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Search results

896 results found for “cysteine-rich secretory protein”

Name

Description

Product #

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  • View Data Sheet

    Name :

    GCHFR Human

    Description:

    GTP Cyclohydrolase I Feedback Regulator Human Recombinant

    GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR

    Product # :

    PRO-2006

    Price :

    Quantity :

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    • description
    • source
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    • More Info

    Description

    GCHFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 107 amino acids (1-84a.a) and having a molecular mass of 12.1kDa. GCHFR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GCHFR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 40% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GTP Cyclohydrolase I Feedback Regulator, also known as GCHFR, is a Protein coding gene which includes a homodimer. GCHFR binds and mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase I. GCHFR also regulates phenylalanine metabolism in the liver and in the production of biogenic amine neurotransmitters and nitric oxide.

    • Synonyms

      GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR

    • 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 MGSMPYLLIS TQIRMEVGPT MVGDEQSDPE LMQHLGASKR RALGNNFYEY YVDDPPRIVL DKLERRGFRV LSMTGVGQTL VWCLHKE.

    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.

    Gchfr Human
  • View Data Sheet

    Name :

    MAPT Human 383a.a.

    Description:

    Microtubule-Associated Protein Tau 383 a.a. Human Recombinant

    Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.

    Product # :

    PRO-012

    Price :

    Quantity :

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    Description

    MAPT Human Recombinant (Isoform 3) fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 403 amino acids (1-383 a.a.) and having a molecular mass of 42.1kDa (Molecular size on SDS-PAGE will appear higher). The MAPT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAPT is a neuronal microtubule associated protein localized mostly on axons.
      MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain.

    • Synonyms

      Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.

    • 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 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL.

    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.

    Mapt Human 383Aa
  • View Data Sheet

    Name :

    CBFB HUman

    Description:

    Core Binding Factor Beta Human Recombinant

    PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.

    Product # :

    PRO-534

    Price :

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    Description

    CBFB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-202 a.a.) and having a molecular mass of 23.6 kDa. The CBFB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.5mg/ml solution containing 20mM MES pH-6, 0.1mM PMSF & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CBFB beta subunit is a heterodimeric core-binding transcription factor that is part of the PEBP2/CBF transcription factor family which controls a host of genes particulary to hematopoiesis and osteogenesis. CBFB is a non-DNA binding regulatory subunit which increases DNA binding by alpha subunit.

    • Synonyms

      PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      CBFB Human although stable at 4C for 1 week, should be stored below -18C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QARFQNACRD GRSEIAFVAT GTNLSLQFFP
      ASWQGEQRQT PSREYVDLER EAGKVYLKAP MILNGVCVIW KGWIDLQRLD GMGCLEFDEE RAQQEDALAQ QAFEEARRRT REFEDRDRSH
      REEMEVRVSQ LLAVTGKKTT RP.

    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.

    Cbfb Human
  • View Data Sheet

    Name :

    PF 4 Protein

    Description:

    Platelet Factor-4 Human (CXCL4)

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

    Product # :

    CHM-234

    Price :

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    More Info

    • description
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    • More Info

    Description

    Human PF-4 a 7.8 kDa protein consisting of 70 amino acid residues.

    Source

    Human Platelets.

    Formulation

    The CXCL4 protein was lyophilized in PBS buffer pH-7.4.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis 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 white lyophilized powder.

    • Stability

      Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first four N-terminal amino acids was determined and was found to be Glu-Ala-Glu-Glu.

    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.

    Pf 4 Human
  • View Data Sheet

    Name :

    GHRL Protein

    Description:

    Ghrelin Human

    Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.

    Product # :

    HOR-297

    Price :

    Quantity :

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    More Info

    • description
    • formulation
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    • More Info

    Description

    Ghrelin Human contains 28 amino acids and a total molecular mass of 3370.9 Dalton and a molecular formula of C149H249N47O42.The GHRL is purified by proprietary chromatographic techniques.

    Formulation

    GHRL was lyophilized without additives.

    Purity

    Greater than 97% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.

    • Synonyms

      Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.

    • Physical Appearance

      Sterile Filtered Yellowish lyophilized (freeze-dried) powder that may appear as a gel form.

    • Stability

      Store the lyophilized Ghrelin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted GHRL 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 a working concentration approximately 0.5mg/1ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      Gly-Ser-Ser(n-octanoyl)-Phe-Leu-Ser-Pro-Glu-His-Gln-Arg-Val-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH.

    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.

    Ghrelin Human
  • View Data Sheet

    Name :

    GTSF1 Human

    Description:

    Gametocyte Specific Factor 1 Human Recombinant

    Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.

    Product # :

    PRO-561

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    Description

    GTSF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167) and having a molecular mass of 21.7 kDa.GTSF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GTSF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Gametocyte Specific Factor 1 (GTSF1) is a member of the UPF0224 (FAM112) family and contains 1 CHHC-type zinc finger. A key paralog of the GTSF1 gene is GTSF1L.

    • Synonyms

      Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.

    • 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 MGSMEETYTD SLDPEKLLQC PYDKNHQIRA CRFPYHLIKC RKNHPDVASK LATCPFNARH QVPRAEISHH ISSCDDRSCI EQDVVNQTRS LRQETLAEST WQCPPCDEDW DKDLWEQTST PFVWGTTHYS DNNSPASNIV TEHKNNLASG MRVPKSLPYV LPWKNNGNAQ.

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    Gtsf1 Human
  • View Data Sheet

    Name :

    OmpA

    Description:

    Outer Membrane Protein-A Bacterial Recombinant

    Outer Membrane Protein-A, OmpA.

    Product # :

    PRO-571

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    Description

    The recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 50.5 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing polyclonal and monoclonal antibodies in ELISA and Western Blot techniques. All forms of A-protein were found to activate the secretion of tumour necrosis factor alpha from murine macrophage. For ref see Maurice et al. (1999) Protein Expression and Purification 16, 396-404.The OmpA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OmpA protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

    The interaction of bacterial and recombinant A-layer protein with murine macrophages was directed at determining the effect of A-protein on intracellular events that occur in primed macrophages. This was accomplished by measuring the cytotoxic product produced by peritoneal macrophages when exposed to A-protein coated latex beads. Thioglycolate elicited macrophages exhibited a low level of activation (18% cytotoxicity) that was significantly increased (48% cytotoxicity) in the presence of latex beads. Coating of the latex beads with each of the three A-protein products resulted in an increase of cytoxicity (mean +/- SEM) from 48% to 91%.

    More Info

    • Introduction

      The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.

    • Synonyms

      Outer Membrane Protein-A, OmpA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      mdvvispndn tfvttslasv tkqpvldfst aqqnltlnfs evgdlknngf ivleiqgegq fndaeirqwl sngfwrrpft gllvnpndhg nfansgevnd vrkffkiisd gtqltivhti dsngkrlrla lasdveetin fadaevelkl nlanqafklt sgsqgtvalt agalwnasyt adpvatkplf klgklfqlsl tnagkatalv segflklnig danisatdfa itnvttnqti qrdkvnltlt gdvsafkkda ngnlvnkaga sigwkaaadg qsatavlgag nmaggvqnal aafgtlyvaa dntvpvpavn fnvkaeiqgd sqatynyfkd eladlfiltr dgmkfdtitt gttsanlihi rdvsnilpte ggkifvtite yadhaangrg egtvlvtrka lsvtlpsgga vtlkpadvaa dvgasitagr qarlvfevet nqgevavkks naegvdiqng trgtaplvdf tl.

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    Outer Membrane Protein A
  • View Data Sheet

    Name :

    NEFL Bovine

    Description:

    Neurofilament Light Bovine

    Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    Product # :

    PRO-2786

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    Description

    NEFL Bovine having a calculated molecular mass of 68 kDa, pI-5.0.

    Source

    Bovine spinal cord.

    Formulation

    NEFL was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized NEFL between 2-8°C, do not freeze. Upon reconstitution NEFL should be stored at -20°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Background

      Neurofilament light chain (NEFL) is a critical component of the neuronal cytoskeleton, primarily found in neurons of the central and peripheral nervous systems. While extensive research has been conducted on NEFL in human and rodent models, the study of NEFL in bovine nervous tissues is an emerging area with potential for advancing our understanding of neuronal biology in larger mammals and its applications in veterinary medicine and neurobiology.

      Bovine nervous tissues, such as the brain and spinal cord, are of particular interest due to their relevance in cattle health and the food industry. This research aims to provide a comprehensive exploration of NEFL in bovine nervous tissues, elucidating its functions, structural significance, and potential applications.

      The primary objective of this research is to elucidate the role of NEFL in bovine nervous tissues, particularly in maintaining the structural integrity of neurons and axons. In vitro and ex vivo experiments, utilizing bovine neuronal cell cultures and tissue specimens, will be conducted to investigate how NEFL contributes to neuronal morphology, axonal transport, and neuronal resilience. Understanding these mechanisms is fundamental for deciphering the complexities of neuronal biology in bovine species.

      The second objective is to assess the relevance of bovine NEFL in veterinary medicine. Studies involving bovine models will be conducted to evaluate the impact of NEFL mutations or variations on neuronal health, disease susceptibility, and neurodegenerative conditions. These investigations may provide valuable insights into potential applications in cattle health and the development of diagnostic tools for neurological disorders.

      The third objective is to explore the potential applications of bovine NEFL in neurobiology and biotechnology. Research will investigate the use of bovine NEFL-expressing cells as models for studying neuronal-related diseases and for developing tissue engineering approaches for veterinary medicine and biotechnology.

      By delving into the functions and roles of NEFL in bovine nervous tissues, this research aims to expand our knowledge of neuronal biology, its implications for veterinary medicine, and its potential applications in neurobiology and cattle health

    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.

    Nefl Bovine
  • View Data Sheet

    Name :

    TULP1 Human

    Description:

    Tubby Like Protein 1 Human Recombinant

    Tubby like protein 1, TUBL1, RP14, LCA15, tubby-related protein 1.

    Product # :

    PRO-1191

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    Description

    TULP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 276 amino acids (290-542) and having a molecular mass of 31.1 kDa.TULP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TULP1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tubby-related protein 1 (TULP1) belongs to the TULP family of 4 proteins (TUB and TULP1, -2, and -3), categorized structurally by the highly conserved C-terminal half of the protein. Tubby-like gene family (TULPs) members are found in plants, vertebrates, and invertebrates and encode proteins of unknown function. TULP proteins share a conserved C-terminal region of roughly 200 amino acid residues. In the retina, TULP1 is observed exclusively in the photoreceptor cells, localizing predominantly in the inner segments and connecting cilium and to a lesser degree in the perinuclear cytoplasm and synaptic termini. TULP1 gene mutations are linked with retinitis pigmentosa.

    • Synonyms

      Tubby like protein 1, TUBL1, RP14, LCA15, tubby-related protein 1.

    • 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 MGSEPREFVL RPAPQGRTVR CRLTRDKKGM DRGMYPSYFL HLDTEKKVFL LAGRKRKRSK TANYLISIDP TNLSRGGENF IGKLRSNLLG NRFTVFDNGQ NPQRGYSTNV ASLRQELAAV IYETNVLGFR GPRRMTVIIP GMSAENERVP IRPRNASDGL LVRWQNKTLE SLIELHNKPP VWNDDSGSYT LNFQGRVTQA SVKNFQIVHA DDPDYIVLQF GRVAEDAFTL DYRYPLCALQ AFAIALSSFD GKLACE

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    Tulp1 Human
  • View Data Sheet

    Name :

    Protein-A/G/L

    Description:

    Protein A/G/L Recombinant

    Product # :

    PRO-1936

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    Description

    Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 805 amino acids in total and having a molecular mass of 89.2kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    More Info

    • Introduction

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

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    Protein A G L
  • View Data Sheet

    Name :

    SNTN Human

    Description:

    Sentan Cilia Apical Structure Protein Human Recombinant

    Sentan cilia apical structure protein, FLJ44379, S100AL, S100A1L, S100A-like protein, sentan, S100 calcium-binding protein A1-like.

    Product # :

    PRO-216

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    Description

    SNTN 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 167 amino acids (1-147a.a.) and having a molecular mass of 18.6kDa. The SNTN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNTN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.15M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNTN is a member of to the S-100 family. SNTN is localized solely to the bridging structure between the cell membrane and peripheral singlet microtubules that specifically exists in the narrowed distal portion of cilia. Exogenously expressed sentan displayed affinity for the membrane protrusions, and a protein-lipid binding assay discovered that sentan bounds to phosphatidylserine which indicate that sentan is the leading molecular component of the ciliary tip to link the cell membrane and peripheral singlet microtubules, making the distal portion of the cilia narrow and stiff to permit better airway approval or ovum transport.

    • Synonyms

      Sentan cilia apical structure protein, FLJ44379, S100AL, S100A1L, S100A-like protein, sentan, S100 calcium-binding protein A1-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 MGGCMHSTQD KSLHLEGDPN PSAAPTSTCA PRKMPKRISI SKQLASVKAL RKCSDLEKAI ATTALIFRNS SDSDGKLEKA IAKDLLQTQF RNFAEGQETK PKYREILSEL DEHTENKLDF EDFMILLLSI TVMSDLLQNI RNVKIMK

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    Sntn Human
  • View Data Sheet

    Name :

    CXCL1 Mouse

    Description:

    GRO1/KC Mouse Recombinant (CXCL1)

    Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.

    Product # :

    CHM-335

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    Description

    KC Mouse Recombinant also known as N51 and GRO-1 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of approximately 7.8 kDa. The GRO-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) was lyophilized from 20mM phosphate buffer pH-7.4 and 0.1M NaCl.

    Purity

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

    Biological Activity

    The biological activity was determined by measuring the ability to chemoattrat human neutrophilsat a concentration of 10ng/ml-100ng/ml.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophils and epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.

    • Synonyms

      Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KC Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 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 GRO1 Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APIANELRCQ CLQTMAGIHL KNIQSLKVLP SGPHCTQTEV IATLKNGREA CLDPEAPLVQ KIVQKMLKGV PK.

    • Background

      What is the molecular weight/Mw of CXCL1 MOUSE Protein?
      CXCL1 MOUSE Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CXCL1 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL1 MOUSE Protein?
      CXCL1 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL1 MOUSE Protein?
      The biological activity was determined by measuring the ability to chemoattrat human neutrophilsat a concentration of 10ng/ml-100ng/ml.

      What is the amino acid sequence of CXCL1 MOUSE Protein?
      APIANELRCQ CLQTMAGIHL KNIQSLKVLP SGPHCTQTEV IATLKNGREA CLDPEAPLVQ KIVQKMLKGV PK.

      What applications can CXCL1 MOUSE Protein be used in?
      CXCL1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL1 MOUSE Protein?
      The endotoxin level is minimal, CXCL1 MOUSE Protein was purified using conventional chromatography techniques.


    • Protein content

      Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.03 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 standard solution of KC as a Reference Standard.

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    Gro A Mouse
  • View Data Sheet

    Name :

    GroES Human, His

    Description:

    GroES (HSP10) Human Recombinant, His Tag

    CPN10, GROES, HSP10, HSPE1, Chaperonin-10, 10 kDa heat shock protein mitochondrial, 10 kDa chaperonin, Early-pregnancy factor, EPF.

    Product # :

    HSP-040

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    Description

    GroES His Protein is 12.0 kDa protein containing 111 amino acid residues of the GroES Human and the 10 aa N-Terminal His-tag.

    Source

    E. coli

    Formulation

    GroES His Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 0.05M phosphate buffer, 0.075 M NaCl, pH 7.4.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      HSP10 is part of the molecular chaperons, that are crucial for thir efficient folding of proteins in normal as well as stress conditions. GroES function is to bind to HSP60 in the presence of ATP, thus causing a change in the HSP60 conformation & enclosing the protein substrate within the complex. ATP hydrolysis by chaperonin-60 which destabilizes the HSP10-HSP60 complex, thereby allowing it to dissociate and secrete the substrate protein. GroES having the NCBI accession number of NP_002148 was purified by using conventional chromatography techniques.

    • Synonyms

      CPN10, GROES, HSP10, HSPE1, Chaperonin-10, 10 kDa heat shock protein mitochondrial, 10 kDa chaperonin, Early-pregnancy factor, EPF.

    • Stability

      Store lyophilized GroES His at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted GroES His 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.

    • Amino Acid Sequence

      MKHHHHHHAS AGQAFRKFLP LFDRVLVERS AAETVTKGGI MLPEKSQGKV LQATVVAVGS GSKGKGGEIQ PVSVKVGDKV LLPEYGGTKV VLDDKDYFLF RDGDILGKYV D.

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    Groes His Human
  • View Data Sheet

    Name :

    UXT Human

    Description:

    Ubiquitously-Expressed, Prefoldin-Like Chaperone Human Recombinant

    Protein UXT, Androgen receptor trapped clone 27 protein, ART-27, Ubiquitously expressed transcript protein, UXT, HSPC024, STAP1.

    Product # :

    PRO-1312

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    Description

    UXT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (1-157 a.a.) and having a molecular mass of 20.4kDa.UXT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitously-expressed transcript (UXT) is a member of the UXT family. UXT serves as a cofactor which modulates androgen receptor-dependent transcription, and also has a crucial role in tumor necrosis factor-induced apoptosis. UXT gene expression has a role in tumorigenesis. UXT is ubiquitous expressed: it is expressed in prostate epithelial cells, overexpressed in a number of tumor tissues. The highest levels are found in the heart, skeletal muscle, pancreas, kidney, liver, adrenal gland, peripheral blood leukocytes, lymph node, prostate, and thyroid and the lowest levels in bladder and uterus.

    • Synonyms

      Protein UXT, Androgen receptor trapped clone 27 protein, ART-27, Ubiquitously expressed transcript protein, UXT, HSPC024, STAP1.

    • 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 MATPPKRRAV EATGEKVLRY ETFISDVLQR DLRKVLDHRD KVYEQLAKYL QLRNVIERLQ EAKHSELYMQ VDLGCNFFVD TVVPDTSRIY VALGYGFFLE LTLAEALKFI DRKSSLLTEL SNSLTKDSMN IKAHIHMLLE GLRELQGLQN FPEKPHH.

    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.

    Uxt Human
  • View Data Sheet

    Name :

    CARHSP1 Human

    Description:

    Calcium Regulated Heat Stable Protein 1 Human Recombinant

    Calcium-regulated heat stable protein 1, Calcium-regulated heat-stable protein of 24 kDa, CRHSP-24, CARHSP1, asCSDC1, MGC111446.

    Product # :

    PRO-257

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    Description

    CRAHSP1 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 167 amino acids (1-147 a.a.) and having a molecular mass of 18kDa. The CRAHSP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRAHSP1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRAHSP1 is a serine phosphoprotein initially identified as a physiological substrate for the Ca2+-calmodulin regulated protein phosphatase calcineurin (PP2B). CRAHSP1 interacts with the STYX/dead phosphate protein in developing spermatids and is a paralog of the brain-specific mRNA-binding protein PIPPIN. It is believed to have a common role in calcium-mediated signal transduction resulting from phosphorylation on serine residues.

    • Synonyms

      Calcium-regulated heat stable protein 1, Calcium-regulated heat-stable protein of 24 kDa, CRHSP-24, CARHSP1, asCSDC1, MGC111446.

    • 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 MSSEPPPPPQ PPTHQASVGL LDTPRSRERS PSPLRGNVVP SPLPTRRTRT FSATVRASQG PVYKGVCKCF CRSKGHGFIT PADGGPDIFL HISDVEGEYV PVEGDEVTYK MCSIPPKNEK LQAVEVVITH LAPGTKHETW SGHVISS.

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    Carhsp1 Human
  • View Data Sheet

    Name :

    CINP Human

    Description:

    Cyclin-Dependent Kinase 2 Interacting Protein Human Recombinant

    Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.

    Product # :

    PKA-269

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    Description

    CINP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212) and having a molecular mass of 26.4 kDa.The CINP is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CINP protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CINP is a member of the CINP family. CINP cooperates with the components of the replication complex and 2 kinases, CDK2 and CDC7, to provide a working and physical link between CDK2 and CDC7 throughout the firing of the origins of replication.

    • Synonyms

      Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.

    • Physical Appearance

      CINP is supplied as a 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 MEAKTLGTVT PRKPVLSVSA RKIKDNAADW HNLILKWETL NDAGFTTANN IANLKISLLN KDKIELDSSS PASKENEEKV CLEYNEELEK LCEELQATLD GLTKIQVKME KLSSTTKGIC ELENYHYGEE SKRPPLFHTW PTTHFYEVSH KLLEMYRKEL LLKRTVAKEL AHTGDPDLTL SYLSMWLHQP YVESDSRLHL ESMLLETGHR AL

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

    Cinp Human
  • View Data Sheet

    Name :

    SKP E. Coli

    Description:

    Chaperone Protein SKP E.Coli Recombinant

    hlpA, ompH, Chaperone protein skp, skp.

    Product # :

    HSP-034

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    Description

    SKP Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (21-161 a.a.) and having a molecular mass of 17.9 kDa. The SKP is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SKP E.Coli solution containing 20mM Tris-HCl pH-8 & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SKP is a 17kDa trimeric periplasmic chaperone that supports outer membrane proteins in their folding and insertion into membranes. SKP protein is necessary for the normal release of ompA from the inner membrane, the maintenance of its solubility in the periplasm, and, in association with lipopolysaccharide (LPS), for the efficient folding and insertion of ompA into the outer membrane.

    • Synonyms

      hlpA, ompH, Chaperone protein skp, skp.

    • 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 MADKIAIVNM GSLFQQVAQK TGVSNTLENE FKGRASELQR METDLQAKMK KLQSMKAGSD RTKLEKDVMA QRQTFAQKAQ AFEQDRARRS NEERGKLVTR IQTAVKSVAN SQDIDLVVDA NAVAYNSSDV KDITADVLKQ VK.

    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.

    Skp E Coli
  • View Data Sheet

    Name :

    GCSH Human

    Description:

    Glycine Cleavage System Protein H Human Recombinant

    Glycine cleavage system protein H (aminomethyl carrier), NKH, GCE, Lipoic acid-containing protein, Mitochondrial glycine cleavage system H-protein.

    Product # :

    PRO-973

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    Description

    GCSH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (48-173) and having a molecular mass of 16.4 kDa.GCSH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      There are four mitochondrial proteins composing the enzyme system for cleavage of glycine (glycine cleavage system): P protein, H protein, T protein, and L protein. GCSH is the H protein. GCSH transfers the methylamine group of glycine from the P protein to the T protein. Mutations in this gene results in nonketotic hyperglycinemia (NKH).

    • Synonyms

      Glycine cleavage system protein H (aminomethyl carrier), NKH, GCE, Lipoic acid-containing protein, Mitochondrial glycine cleavage system H-protein.

    • 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 MGSMSVRKFT EKHEWVTTEN GIGTVGISNF AQEALGDVVY CSLPEVGTKL NKQDEFGALE SVKAASELYS PLSGEVTEIN EALAENPGLV NKSCYEDGWL IKMTLSNPSE LDELMSEEAY EKYIKSIEE

    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.

    Gcsh Human
  • View Data Sheet

    Name :

    GCSF Rat

    Description:

    Granulocyte-Colony Stimulating Factor Rat Recombinant

    Granulocyte colony stimulating factor, Protein Csf3, Csf3.

    Product # :

    CYT-940

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    Description

    GCSF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 21.5kDa.The G-CSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in 5mM Sodium Citrate, pH 4.0.

    Purity

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

    Biological Activity

    The ED50 determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 107 IU/mg.

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

    • Synonyms

      Granulocyte colony stimulating factor, Protein Csf3, Csf3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.

    • Background

      What is the molecular weight/Mw of G CSF RAT Protein?
      G CSF RAT Protein has a total Mw of 21.5kDa.

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

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

      What is the Biological Activity of G CSF RAT Protein?
      The ED50 determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 107 IU/mg.

      What is the amino acid sequence of G CSF RAT Protein?
      KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.

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

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


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    Gcsf Rat
  • View Data Sheet

    Name :

    YWHAG Human, His

    Description:

    Tyr-3/Trp-5 Monooxygenase Activation Protein Gamma Human Recombinant, His Tag

    14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

    Product # :

    PKA-262

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    Description

    YWHAG Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids (2-247) and having a molecular mass of 36 kDa. YWHAG is fused to His Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    YWHAG solution containing 1x PBS and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.

    • Synonyms

      14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

    • 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. Avoid multiple freeze-thaw cycles.

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

    Ywhag Human His
  • View Data Sheet

    Name :

    KRT5 Human

    Description:

    Cytokeratin 5 Human Recombinant

    Keratin 5, KRT5, EBS2, Epidermolysis Bullosa Simplex 2 Dowling-Meara/Kobner/Weber-Cockayne Types, Keratin 5 (Epidermolysis Bullosa Simplex,Dowling-Meara/Kobner/Weber-Cockayne Types), 58 KDa Cytokeratin, Type-II Keratin Kb5, CK-5, K5, DDD1, CK5, DDD, KRT5A, cytokeratin-5, Keratin, Type II Cytoskeletal 5, Cytokeratin-5, Keratin-5.

    Product # :

    PRO-1940

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    Description

    KRT5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 613 amino acids (1-590) and having a molecular mass of 64.8 kDa.KRT5 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The KRT5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokeratin 5 (KRT5) belongs to the keratin gene family. The type II cytokeratins are comprised of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed throughout differentiation of simple and stratified epithelial tissues. The type II cytokeratins are clustered in a region of chromosome 12q12-q13. The KRT5 type II cytokeratin is specifically expressed in the basal layer of the epidermis with family member KRT14. Mutations in these genes are linked with a complex of diseases termed epidermolysis bullosa simplex.

    • Synonyms

      Keratin 5, KRT5, EBS2, Epidermolysis Bullosa Simplex 2 Dowling-Meara/Kobner/Weber-Cockayne Types, Keratin 5 (Epidermolysis Bullosa Simplex,Dowling-Meara/Kobner/Weber-Cockayne Types), 58 KDa Cytokeratin, Type-II Keratin Kb5, CK-5, K5, DDD1, CK5, DDD, KRT5A, cytokeratin-5, Keratin, Type II Cytoskeletal 5, Cytokeratin-5, Keratin-5.

    • 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 MGSMSRQSSV SFRSGGSRSF STASAITPSV SRTSFTSVSR SGGGGGGGFG RVSLAGACGV GGYGSRSLYN LGGSKRISIS TSGGSFRNRF GAGAGGGYGF GGGAGSGFGF GGGAGGGFGL GGGAGFGGGF GGPGFPVCPP GGIQEVTVNQ SLLTPLNLQI DPSIQRVRTE EREQIKTLNN KFASFIDKVR FLEQQNKVLD TKWTLLQEQG TKTVRQNLEP LFEQYINNLR RQLDSIVGER GRLDSELRNM QDLVEDFKNK YEDEINKRTT AENEFVMLKK DVDAAYMNKV ELEAKVDALM DEINFMKMFF DAELSQMQTH VSDTSVVLSM DNNRNLDLDS IIAEVKAQYE EIANRSRTEA ESWYQTKYEE LQQTAGRHGD DLRNTKHEIS EMNRMIQRLR AEIDNVKKQC ANLQNAIADA EQRGELALKD ARNKLAELEE ALQKAKQDMA RLLREYQELM NTKLALDVEI ATYRKLLEGE ECRLSGEGVG PVNISVVTSS VSSGYGSGSG YGGGLGGGLG GGLGGGLAGG GSGSYYSSSS GGVGLSGGLS VGGSGFSASS GRGLGVGFGS GGGSSSSVKF VSTTSSSRKS FKS.

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    Krt5 Human
  • View Data Sheet

    Name :

    SYT13 Human

    Description:

    Synaptotagmin XIII Human Recombinant

    Synaptotagmin XIII, KIAA1427, synaptotagmin-13, sytXIII.

    Product # :

    PRO-1550

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    Description

    SYT13 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 420 amino acids (30-426) and having a molecular mass of 46.5kDa.SYT13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SYT13 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT, 1mM PMSF, 1mM EDTA and 30% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SYT13 belongs to the great synaptotagmin protein family which contain 2 domains: cytoplasmic C terminus with two tandem C2 domains (C2A and C2B) and extracellular N-terminal transmembrane domain. Synaptotogmin family members have dissimilar biochemical properties and developmental profiles, and patterns of tissue distribution. Additionally, Synaptotogmins formulate homo- and heteromeric complexes with each other. Synaptotagmins operate as membrane traffickers in multicellular organisms.

    • Synonyms

      Synaptotagmin XIII, KIAA1427, synaptotagmin-13, sytXIII.

    • 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 MGSCRHMHPK KGLLPRDQDP DLEKAKPSLL GSAQQFNVKK STEPVQPRAL LKFPDIYGPR PAVTAPEVIN YADYSLRSTE EPTAPASPQP PNDSRLKRQV TEELFILPQN GVVEDVCVME TWNPEKAASW NQAPKLHYCL DYDCQKAELF VTRLEAVTSN HDGGCDCYVQ GSVANRTGSV EAQTALKKRQ LHTTWEEGLV LPLAEEELPT ATLTLTLRTC DRFSRHSVAG ELRLGLDGTS VPLGAAQWGE LKTSAKEPSA GAGEVLLSIS YLPAANRLLV VLIKAKNLHS NQSKELLGKD VSVKVTLKHQ ARKLKKKQTK RAKHKINPVW NEMIMFELPD DLLQASSVEL EVLGQDDSGQ SCALGHCSLG LHTSGSERSH WEEMLKNPRR QIAMWHQLHL

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    Syt13 Human
  • View Data Sheet

    Name :

    KRT20 Human, His

    Description:

    Cytokeratin 20 Human Recombinant, His Tag

    Keratin, type I cytoskeletal 20, CD20, CK-20, CK20, K20, KRT21, Keratin, Cytokeratin-20, Keratin-20, Protein IT, KRT20.

    Product # :

    PRO-1358

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    Description

    KRT20 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (1-424 a.a) and having a molecular mass of 50.9kDa. KRT20 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KRT20 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Recombinant Human Cytokeratin 20 His Tag (KRT20) belongs to the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins is comprised of acidic proteins that are organized in pairs of heterotypic keratin chains. KRT20 is a main cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa.

    • Synonyms

      Keratin, type I cytoskeletal 20, CD20, CK-20, CK20, K20, KRT21, Keratin, Cytokeratin-20, Keratin-20, Protein IT, KRT20.

    • 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 MGSMDFSRRS FHRSLSSSLQ APVVSTVGMQ RLGTTPSVYG GAGGRGIRIS NSRHTVNYGS DLTGGGDLFV GNEKMAMQNL NDRLASYLEK VRTLEQSNSK LEVQIKQWYE TNAPRAGRDY SAYYRQIEEL RSQIKDAQLQ NARCVLQIDN AKLAAEDFRL KYETERGIRL TVEADLQGLN KVFDDLTLHK TDLEIQIEEL NKDLALLKKE HQEEVDGLHK HLGNTVNVEV DAAPGLNLGV IMNEMRQKYE VMAQKNLQEA KEQFERQTAV LQQQVTVNTE ELKGTEVQLT ELRRTSQSLE IELQSHLSMK ESLEHTLEET KARYSSQLAN LQSLLSSLEA QLMQIRSNME RQNNEYHILL DIKTRLEQEI ATYRRLLEGE DVKTTEYQLS TLEERDIKKT RKIKTVVQEV VDGKVVSSEV KEVEENI.

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    Krt20 Human His
  • View Data Sheet

    Name :

    CYGB Human

    Description:

    Cytoglobin Human Recombinant

    HGB, STAP, Cytoglobin, CYGB.

    Product # :

    PRO-842

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    • More Info

    Description

    CYGB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-190 a.a.) and having a molecular mass of 23.5kDa. The CYGB is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CYGB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytoglobin is a globin protein found in the brain and is mainly utilized in marine mammals. CYGB acts a a protector under conditions of hypoxia. The suggested function of CYGB is the modulation of oxygen and nitric oxide metabolism or scavenging free radicals within a cell.

    • Synonyms

      HGB, STAP, Cytoglobin, CYGB.

    • 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 MEKVPGEMEI ERRERSEELS EAERKAVQAM WARLYASCED VGVAILVRFF VNFPSAKQYF SQFKHMEDPL EMERSPQLRK HACRVMGALN TVVENLHDPD KVSSVLALVG KAHALKHKVE PVYFKILSGV ILEVVAEEFA SDFPPETQRA WAKLRGLIYS HVTAAYKEVG WVQQVPNATT PPATLPSSGP.

    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.

    Cygb Human
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