LKQS.

    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.

    Spop Human
  • View Data Sheet

    Name :

    IL 13 Rat

    Description:

    Interleukin-13 Rat Recombinant

    NC300, ALRH, BHR1, P600, IL-13.

    Product # :

    CYT-391

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    Description

    Interleukin-13 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 113 amino acids and having a molecular mass of 12.7 kDa.The IL-13 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    ED50 range = 2-6 ng/mL as determined by the dose dependent proliferation of human TF-1 cells. Optimal concentration for individual application should be determined by a dose response assay.

    More Info

    • Introduction

      IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.

    • Synonyms

      NC300, ALRH, BHR1, P600, IL-13.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 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 Interleukin 13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.69 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IL-13 as a Reference Standard.

    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.

    Il 13 Rat
  • View Data Sheet

    Name :

    OSM Human, 209 a.a

    Description:

    Oncostatin M Human Recombinant (209 a.a.)

    OSM, MGC20461, Oncostatin M.

    Product # :

    CYT-639

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    Description

    Oncostatin-M (209 a.a.) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids and having a molecular mass of 23.9kDa. The Oncostatin-M (209 a.a.) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Oncostatin-M (209 a.a.) was lyophilized from a concentrated (1mg/ml) solution containing 1x PBS pH-7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 IU/mg.

    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

      OSM, MGC20461, Oncostatin M.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Oncostatin-M (209 a.a.) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin-M (209 a.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 Oncostatin-M (209 a.a.) in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPG
      AFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDL
      EKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQ
      RKLEGCRFLHGYHRFMHSVGRVFKWGESPNRSRRHSPHQALRKGVRR.

    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.

    Oncostatin M Human 209 Aa
  • View Data Sheet

    Name :

    IL 29 Human, Sf9

    Description:

    Interleukin-29 Human Recombinant, Sf9

    Interleukin-29, IL-29, IFN-Lambda 1, Interferon-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.

    Product # :

    CYT-988

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    Description

    Interleukin-29 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 187 amino acids (20-200a.a.) and having a molecular mass of 20.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).IL29 is fused with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL29 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL-29 is distantly related to type I interferons and the IL-10 family. Expression of IL-29 is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-29 exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
      IL-29 acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda3 are closely positioned genes on human chromosome 19.
      IL-29 induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
      IL-29 is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-29 produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
      IFN-Lambda 1 antiviral and antiproliferative activity requires Interferon-Lambda 2 receptor tyrosine residues.

    • Synonyms

      Interleukin-29, IL-29, IFN-Lambda 1, Interferon-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.

    • 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

      GPVPTSKPTT TGKGCHIGRF KSLSPQELAS FKKARDALEE SLKLKNWSCS SPVFPGNWDL RLLQVRERPV ALEAELALTL KVLEAAAGPA LEDVLDQPLH TLHHILSQLQ ACIQPQPTAG PRPRGRLHHW LHRLQEAPKK ESAGCLEASV TFNLFRLLTR DLKYVADGNL CLRTSTHPES THHHHHH.

    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.

    Il29 Human Sf9
  • View Data Sheet

    Name :

    IL34 Mouse

    Description:

    Interleukin 34 Mouse Recombinant

    Interleukin-34, IL-34, Il34.

    Product # :

    CYT-863

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    Description

    IL34 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (21-235 a.a) and having a molecular mass of 26.8kDa.IL34 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    IL34 protein solution (0.5mg/ml) in 20mM Tris-HCl buffer (pH 8.0) and 10% Glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Interleukin 34 (IL34) is a cytokine that promotes the differentiation and viability of monocytes and macrophages through the colony-stimulating factor-1 receptor and is a part of a group of cytokines called interleukins. IL34 increases growth or survival of immune cells known as monocytes. IL34 protein obtains its activity by binding the Colony stimulating factor 1 receptor. Interleukin 34 has also a potential part in viral infection, the adaptive immune response and bone marrow cell proliferation. Furthermore, IL34 plays an important role in innate immunity and in inflammatory processes.

    • Synonyms

      Interleukin-34, IL-34, Il34.

    • 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 MNENLEIWTL TQDKECDLTG YLRGKLQYKN RLQYMKHYFP INYRIAVPYE GVLRVANITR LQKAHVSERE LRYLWVLVSL NATESVMDVL LEGHPSWKYL QEVQTLLENV QRSLMDVEIG PHVEAVLSLL STPGLSLKLV RPKALLDNCF RVMELLYCSC CKQSPILKWQ DCELPRLHPH SPGSLMQCTA TNVYPLSRQT PTSLPGSPSS SHGSLP.

    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.

    Il34 Mouse
  • View Data Sheet

    Name :

    ErbB2 (146-192) Human

    Description:

    Tyrosine Kinase ErbB-2 (146-192) Human Recombinant

    erbB-2, EC 2.7.10.1, p185erbB2, C-erbB-2.

    Product # :

    PKA-136

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    Description

    The ErbB2 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The ErbB2 His-Tagged Fusion Protein, produced in E. coli, is a 14kDa protein containing 47 amino acid residues of the ErbB2 Human, 146-192amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      erbB-2, EC 2.7.10.1, p185erbB2, C-erbB-2.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized ErbB2 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      HER2 / ErbB2 (human epidermal growth factor receptor 2) is a member of the ErbB family of receptor tyrosine kinases. It plays a role in cell signalling related to growth, differentiation and proliferation.

      erbB-2 encodes a 185-kDa orphan receptor tyrosine kinase that is constitutively active as a dimer and displays potent oncogenic activity when overexpressed.

      ErbB2 works as a receptor that, upon ligand binding activates downstream signalling pathways such as the MAPK and PI3K/AKT pathways, promoting cell proliferation and survival.

      The activation of ErbB2 leads to enhanced cell growth and survival, making it critical in normal cellular functions and in the pathogenesis of cancer.

      Herstatin, as the product of alternative HER-2 transcript, retains intron 8.
      The herstatin mRNA is expressed in normal human fetal kidney and liver, but is at reduced levels relative to p185HER-2 mRNA in carcinoma cells that contain an amplified HER-2 gene. Herstatin appears to be an inhibitor of p185HER-2, because it disrupts dimers, reduces tyrosine phosphorylation of p185, and inhibits the anchorage-independent growth of transformed cells that overexpress HER-2.

    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.

    Erbb2 Protein
  • View Data Sheet

    Name :

    SERPINA9 Mouse

    Description:

    Serpin Peptidase Inhibitor, Clade A Mouse Recombinant

    Serpin A9, Serpina9, SERPINA9.

    Product # :

    PRO-2366

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    Description

    SERPINA9 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 401 amino acids (26-418 a.a) and having a molecular mass of 45.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).SERPINA9 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SERPINA9 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serpin Peptidase Inhibitor, Clade A Member 9, also known as serpin A9, belongs to the Serpin superfamily of serine protease inhibitors. Serpins are the most extensively distributed superfamily of protease inhibitors which use a conformational modification to inhibit target enzymes. Serpins are known to inhibit serine proteases as well as inhibiting caspases in addition to papain-like cysteine proteases. Serpins are conformational labile and numerous of the disease-linked mutations of serpins outcome in misfolding or in pathogenic, inactive polymers. serpin A9 demonstrates inhibition towards trypsin, thrombin, as well as plasmin and binds DNA and heparin.

    • Synonyms

      Serpin A9, Serpina9, SERPINA9.

    • 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

      NPYNQESSHL PSMKKNPASQ VSPSNTRFSF LLYQRLAQEN PGQNILFSPV SISTSLAMLS LGARSATKTQ ILRTLGFNFT WVSEPTIHMG FEYLVRSLNK CHQGRELRMG SVLFIRKELQ LQATFLDRVK KLYGAKVFSE DFSNAATAQA QINSYVEKET KGKVVDVIQD LDSQTAMVLV NHIFFKANWT QPFSTANTNK SFPFLLSKGT TVHVPMMHQT ESFAFGVDKE LGCSILQMDY RGDAVAFFVL PGKGKMRQLE KSLSARRLRK WSRSLQKRWI KVFIPKFSIS ASYNLETILP KMGIRDAFNS NADFSGITKT HFLQVSKAAH KAVLDVSEEG TEAAAATTTK LIVRSRDTPS SIIAFKEPFL ILLLDKNTES VLFLGKVENP RKMLEHHHHH H

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    Serpina9 Mouse
  • View Data Sheet

    Name :

    ANKRD54 Human

    Description:

    Ankyrin Repeat Domain 54 Protein Human Recombinant

    LIAR, Lyn-interacting ankyrin repeat protein.

    Product # :

    PRO-1480

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    Description

    ANKRD54 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300 a.a.) and having a molecular mass of 34.9kDa.ANKRD54 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ANKRD54 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ankyrin Repeat Domain 54 (ANKRD54), which is also known as LIAR contains 4 ANK repeats. ANKRD54 plays a vital role in regulating intracellular signaling events related with erythroid terminal differentiation. ANKRD54 interacts with LYN through ankyrin repeat region and the SH3-domain in an activation-independent status of LYN. ANKRD54 creates a multiprotein complex with LYN and HCLS1.

    • Synonyms

      LIAR, Lyn-interacting ankyrin repeat 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 MGSMAAAAGD ADDEPRSGHS SSEGECAVAP EPLTDAEGLF SFADFGSALG GGGAGLSGRA SGGAQSPLRY LHVLWQQDAE PRDELRCKIP AGRLRRAARP HRRLGPTGKE VHALKRLRDS ANANDVETVQ QLLEDGADPC AADDKGRTAL HFASCNGNDQ IVQLLLDHGA DPNQRDGLGN TPLHLAACTN HVPVITTLLR GGARVDALDR AGRTPLHLAK SKLNILQEGH AQCLEAVRLE VKQIIHMLRE YLERLGQHEQ RERLDDLCTR LQMTSTKEQV DEVTDLLASF TSLSLQMQSM EKR.

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    Ankrd54 Human
  • View Data Sheet

    Name :

    EEF2K Human

    Description:

    Eukaryotic Elongation Factor-2 Kinase Human Recombinant

    Eukaryotic Elongation Factor 2 Kinase, Calcium/Calmodulin-Dependent Eukaryotic Elongation Factor 2 Kinase, EEF-2 Kinase, EC 2.7.11.20, EEF-2K, Calcium/Calmodulin-Dependent Eukaryotic Elongation Factor-2 Kinase, Calmodulin-Dependent Protein Kinase III, Eukaroytic Elongation Factor 2 Kinase, Eukaryotic Elongation Factor-2 Kinase, Elongation Factor-2 Kinase, EC 2.7.11, HSU93850, Eukaryotic elongation factor 2 kinase.

    Product # :

    PKA-061

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    Description

    EEF2K Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 748 amino acids (1-725 a.a) and having a molecular mass of 84.6kDa. EEF2K is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EEF2K protein solution (0.25 mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eukaryotic elongation factor-2 kinase (EEF2K) is threonine kinase which regulates protein synthesis by means of controlling the rate of peptide chain elongation. Upon activation through a diversity of upstream kinases including AMPK or TRPM7, EEF2K phosphorylates the elongation factor EEF2 at a sole site, renders it unable to bind ribosomes and therefore inactive. In turn, the rate of protein synthesis is being reduced.

    • Synonyms

      Eukaryotic Elongation Factor 2 Kinase, Calcium/Calmodulin-Dependent Eukaryotic Elongation Factor 2 Kinase, EEF-2 Kinase, EC 2.7.11.20, EEF-2K, Calcium/Calmodulin-Dependent Eukaryotic Elongation Factor-2 Kinase, Calmodulin-Dependent Protein Kinase III, Eukaroytic Elongation Factor 2 Kinase, Eukaryotic Elongation Factor-2 Kinase, Elongation Factor-2 Kinase, EC 2.7.11, HSU93850, Eukaryotic elongation factor 2 kinase.

    • 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 MGSMADEDLI FRLEGVDGGQ SPRAGHDGDS DGDSDDEEGY FICPITDDPS SNQNVNSKVN KYYSNLTKSE RYSSSGSPAN SFHFKEAWKH AIQKAKHMPD PWAEFHLEDI ATERATRHRY NAVTGEWLDD EVLIKMASQP FGRGAMRECF RTKKLSNFLH AQQWKGASNY VAKRYIEPVD RDVYFEDVRL QMEAKLWGEE YNRHKPPKQV DIMQMCIIEL KDRPGKPLFH LEHYIEGKYI KYNSNSGFVR DDNIRLTPQA FSHFTFERSG HQLIVVDIQG VGDLYTDPQI HTETGTDFGD GNLGVRGMAL FFYSHACNRI CESMGLAPFD LSPRERDAVN QNTKLLQSAK TILRGTEEKC GSPRVRTLSG SRPPLLRPLS ENSGDENMSD VTFDSLPSSP SSATPHSQKL DHLHWPVFSD LDNMASRDHD HLDNHRESEN SGDSGYPSEK RGELDDPEPR EHGHSYSNRK YESDEDSLGS SGRVCVEKWN LLNSSRLHLP RASAVALEVQ RLNALDLEKK IGKSILGKVH LAMVRYHEGG RFCEKGEEWD QESAVFHLEH AANLGELEAI VGLGLMYSQL PHHILADVSL KETEENKTKG FDYLLKAAEA GDRQSMILVA RAFDSGQNLS PDRCQDWLEA LHWYNTALEM TDCDEGGEYD GMQDEPRYMM LAREAEMLFT GGYGLEKDPQ RSGDLYTQAA EAAMEAMKGR LANQYYQKAE EAWAQMEE.

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    Eef2K Human
  • View Data Sheet

    Name :

    TBCC Human

    Description:

    Tubulin Folding Cofactor C Human Recombinant

    Tubulin folding cofactor C, tubulin-specific chaperone c, Tubulin-folding cofactor C, CFC.

    Product # :

    PRO-1180

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    Description

    TBCC Human Recombinant produced in E. coli is a single polypeptide chain containing 369 amino acids (1-346) and having a molecular mass of 41.7 kDa.TBCC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tubulin folding cofactor C (TBCC) is a member of the TBCC family. TBCC has a role in the control of centrosome and Golgi apparatus positioning, with effects on cell shape and cell migration. Cofactor C is 1 of 4 proteins (cofactors A,D,E and C) engaged in the pathway leading to properly folded b-tubulin from folding intermediates. Cofactor E attaches to the cofactor D/beta-tubulin complex; their interaction with cofactor C subsequently causes the release of beta-tubulin polypeptides which are bound to the native state.

    • Synonyms

      Tubulin folding cofactor C, tubulin-specific chaperone c, Tubulin-folding cofactor C, CFC.

    • 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 MGSMESVSCS AAAVRTGDME SQRDLSLVPE RLQRREQERQ LEVERRKQKR QNQEVEKENS HFFVATFARE RAAVEELLER AESVERLEEA ASRLQGLQKL INDSVFFLAA YDLRQGQEAL ARLQAALAER RRGLQPKKRF AFKTRGKDAA SSTKVDAAPG IPPAVESIQD SPLPKKAEGD LGPSWVCGFS NLESQVLEKR ASELHQRDVL LTELSNCTVR LYGNPNTLRL TKAHSCKLLC GPVSTSVFLE DCSDCVLAVA CQQLRIHSTK DTRIFLQVTS RAIVEDCSGI QFAPYTWSYP EIDKDFESSG LDRSKNNWND VDDFNWLARD MASPNWSILP EEERNIQWD

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    Tbcc Human
  • View Data Sheet

    Name :

    PF4 Human, His

    Description:

    Platelet Factor-4 Human Recombinant (CXCL4), His Tag

    CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    Product # :

    CHM-015

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    Description

    PF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (32-101 a.a) and having a molecular mass of 10kDa.PF4 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PF4 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Human PF4 is used for the proof of heparin-induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.

    • Synonyms

      CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    • 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 MEAEEDGDLQ CLCVKTTSQV RPRHITSLEV IKAGPHCPTA QLIATLKNGR KICLDLQAPL YKKIIKKLLE S.

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    Pf4 Human His
  • View Data Sheet

    Name :

    FLRT3 Human, HEK

    Description:

    Fibronectin Leucine Rich Transmembrane Protein 3 Human Recombinant, HEK

    Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.

    Product # :

    PRO-2805

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    Description

    FLRT3 Human Recombinant is a single, glycosylated, polypeptide chain (29-528 a.a) containing a total of 506 amino acids and having a molecular mass of 57.3 kDa. FLRT3 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    FLRT3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    >40%.  Measured by the ability of the immobilized protein to support the adhesion of Neuro-2a neuroblast cells. When cells are added to human FLRT3 coated plates 5 ug/ml.

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    • Synonyms

      Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.

    • 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

      KSCPSVCRCD AGFIYCNDRF LTSIPTGIPE DATTLYLQNN QINNAGIPSD LKNLLKVERI YLYHNSLDEF PTNLPKYVKE LHLQENNIRT ITYDSLSKIP YLEELHLDDN SVSAVSIEEG AFRDSNYLRL LFLSRNHLST IPWGLPRTIE ELRLDDNRIS TISSPSLQGL TSLKRLVLDG NLLNNHGLGD KVFFNLVNLT ELSLVRNSLT AAPVNLPGTN LRKLYLQDNH INRVPPNAFS
      YLRQLYRLDM SNNNLSNLPQ GIFDDLDNIT QLILRNNPWY CGCKMKWVRD WLQSLPVKVN VRGLMCQAPE KVRGMAIKDL NAELFDCKDS GIVSTIQITT AIPNTVYPAQ GQWPAPVTKQ PDIKNPKLTK DHQTTGSPSR KTITITVKSV TSDTIHISWK LALPMTALRL SWLKLGHSPA FGSITETIVT GERSEYLVTA LEPDSPYKVC MVPMETSNLY LFDETPVCIE TETAPLRMYN
      PTTTLNREQE KEPYKNPNLP HHHHHH.

    • Background

      Fibronectin leucine-rich transmembrane protein 3, commonly known as FLRT3, stands as a molecular architect in the intricate landscape of neural development. Its roles, initially discovered in the embryonic nervous system, have expanded to encompass various physiological and pathological processes in both the brain and beyond. This research endeavors to unravel the enigma of FLRT3 protein, exploring its structural intricacies, physiological functions, and its far-reaching implications in neurobiology, embryogenesis, and disease. By delving into FLRT3's multifaceted roles, scientists aim to decipher the underlying mechanisms that govern its diverse functions and explore potential therapeutic avenues in the realms of neuroscience and beyond.

      Structural Complexities of FLRT3:

      FLRT3 belongs to the FLRT family, characterized by extracellular leucine-rich repeats (LRRs) and a transmembrane domain. These structural motifs enable FLRT3 to participate in a myriad of interactions, including binding with cell adhesion molecules and guidance cues. Understanding the three-dimensional architecture of FLRT3 is fundamental for unraveling its molecular partnerships, biological activities, and its contributions to cell adhesion and signaling.

      Physiological Functions in Neural Development:

      In the developing nervous system, FLRT3 acts as a guidance molecule, steering growing axons and dendrites to their precise destinations. Through interactions with other cell surface receptors and ligands, FLRT3 modulates axon pathfinding, synapse formation, and neuronal migration. Its presence in growth cones and developing neural circuits underscores its significance in sculpting the intricate neural networks essential for proper brain function.

      Beyond Neural Development:

      Beyond its canonical roles in neurodevelopment, FLRT3 has emerged as a versatile player in various physiological processes. It participates in tissue morphogenesis, modulates cell adhesion, and influences immune responses. Recent studies have also implicated FLRT3 in cancer progression, highlighting its involvement in pathological conditions and making it a potential target for therapeutic interventions in cancer therapy.

      FLRT3 as a Therapeutic Target:

      The diverse roles of FLRT3 in neural development and diseases position it as an attractive target for therapeutic interventions. Modulating FLRT3 interactions offers novel avenues for neurological disorder treatments, including neurodevelopmental disorders and neurodegenerative diseases. Moreover, understanding FLRT3's involvement in cancer biology opens doors for innovative cancer therapies, making it a promising target for precision medicine approaches.

      FLRT3, with its intricate structural features and diverse functional roles, stands as a linchpin in the realms of neuroscience, embryogenesis, and disease. Its multifaceted contributions to neural development, tissue morphogenesis, and disease pathogenesis underscore its significance in both health and pathology. As researchers continue to unravel FLRT3’s complexities, they not only deepen our understanding of fundamental biological processes but also pave the way for groundbreaking discoveries in neuroscience and therapeutic interventions, ultimately shaping the future landscape of medicine and scientific inquiry.

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    Flrt3 Protein
  • View Data Sheet

    Name :

    Leptin N82K Human, PEG

    Description:

    Leptin N82K Human Recombinant, Pegylated

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1107

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    Description

    Pegylated Leptin N82K Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Pegylated Leptin N82K Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3 Having 35-40% protein.

    Purity

    Greater than 99.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Leptin Human is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated Leptin in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo Pegylated Leptin has profound weight reducing effect (as compared to the non-pegylated recombinant human leptin), resulting mainly from reduced food intake.

    More Info

    • Introduction

      Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pegylated Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Pegylated Leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Leptin Mutant Protein
  • View Data Sheet

    Name :

    UGDH Mouse

    Description:

    UDP-Glucose Dehydrogenase Mouse Recombinant

    GDH, UDP-GlcDH, UDPGDH, UGD, EC=1.1.1.22, UDP-Glc dehydrogenase, UDP-glucose 6-dehydrogenase, UGDH.

    Product # :

    ENZ-1070

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    Description

    UGDH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-493a.a.) and having a molecular mass of 57.2kDa. UGDH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UGDH protein solution (0.5mg/ml) containing 20mM MES buffer (pH5.0), 20% glycerol 150mM NaCl and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,500 pmol/min/ug, and is defined as the amount of enzyme that converts 1.0 pmole of UDP-glucose to UDP-glucuronate per minute at pH 8.7 at 37°C.

    More Info

    • Introduction

      UGDH is part of the UDP-glucose/GDP-mannose dehydrogenase family and is a widely expressed enzyme localized in the liver. UGDH transfers UDP-glucose to UDP-glucuronate and thus takes part in the biosynthesis of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosylated products are ordinary molecules of the extracellular matrix and participate in signal transduction, cell migration, and cancer growth and metastasis.

    • Synonyms

      GDH, UDP-GlcDH, UDPGDH, UGD, EC=1.1.1.22, UDP-Glc dehydrogenase, UDP-glucose 6-dehydrogenase, UGDH.

    • 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). Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMVEIKKI CCIGAGYVGG PTCSVIAHMC PEIRVTVVDV NEARINAWNS PTLPIYEPGL KEVVESCRGK NLFFSTNIDD AIREADLVFI SVNTPTKTYG MGKGRAADLK YIEACARRIV QNSNGYKIVT EKSTVPVRAA ESIRRIFDAN TKPNLNLQVL SNPEFLAEGT AIKDLKNPDR VLIGGDETPE GQKAVRALCA VYEHWVPKEK ILTTNTWSSE LSKLAANAFL AQRISSINSI SALCEATGAD VEEVATAIGM DQRIGNKFLK ASVGFGGSCF QKDVLNLVYL CEALNLPEVA RYWQQVIDMN DYQRRRFASR IIDSLFNTVT DKKIAILGFA FKKDTGDTRE SSSIYISKYL MDEGAHLHIY DPKVPREQIV VDLSHPGVSA DDQVSRLVTI SKDPYEACDG AHALVICTEW DMFKELDYER IHKKMLKPAF IFDGRRVLDG LHSELQTIGF QIETIGKKVS SKRIPYTPGE IPKFSLQDPP NKKPKV.

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    Ugdh Mouse
  • View Data Sheet

    Name :

    MAPK10 Human

    Description:

    Mitogen-Activated Protein Kinase 10 Human Recombinant

    C-Jun N-Terminal Kinase 3, MAP Kinase P49 3F12, MAP Kinase 10, PRKM10, SAPK1b, JNK3A, JNK3.

    Product # :

    PKA-115

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    Description

    MAPK10 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 470 amino acids (1-464 a.a.) and having a molecular mass of 53.4kDa. MAPK10 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MAPK10 is protein solution ( 0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 30% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAPK10 is part of the MAP kinase protein family. MAP Kinases perform as assimilation point for many biochemical pathways. The enzyme also takes part in wide range of cellular pathways: differentiation, proliferation, development and transcription regulation.

    • Synonyms

      C-Jun N-Terminal Kinase 3, MAP Kinase P49 3F12, MAP Kinase 10, PRKM10, SAPK1b, JNK3A, JNK3.

    • 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

      MSLHFLYYCS EPTLDVKIAF CQGFDKQVDV SYIAKHYNMS KSKVDNQFYS VEVGDSTFTV LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ NQTHAKRAYR ELVLMKCVNH KNIISLLNVF TPQKTLEEFQ DVYLVMELMD ANLCQVIQME LDHERMSYLL YQMLCGIKHL HSAGIIHRDL KPSNIVVKSD CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY KENVDIWSVG CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV DDALQHPYIN VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN SEEKTKNGVV KGQPSPSGAA VNSSESLPPS SSVNDISSMS TDQTLASDTD SSLEASAGPL GCCRHHHHHH.

    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.

    Mapk10 Human
  • View Data Sheet

    Name :

    RABL5 Human

    Description:

    RAB, Member RAS Oncogene Family-Like 5 Human Recombinant

    Rab-like protein 5 isoform a, Rab-like protein 5, RABL5, RAB, Member RAS Oncogene Family-Like 5.

    Product # :

    PRO-1472

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    RABL5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (1-185) and having a molecular mass of 23.2 kDa. RABL5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RABL5 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      RAB, Member RAS Oncogene Family-Like 5 (RABL5) belongs to the Ras superfamily of small GTP-binding proteins. The Ras-related superfamily of guanine nucleotide binding proteins includes the R-Ras, Rap, Ral/Rec and Rho/Rab subfamilies. Rab proteins have an essential role in endocytosis or in biosynthetic protein transport. The transporting process of newly synthesized proteins from the endoplasmic reticulum to various stacks of the Golgi complex and to secretory vesicles includes the movement of carrier vesicles and requires Rab protein function.

    • Synonyms

      Rab-like protein 5 isoform a, Rab-like protein 5, RABL5, RAB, Member RAS Oncogene Family-Like 5.

    • 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 MGSMLKAKIL FVGPCESGKT VLANFLTESS DITEYSPTQG VRILEFENPH VTSNNKGTGC EFELWDCGGD AKFESCWPAL MKDAHGVVIV FNADIPSHRK EMEMWYSCFV QQPSLQDTQC MLIAHHKPGS GDDKGSLSLS PPLNKLKLVH SNLEDDPEEI RMEFIKYLKS IINSMSESRD REEMSIMT.

    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.

    Rabl5 Human
  • View Data Sheet

    Name :

    CCL13 Human, His

    Description:

    Monocyte Chemotactic Protein-4 Human Recombinant (CCL13), His-Tag

    CKb10, MCP-4, NCC-1, NCC1, SCYA1, SCYL1, CK-beta-10, Small-inducible cytokine A13.

    Product # :

    CHM-275

    Price :

    Quantity :

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    • description
    • source
    • formulation
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    Description

    MCP4 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 96 amino acids (24-98) and having a molecular mass of 10.8 kDa. The MCP-4 is fused to 21 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The His Tag 0.25mg/ml MCP4 protein solution contains PBS pH-7.4, 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCL13 chemokine is part of the CC chemokine family (TARC). CCL13 protein induces chemotaxis in monocytes, eosinophils, T lymphocytes, and basophils by binding cell surface G-protein linked chemokine receptors such as CCR2, CCR3 and CCR5. CCL13 is induced by the inflammatory cytokines IL1 & TNFA.

    • Synonyms

      CKb10, MCP-4, NCC-1, NCC1, SCYA1, SCYL1, CK-beta-10, Small-inducible cytokine A13.

    • 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. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQPDALNVPS TCCFTFSSKK ISLQRLKSYV ITTSRCPQKA VIFRTKLGKE ICADPKEKWV QNYMKHLGRK
      .AHTLKT

    • Background

      What is the molecular weight/Mw of CCL13 HUMAN, HIS Protein?
      CCL13 HUMAN, HIS Protein has a total Mw of 10.8kDa.

      What is the source or expression system of CCL13 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL13 HUMAN, HIS Protein?
      CCL13 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL13 HUMAN, HIS Protein?
      The biological functionality of CCL13 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL13 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MQPDALNVPS TCCFTFSSKK ISLQRLKSYV ITTSRCPQKA VIFRTKLGKE ICADPKEKWV QNYMKHLGRK
      .AHTLKT

      What applications can CCL13 HUMAN, HIS Protein be used in?
      CCL13 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL13 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL13 HUMAN, HIS Protein was purified using conventional chromatography techniques.

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

    Mcp4 Human His
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