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Search results

1000 results found for “HINT”

Name

Description

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  • View Data Sheet

    Name :

    MIP 3b Mouse

    Description:

    Macrophage Inflammatory Protein-3 Beta Mouse Recombinant (CCL19)

    Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433, Epstein-Barr virus-induced molecule 1 ligand chemokine, EBI1-ligand chemokine.

    Product # :

    CHM-341

    Price :

    Quantity :

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    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
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    Description

    Macrophage Inflammatory Protein-3 beta Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 9216 Dalton. The MIP-3b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its ability to chemoattract human PBL, is less than 100ng/ml. 

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 19 (CCL19) is a small cytokine belonging to the CC chemokine family that is also known as EBI1 ligand chemokine (ELC) and macrophage inflammatory protein-3-beta (MIP-3-beta). CCL19 is expressed abundantly in thymus and lymph nodes, with moderate levels in trachea and colon and low levels in stomach, small intestine, lung, kidney and spleen. The gene for CCL19 is located on human chromosome 9. This chemokine elicits its effects on its target cells by binding to the chemokine receptor chemokine receptor CCR7. It attracts certain cells of the immune system, including dendritic cells and antigen-engaged B cells.

    • Synonyms

      Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433, Epstein-Barr virus-induced molecule 1 ligand chemokine, EBI1-ligand chemokine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-3b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL19 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 Macrophage Inflammatory Protein-3b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GANDAEDCCL SVTQRPIPGN IVKAFRYLLN EDGCRVPAVV FTTLRGYQLC APPDQPWVDR IIRRLKKSSA KNKGNSTRRS PVLE.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.91 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 MIP-3b 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.

    Mip 3B Mouse
  • View Data Sheet

    Name :

    ADH5 Human

    Description:

    Alcohol Dehydrogenase 5 Human Recombinant

    Alcohol dehydrogenase 5 (class III) chi polypeptide, Alcohol dehydrogenase class chi chain, Glutathione-dependent formaldehyde dehydrogenase, S-(hydroxymethyl) glutathione dehydrogenase, FDH, ADHX, ADH-3, FALDH, GSH-FDH, GSNOR, EC 1.1.1.1, EC 1.1.1.284.

    Product # :

    ENZ-595

    Price :

    Quantity :

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    • More Info

    Description

    ADH5 Recombinant produced in E. coli is a single polypeptide chain containing 398 amino acids (1-374) and having a molecular mass of 42.3kDa.ADH5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ADH5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADH5 belongs to the alcohol dehydrogenase family which metabolizes a large selection of substrates, such as retinol, ethanol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH5 has practically no activity for ethanol oxidation, but displays high activity for oxidation of long-chain primary alcohols and for oxidation of S-hydroxymethyl-glutathione, a spontaneous adduct between glutathione and formaldehyde. ADH5 enzyme is a key factor of cellular metabolism for the removal of formaldehyde, a powerful aggravating and alerting mediator which causes pharyngitis, lacrymation, rhinitis and contact dermatitis.

    • Synonyms

      Alcohol dehydrogenase 5 (class III) chi polypeptide, Alcohol dehydrogenase class chi chain, Glutathione-dependent formaldehyde dehydrogenase, S-(hydroxymethyl) glutathione dehydrogenase, FDH, ADHX, ADH-3, FALDH, GSH-FDH, GSNOR, EC 1.1.1.1, EC 1.1.1.284.

    • 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 MGSHMANEVI KCKAAVAWEA GKPLSIEEIE VAPPKAHEVR IKIIATAVCH TDAYTLSGAD PEGCFPVILG HEGAGIVESV GEGVTKLKAG DTVIPLYIPQ CGECKFCLNP KTNLCQKIRV TQGKGLMPDG TSRFTCKGKT ILHYMGTSTF SEYTVVADIS VAKIDPLAPL DKVCLLGCGI STGYGAAVNT AKLEPGSVCA VFGLGGVGLA VIMGCKVAGA SRIIGVDINK DKFARAKEFG ATECINPQDF SKPIQEVLIE MTDGGVDYSF ECIGNVKVMR AALEACHKGW GVSVVVGVAA SGEEIATRPF QLVTGRTWKG TAFGGWKSVE SVPKLVSEYM SKKIKVDEFV THNLSFDEIN KAFELMHSGK SIRTVVKI

    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.

    Adh5 Human
  • View Data Sheet

    Name :

    CYTH2 Human

    Description:

    Cytohesin 2 Human Recombinant

    ARF Nucleotide-Binding Site Opener, Pleckstrin Homology Sec7 And Coiled-Coil Domains 2 (Cytohesin-2), PH SEC7 And Coiled-Coil Domain-Containing Protein 2, Cytohesin 2, Protein ARNO, ARF Exchange Factor, Sec7p-Like, PSCD2, PSCD2L, CTS18.1, Sec7p-L, SEC7L.

    Product # :

    PRO-1248

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • More Info

    Description

    CYTH2 Human Recombinant produced in E. coli is a single polypeptide chain containing 422 amino acids (1-399) and having a molecular mass of 48.9 kDa. CYTH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CYTH2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytohesin 2 (CYTH2) is an ARF-1 guanine nucleotide exchange factor (GEF). ARF (ADP ribosylation factor) proteins are a part of a group within the RAS superfamily and bindes GTP-b proteins central to the process of vesicle budding. CYTH2 promotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Furthermore, CYTH2 promotes the activation of ARF factors through replacement of GDP with GTP. The protein encoded by CYTH2 is a member of the PSCD family. Members of PSCD family appear to mediate the regulation of protein sorting and membrane trafficking. The cell membrane form, in association with ARL4 proteins, recruits ARF6 to the plasma membrane.

    • Synonyms

      ARF Nucleotide-Binding Site Opener, Pleckstrin Homology Sec7 And Coiled-Coil Domains 2 (Cytohesin-2), PH SEC7 And Coiled-Coil Domain-Containing Protein 2, Cytohesin 2, Protein ARNO, ARF Exchange Factor, Sec7p-Like, PSCD2, PSCD2L, CTS18.1, Sec7p-L, SEC7L.

    • 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 MGSMEDGVYE PPDLTPEERM ELENIRRRKQ ELLVEIQRLR EELSEAMSEV EGLEANEGSK TLQRNRKMAM GRKKFNMDPK KGIQFLVENE LLQNTPEEIA RFLYKGEGLN KTAIGDYLGE REELNLAVLH AFVDLHEFTD LNLVQALRQF LWSFRLPGEA QKIDRMMEAF AQRYCLCNPG VFQSTDTCYV LSFAVIMLNT SLHNPNVRDK PGLERFVAMN RGINEGGDLP EELLRNLYDS IRNEPFKIPE DDGNDLTHTF FNPDREGWLL KLGGRVKTWK RRWFILTDNC LYYFEYTTDK EPRGIIPLEN LSIREVDDPR KPNCFELYIP NNKGQLIKAC KTEADGRVVE GNHMVYRISA PTQEEKDEWI KSIQAAVSVD PFYEMLAARK KRISVKKKQE QP.

    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.

    Cyth2 Human
  • View Data Sheet

    Name :

    AKR1D1 Human, His

    Description:

    Aldo-Keto Reductase Family 1 Member D1 Human Recombinant, His Tag

    3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-keto reductase family 1 member D1, Delta(4)-3-ketosteroid 5-beta-reductase, Delta(4)-3-oxosteroid 5-beta-reductase, KR1D1, SRD5B1, CBAS2, 3o5bred.

    Product # :

    ENZ-098

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    AKR1D1 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 346 amino acids (1-326 a.a.) and having a molecular mass of 39.5kDa. The AKR1D1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR1D1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 100mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aldo-keto reductase family 1 member D1 (AKR1D1) belongs to the AKR superfamily. The AKR family proteins are soluble NADPH oxidoreductases, which have vital roles in the metabolism of drugs, carcinogens and reactive aldehydes. AKR1D1 is also responsible for the catalysis of the 5-beta-reduction of bile acid intermediates and steroid hormones that carry a delta (4)-3-1 structure. AKR1D1 is highly expressed in the liver, colon and testis. Deficiency of the AKR1D1 enzyme may contribute to hepatic dysfunction.

    • Synonyms

      3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-keto reductase family 1 member D1, Delta(4)-3-ketosteroid 5-beta-reductase, Delta(4)-3-oxosteroid 5-beta-reductase, KR1D1, SRD5B1, CBAS2, 3o5bred.

    • 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 MDLSAASHRI PLSDGNSIPI IGLGTYSEPK STPKGACATS VKVAIDTGYR HIDGAYIYQN EHEVGEAIRE KIAEGKVRRE DIFYCGKLWA TNHVPEMVRP TLERTLRVLQ LDYVDLYIIE VPMAFKPGDE IYPRDENGKW LYHKSNLCAT WEAMEACKDA GLVKSLGVSN FNRRQLELIL NKPGLKHKPV SNQVECHPYF TQPKLLKFCQ QHDIVITAYS PLGTSRNPIW VNVSSPPLLK DALLNSLGKR YNKTAAQIVL RFNIQRGVVV IPKSFNLERI KENFQIFDFS LTEEEMKDIE ALNKNVRFVE LLMWRDHPEY PFHDEY.

    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.

    Akr1D1 Human
  • View Data Sheet

    Name :

    ALDH2 Mouse

    Description:

    Aldehyde Dehydrogenase 2 Mouse Recombinant

    Aldehyde dehydrogenase, mitochondrial, AHD-M1, ALDH class 2, ALDH-E2, ALDHI.

    Product # :

    ENZ-879

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    Description

    ALDH2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (20-519 a.a) and having a molecular mass of 56.8kDa. ALDH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ALDH2 protein e solution (0.5mg/ml) containing Phosphate buffered salin(pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial isozyme. ALDH2 has a low Km for acetaldehydes, and is localized in mitochondrial matrix.

    • Synonyms

      Aldehyde dehydrogenase, mitochondrial, AHD-M1, ALDH class 2, ALDH-E2, ALDHI.

    • 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 MGSSAAATSA VPAPNHQPEV FCNQIFINNE WHDAVSRKTF PTVNPSTGEV ICQVAEGNKE DVDKAVKAAR AAFQLGSPWR RMDASDRGRL LYRLADLIER DRTYLAALET LDNGKPYVIS YLVDLDMVLK CLRYYAGWAD KYHGKTIPID GDFFSYTRHE PVGVCGQIIP WNFPLLMQAW KLGPALATGN VVVMKVAEQT PLTALYVANL IKEAGFPPGV VNIVPGFGPT AGAAIASHEG VDKVAFTGST EVGHLIQVAA GSSNLKRVTL ELGGKSPNII MSDADMDWAV EQAHFALFFN QGQCCCAGSR TFVQENVYDE FVERSVARAK SRVVGNPFDS RTEQGPQVDE TQFKKILGYI KSGQQEGAKL LCGGGAAADR GYFIQPTVFG DVKDGMTIAK EEIFGPVMQI LKFKTIEEVV GRANDSKYGL AAAVFTKDLD KANYLSQALQ AGTVWINCYD VFGAQSPFGG YKMSGSGREL GEYGLQAYTE VKTVTVKVPQ KNS.

    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.

    Aldh2 Mouse
  • View Data Sheet

    Name :

    HMBS Human

    Description:

    Hydroxymethylbilane Synthase Human Recombinant

    Porphobilinogen deaminase, PBG-D, Hydroxymethylbilane synthase, HMBS, Pre-uroporphyrinogen synthase, HMBS, PBGD, UPS, PORC.

    Product # :

    ENZ-581

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    Description

    HMBS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-361) and having a molecular mass of 41.9kDa.HMBS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Porphobilinogen deaminase (HMBS) belongs to the hydroxymethylbilane synthase superfamily. HMBS is a cytoplasmic enzyme found in the heme synthesis pathway. HMBS is the 3rd enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of 4 porphobilinogen molecules into the linear hydroxymethylbilane. HMBS gene mutations cause errors in pyrrole metabolism which in turn lead to the autosomal dominant disease acute intermittent porphyria.

    • Synonyms

      Porphobilinogen deaminase, PBG-D, Hydroxymethylbilane synthase, HMBS, Pre-uroporphyrinogen synthase, HMBS, PBGD, UPS, PORC.

    • 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 MGSHMSGNGN AAATAEENSP KMRVIRVGTR KSQLARIQTD SVVATLKASY PGLQFEIIAM STTGDKILDT ALSKIGEKSL FTKELEHALE KNEVDLVVHS LKDLPTVLPP GFTIGAICKR ENPHDAVVFH PKFVGKTLET LPEKSVVGTS SLRRAAQLQR
      KFPHLEFRSI RGNLNTRLRK LDEQQEFSAI ILATAGLQRM GWHNRVGQIL HPEECMYAVG QGALGVEVRA KDQDILDLVG VLHDPETLLR CIAERAFLRH LEGGCSVPVA VHTAMKDGQL YLTGGVWSLD GSDSIQETMQ ATIHVPAQHE DGPEDDPQLV GITARNIPRG PQLAAQNLGI
      SLANLLLSKG AKNILDVARQ LNDAH.

    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.

    Hmbs Human
  • View Data Sheet

    Name :

    ASPH Human

    Description:

    Aspartate Beta-Hydroxylase Human Recombinant

    AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH.

    Product # :

    ENZ-488

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    Description

    ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (75-270 a.a.) and having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters and goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Further isoforms diverge mainly in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum.

    • Synonyms

      AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH.

    • 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 MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT.

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    Asph Human
  • View Data Sheet

    Name :

    SNAPIN Human

    Description:

    SNAP Associated Protein Human Recombinant

    SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.

    Product # :

    PRO-663

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    Description

    SNAPIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-136) and having a molecular mass of 17 kDa. SNAPIN is fused to 20 amino acid His Tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH-8, 5mM DTT, 2mM EDTA, 0.2M NaCl, and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNAPIN is involved in the neurotransmitter release process through its modulation of the sequential interactions between the SNAREs and synaptotagmin. SNAPIN is part of the SNARE complex of proteins that is needed for synaptic vesicle docking and fusion. SNAPAP is enriched in neurons and exclusively located on synaptic vesicle membrane protein. SNAPIN is also an important factor of the BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.

    • Synonyms

      SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.

    • 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 MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN LATELCRINEDQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK.

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    Snapin Human
  • View Data Sheet

    Name :

    STMN4 Human

    Description:

    Stathmin Like-4 Human Recombinant

    RB3, Stathmin-4, Stathmin-like protein B3, TMN4.

    Product # :

    PRO-1497

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    Description

    STMN4 Human Recombinant produced in E. coli is a single polypeptide chain containing 239 amino acids (1-216) and having a molecular mass of 27.8kDa. STMN4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The STMN4 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Stathmin Like-4, also known as STMN4, belongs to the stathmin family and shows signs of smicrotubule-destabilizing activity. A significant paralog of STMN4 is STMN3.

    • Synonyms

      RB3, Stathmin-4, Stathmin-like protein B3, TMN4.

    • 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 MGSMTLAAYK EKMKELPLVS LFCSCFLADP LNKSSYKYEG WCGRQCRRKD ESQRKDSADW RERRAQADTV DLNWCVISDM EVIELNKCTS GQSFEVILKP PSFDGVPEFN ASLPRRRDPS LEEIQKKLEA AEERRKYQEA ELLKHLAEKR EHEREVIQKA IEENNNFIKM AKEKLAQKME SNKENREAHL AAMLERLQEK DKHAEEVRKN KELKEEASR.

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    Stmn4 Human
  • View Data Sheet

    Name :

    Streptavidin (37-159), His

    Description:

    Streptavidin (37-159 a.a) Recombinant, His Tag

    Product # :

    PRO-1495

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    Description

    Streptavidin Recombinant produced in E. coli is a single polypeptide chain containing 148 amino acids (37-159) and having a molecular mass of 15.6kDa. Streptavidin is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

    • 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 MGSHMAEAGI TGTWYNQLGS TFIVTAGADG ALTGTYESAV GNAESRYVLT GRYDSAPATD GSGTALGWTV AWKNNYRNAH SATTWSGQYV GGAEARINTQ WLLTSGTTEA NAWKSTLVGH DTFTKVKP.

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    Streptavidin 37 159 His
  • View Data Sheet

    Name :

    STX3 Human

    Description:

    Syntaxin-3 Human Recombinant

    Syntaxin-3, STX3, STX3A.

    Product # :

    PRO-1082

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    Description

    STX3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids (1-263 a.a) and having a molecular mass of 33.2kDa.STX3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    STX3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Syntaxin 3 (STX3) is a member of the syntaxin family. The syntaxin family members are cellular receptors for transport vesicles which participate in exocytosis in neutrophils. STX3 has a significant role in the growth of neurites and functions as a direct target for omega-6 arachidonic acid. STX3 is steered to the apical membrane of epithelial cells where it forms clusters and is vital in establishing and maintaining polarity required for protein trafficking involving vesicle fusion and exocytosis.

    • Synonyms

      Syntaxin-3, STX3, STX3A.

    • 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 MGSHMMKDRL EQLKAKQLTQ DDDTDAVEIA IDNTAFMDEF FSEIEETRLN IDKISEHVEE AKKLYSIILS APIPEPKTKD DLEQLTTEIK KRANNVRNKL KSMEKHIEED EVRSSADLRI RKSQHSVLSR KFVEVMTKYN EAQVDFRERS KGRIQRQLEI TGKKTTDEEL EEMLESGNPA IFTSGIIDSQ ISKQALSEIE GRHKDIVRLE SSIKELHDMF MDIAMLVENQ GEMLDNIELN VMHTVDHVEK ARDETKKAVK YQSQARKK.

    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.

    Stx3 Human
  • View Data Sheet

    Name :

    FABP2 Human, His

    Description:

    Fatty Acid Binding Protein 2 Human Recombinant, His Tag

    Fatty acid-binding protein 2, IFABP, I-FABP, FABPI, FABP-2, Fatty acid-binding protein intestinal, FABP2, MGC133132.

    Product # :

    PRO-669

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    Description

    FABP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 17.3kDa. FABP2 is fused to a 20 aa His tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    FABP2 His-Tag is supplied in 20mM Tris-HCl pH 8 and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      FABP multigene family has almost 20 known members. FABPs are divided into 3 different types: hepatic, intestinal and cardiac which form 14-15 kDa proteins that take part in the uptake, intracellular metabolism and/or transport of long-chain fatty acids. FABPs are involved in the modulation of cell growth and proliferation. Intestinal FABP (FABP2) gene has a polymorphism at codon 54 that identified an alanine-encoding allele and a threonine-encoding allele. Thr-54 protein is associated with increased fat oxidation and insulin resistance. High serum levels of FABP2 is ulcerative colitis indicates ileitis. FABP2 is has part in triglyceride-rich lipoprotein synthesis. FABP2 binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long- chain fatty acids. FABP2 helps maintain energy homeostasis by functioning as a lipid sensor.

    • Synonyms

      Fatty acid-binding protein 2, IFABP, I-FABP, FABPI, FABP-2, Fatty acid-binding protein intestinal, FABP2, MGC133132.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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 MAFDSTWKVD RSENYDKFME KMGVNIVKRK LAAHDNLKLT ITQEGNKFTV KESSAFRNIE VVFELGVTFN YNLADGTELR GTWSLEGNKL IGKFKRTDNG NELNTVREII GDELVQTYVY EGVEAKRIFK KD

    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.

    Fabp2 Human
  • View Data Sheet

    Name :

    CXCL8 Human, His

    Description:

    Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8), His Tag

    IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    Product # :

    CHM-345

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    Description

    Interleukin-8 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 77 amino acids fragment (23-99) and having a total molecular mass of 13.7kDa with an amino-terminal hexahistidine tag. The IL-8 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL8 His is supplied in 10mM Tris-HCl pH 8, 250mM NaCl and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Background

      What is the molecular weight/Mw of CXCL8 HUMAN, HIS Protein?
      CXCL8 HUMAN, HIS Protein has a total Mw of 13.7kDa.

      What is the source or expression system of CXCL8 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 HUMAN, HIS Protein?
      CXCL8 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 HUMAN, HIS Protein?
      The biological functionality of CXCL8 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL8 HUMAN, HIS Protein?
      CXCL8 HUMAN, HIS Protein is composed from 77 amino acids.

      What applications can CXCL8 HUMAN, HIS Protein be used in?
      CXCL8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 HUMAN, HIS Protein?
      The endotoxin level is minimal, CXCL8 HUMAN, HIS Protein was purified using conventional chromatography techniques.



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    Il 8 77 Human His
  • View Data Sheet

    Name :

    TFF1 Human, His

    Description:

    Trefoil Factor-1 Human Recombinant, His Tag

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

    Product # :

    CYT-610

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    Description

    TFF-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids (25-84) which includes a 10 amino acid His Tag and having a total molecular mass of 7.9 kDa. TFF-1 Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFF1 His Tag protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing 20mM Tris pH-7.5 and 20mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF1 His Tag although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF1 His Tag 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 add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS EAQTETCTVA PRERQNCGFP GVTPSQCANK GCCFDDTVRG VPWCFYPNTI DVPPEEECEF.

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    Tff1 Human His
  • View Data Sheet

    Name :

    CCNI Human

    Description:

    Cyclin-I Human Recombinant

    Cyclin-I, CCNI, CYC1, CYI.

    Product # :

    PKA-318

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    Description

    CCNI Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 400 amino acids (1-377 a.a) and having a molecular mass of 44.9kDa.CCNI is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CCNI protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCN1 is a part of the extremely conserved cyclin family, whose members are characterized by a remarkable periodicity in protein abundance through the cell cycle. Cyclins which function as regulators of CDK kinases, shows the highest similarity with cyclin G. Different cyclins display diverse expression and degradation patterns which contribute to the chronological coordination of every mitotic event. The transcript of CCN1was found to be expressed continually during cell cycle progression.

    • Synonyms

      Cyclin-I, CCNI, CYC1, CYI.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMKFPGPL ENQRLSFLLE KAITREAQMW KVNVRKMPSN QNVSPSQRDE VIQWLAKLKY QFNLYPETFA LASSLLDRFL ATVKAHPKYL SCIAISCFFL AAKTVEEDER IPVLKVLARD SFCGCSSSEI LRMERIILDK LNWDLHTATP LDFLHIFHAI AVSTRPQLLF SLPKLSPSQH LAVLTKQLLH CMACNQLLQF RGSMLALAMV SLEMEKLIPD WLSLTIELLQ KAQMDSSQLI HCRELVAHHL STLQSSLPLN SVYVYRPLKH TLVTCDKGVF RLHPSSVPGP DFSKDNSKPE VPVRGTAAFY HHLPAASGCK QTSTKRKVEE MEVDDFYDGI KRLYNEDNVS ENVGSVCGTD LSRQEGHASP CPPLQPVSVM.

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    Ccni Human
  • View Data Sheet

    Name :

    ITGB1 Human

    Description:

    Integrin Beta 1 Human Recombinant

    Integrin beta-1, Fibronectin receptor subunit beta, Glycoprotein IIa, GPIIA, VLA-4 subunit beta, CD29, ITGB1, FNRB, MDF2, MSK12, Integrin beta 1, CD29, VLAB.

    Product # :

    PRO-1817

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    Description

    ITGB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 462 amino acids (21-461) and having a molecular mass of 51.2 kDa.ITGB1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ITGB1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Integrins are heterodimeric proteins consist of alpha and beta subunits. There are more than 18 alpha and 8 beta subunits discovered in mammals. Integrin family members are membrane receptors that participates in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells. ITGB1 encodes a beta subunit.

    • Synonyms

      Integrin beta-1, Fibronectin receptor subunit beta, Glycoprotein IIa, GPIIA, VLA-4 subunit beta, CD29, ITGB1, FNRB, MDF2, MSK12, Integrin beta 1, CD29, VLAB.

    • 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 MQTDENRCLK ANAKSCGECI QAGPNCGWCT NSTFLQEGMP TSARCDDLEA LKKKGCPPDD IENPRGSKDI KKNKNVTNRS KGTAEKLKPE DITQIQPQQL VLRLRSGEPQ TFTLKFKRAE DYPIDLYYLM DLSYSMKDDL ENVKSLGTDL MNEMRRITSD
      FRIGFGSFVE KTVMPYISTT PAKLRNPCTS EQNCTSPFSY KNVLSLTNKG EVFNELVGKQ RISGNLDSPE GGFDAIMQVA VCGSLIGWRN VTRLLVFSTD AGFHFAGDGK LGGIVLPNDG QCHLENNMYT MSHYYDYPSI AHLVQKLSEN NIQTIFAVTE EFQPVYKELK NLIPKSAVGT LSANSSNVIQ LIIDAYNSLS SEVILENGKL SEGVTISYKS YCKNGVNGTG ENGRKCSNIS IGDEVQFEIS ITSNKCPKKD SDSFKIRPLG FTEEVEVILQ YI.

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    Itgb1 Human
  • View Data Sheet

    Name :

    GAMT Human

    Description:

    Guanidinoacetate N-Methyltransferase Human Recombinant

    PIG2, TP53I2, GAMT, Guanidinoacetate N-methyltransferase.

    Product # :

    ENZ-460

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    Description

    Recombinant Human GAMT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 256 amino acids (1-236 a.a) and having a molecular mass of 28.4 kDa. GAMT is fused to a 20 amino acids His-Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The GAMT protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GAMT is a methyltransferase that transfers guanidoacetate to creatine, using S-adenosylmethionine as the methyl donor. Defects GAMT gene result in neurologic syndromes and muscular hypotonia, probably due to creatine deficiency and accumulation of guanidinoacetate in the brain of affected individuals. GAMT take parts in the two-step synthesis of creatine from the protein building blocks glycine, arginine, and methionine. GAMT takes part in supplying the energy for muscle contraction, and is in addition a significant player in nervous system functioning. GAMT is active in the liver, pancreas, and kidne.

    • Synonyms

      PIG2, TP53I2, GAMT, Guanidinoacetate N-methyltransferase.

    • 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 MSAPSATPIF APGENCSPAW GAAPAAYDAA DTHLRILGKP VMERWETPYM HALAAAASSK GGRVLEVGFG MAIAASKVQE APIDEHWIIE CNDGVFQRLR DWAPRQTHKV IPLKGLWEDV APTLPDGHFD GILYDTYPLS EETWHTHQFN FIKNHAFRLL KPGGVLTYCN LTSWGELMKS KYSDITIMFE ETQVPALLEA GFRRENIRTE VMALVPPADC RYYAFPQMIT PLVTKG.

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    Gamt Human
  • View Data Sheet

    Name :

    KRT17 Human

    Description:

    Cytokeratin 17 Human Recombinant

    Keratin 17, PCHC1, 39.1, CK-17, K17, PC2, PC, cytokeratin-17, Keratin 17 Epitope S1, Keratin 17 Epitope S2, Keratin 17 Epitope S4, Keratin, Type I Cytoskeletal 1, keratin-17, Cytokeratin-17, Keratin-17.

    Product # :

    PRO-1883

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    Description

    KRT17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 455 amino acids (1-432 a.a) and having a molecular mass of 50.5kDa.KRT17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KRT17 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokeratin 17 also known as KRT17 is a type I cytokeratin. KRT17 is found in nail beds, hair follicles, sebaceous glands, and other epidermal appendages. Mutations in KRT17 lead to Jackson-Lawler type pachyonychia congenita and steatocystoma multiplex. KRT17 takes part in the formation and maintenance of a variety of skin appendages, particularly in determining shape and orientation of hair. KRT17 also modulates the function of TNF-alpha in the precise context of hair cycling. Moreover, KRT17 regulates protein synthesis and epithelial cell growth all through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway.

    • Synonyms

      Keratin 17, PCHC1, 39.1, CK-17, K17, PC2, PC, cytokeratin-17, Keratin 17 Epitope S1, Keratin 17 Epitope S2, Keratin 17 Epitope S4, Keratin, Type I Cytoskeletal 1, keratin-17, Cytokeratin-17, Keratin-17.

    • 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 MGSMTTSIRQ FTSSSSIKGS SGLGGGSSRT SCRLSGGLGA GSCRLGSAGG LGSTLGGSSY SSCYSFGSGG GYGSSFGGVD GLLAGGEKAT MQNLNDRLAS YLDKVRALEE ANTELEVKIR DWYQRQAPGP ARDYSQYYRT IEELQNKILT ATVDNANILL QIDNARLAAD DFRTKFETEQ ALRLSVEADI NGLRRVLDEL TLARADLEMQ IENLKEELAY LKKNHEEEMN ALRGQVGGEI NVEMDAAPGV DLSRILNEMR DQYEKMAEKN RKDAEDWFFS KTEELNREVA TNSELVQSGK SEISELRRTM QALEIELQSQ LSMKASLEGN LAETENRYCV QLSQIQGLIG SVEEQLAQLR CEMEQQNQEY KILLDVKTRL EQEIATYRRL LEGEDAHLTQ YKKEPVTTRQ VRTIVEEVQD GKVISSREQV HQTTR

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    Krt17 Human
  • View Data Sheet

    Name :

    LACTB E.coli, His

    Description:

    Beta Lactamase E.coli Recombinant, His Tag

    Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.

    Product # :

    ENZ-088

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    Description

    Beta Lactamase is an E.coli Recombinant protein produced in E.Coli containing 379 amino acids (20-377) and having a molecular mass of 41.8kDa. Beta Lactamase is expressed with a 21 N-terminal His tag.The LACTB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LACTB enzyme (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties.

    • Synonyms

      Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.

    • 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 MAPQQINDIV HRTITPLIEQ QKIPGMAVAV IYQGKPYYFT WGYADIAKKQ PVTQQTLFEL GSVSKTFTGV LGGDAIARGE IKLSDPTTKY WPELTAKQWN GITLLHLATY TAGGLPLQVP DEVKSSSDLL RFYQNWQPAW APGTQRLYAN SSIGLFGALA VKPSGLSFEQ AMQTRVFQPL KLNHTWINVP PAEEKNYAWG YREGKAVHVS PGALDAEAYG VKSTIEDMAR WVQSNLKPLD INEKTLQQGI QLAQSRYWQT GDMYQGLGWE MLDWPVNPDS IINGSDNKIA LAARPVKAIT PPTPAVRASW VHKTGATGGF GSYVAFIPEK ELGIVMLANK NYPNPARVDA AWQILNALQ.

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    Lactb Ecoli His
  • View Data Sheet

    Name :

    LDHA Human

    Description:

    Lactate Dehydrogenase A Human Recombinant

    LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.

    Product # :

    ENZ-491

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    Description

    LDHA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-332 a.a.) and having a molecular mass of 38.8 kDa. The LDHA is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The LDHA protein solution (0.5mg/ml) contains 20mM Tris-HCl pH-8.0, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 20 units/mg. in which one unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37°C.

    More Info

    • Introduction

      LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA is localized primarily in muscle tissue and is part of the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria. LDH1 is decreased in essential thrombocythemia. LDHA is induced through a non-genomic pathway of estrogen action. Reduction in LDH-A activity results in stimulation of mitochondrial respiration and decrease of mitochondrial membrane potential.

    • Synonyms

      LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.

    • 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 MATLKDQLIY NLLKEEQTPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG EMMDLQHGSL FLRTPKIVSG KDYNVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI IPNVVKYSPN CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV HPLSCHGWVL GEHGDSSVPV WSGMNVAGVS LKTLHPDLGT DKDKEQWKEV HKQVVESAYE VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPVSTMIKGL YGIKDDVFLS VPCILGQNGI SDLVKVTLTS EEEARLKKSA DTLWGIQKEL QF.

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    Ldha Human
  • View Data Sheet

    Name :

    PRMT3 Human

    Description:

    Protein Arginine Methyltransferase 3 Human Recombinant

    Protein Arginine Methyltransferase 3, Heterogeneous Nuclear Ribonucleoprotein, Methyltransferase-Like Protein 3, HRMT1L3, HMT1 HnRNP Methyltransferase-Like 3 (S. Cerevisiae), Protein Arginine N-Methyltransferase 3, HMT1 HnRNP Methyltransferase-Like 3, EC 2.1.1.- ,EC 2.1.1, PRMT3.

    Product # :

    ENZ-848

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    Description

    PRMT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 554 amino acids (1-531 a.a) and having a molecular mass of 62.3kDa.PRMT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PRMT3 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 20% glycerol, 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PRMT3, also known as protein arginine N-methyltransferase 3, is a member of the protein arginine methyltransferase family. PRMT3 catalyzes the methylation of guanidino nitrogens of arginyl residues of proteins. PRMT3 operates on 40S ribosomal protein S2 ,rpS2, which is the major in-vivo substrate, additionally PRMT3 is also involved in the proper maturation of the 80S ribosome.

    • Synonyms

      Protein Arginine Methyltransferase 3, Heterogeneous Nuclear Ribonucleoprotein, Methyltransferase-Like Protein 3, HRMT1L3, HMT1 HnRNP Methyltransferase-Like 3 (S. Cerevisiae), Protein Arginine N-Methyltransferase 3, HMT1 HnRNP Methyltransferase-Like 3, EC 2.1.1.- ,EC 2.1.1, PRMT3.

    • 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 MGSMCSLASG ATGGRGAVEN EEDLPELSDS GDEAAWEDED DADLPHGKQQ TPCLFCNRLF TSAEETFSHC KSEHQFNIDS MVHKHGLEFY GYIKLINFIR LKNPTVEYMN SIYNPVPWEK EEYLKPVLED DLLLQFDVED LYEPVSVPFS YPNGLSENTS VVEKLKHMEA RALSAEAALA RAREDLQKMK QFAQDFVMHT DVRTCSSSTS VIADLQEDED GVYFSSYGHY GIHEEMLKDK IRTESYRDFI YQNPHIFKDK VVLDVGCGTG ILSMFAAKAG AKKVLGVDQS EILYQAMDII RLNKLEDTIT LIKGKIEEVH LPVEKVDVII SEWMGYFLLF ESMLDSVLYA KNKYLAKGGS VYPDICTISL VAVSDVNKHA DRIAFWDDVY GFKMSCMKKA VIPEAVVEVL DPKTLISEPC GIKHIDCHTT SISDLEFSSD FTLKITRTSM CTAIAGYFDI YFEKNCHNRV VFSTGPQSTK THWKQTVFLL EKPFSVKAGE ALKGKVTVHK NKKDPRSLTV TLTLNNSTQT YGLQ

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    Prmt3 Human
  • View Data Sheet

    Name :

    GNMT Human

    Description:

    Glycine N-methyltransferase Human Recombinant

    Glycine N-methyltransferase, GNMT.

    Product # :

    ENZ-386

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    Description

    GNMT Human Recombinant fused with 20 amino acid His-Tag tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing a total of 315 amino acids (1-295 a.a.) and having a molecular mass of 34.9 kDa.The GNMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GNMT solution contains 20mM Tris pH 8.0 & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.

    • Synonyms

      Glycine N-methyltransferase, GNMT.

    • 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 MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT LDKDVPQSAE GGFDAVICLG NSFAHLPDCK GDQSEHRLAL KNIASMVRAG GLLVIDHRNY DHILSTGCAP PGKNIYYKSD LTKDVTTSVL IVNNKAHMVT LDYTVQVPGA GQDGSPGLSK FRLSYYPHCL ASFTELLQAA FGGKCQHSVL GDFKPYKPGQ TYIPCYFIHV LKRTD.

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    Gnmt Human
  • View Data Sheet

    Name :

    CXCL3 Mouse, His

    Description:

    GRO-Gamma Mouse Recombinant (CXCL3), His Tag

    C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.

    Product # :

    CHM-283

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    Description

    GRO-g Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (28-100 a.a.) and having a molecular mass of 10.6kDa.CXCL3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GRO-gamma protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.15M NaCl and 5mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.

    • Synonyms

      C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.

    • 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 MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.

    • Background

      What is the molecular weight/Mw of CXCL3 MOUSE, HIS Protein?
      CXCL3 MOUSE, HIS Protein has a total Mw of 10.6kDa.

      What is the source or expression system of CXCL3 MOUSE, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL3 MOUSE, HIS Protein?
      CXCL3 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL3 MOUSE, HIS Protein?
      The biological functionality of CXCL3 MOUSE, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL3 MOUSE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.

      What applications can CXCL3 MOUSE, HIS Protein be used in?
      CXCL3 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL3 MOUSE, HIS Protein?
      The endotoxin level is minimal, CXCL3 MOUSE, 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.

    Gro G Mouse His
  • View Data Sheet

    Name :

    CLCF1 Human, His

    Description:

    Neurotrophin-1 Human Recombinant, His Tag

    Cardiotrophin-like cytokine factor 1, B-cell-stimulating factor 3, BSF-3, Novel neurotrophin-1, NNT-1, CLCF1, BSF3, CLC, NNT1, NR6, CISS2.

    Product # :

    CYT-071

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • sds-page

    Description

    CLCF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (28-225 a.a) and having a molecular mass of 24.6kDa.CLCF1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CLCF1 protein solution (1mg/ml) containing 20mM sodium citrate (pH 3.5), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    CLCF-sds-page - Product image 1

    More Info

    • Introduction

      Cardiotrophin-like cytokine factor 1 (CLCF1) is a member of the interleukin 6 family of cytokines, which are involved in cell signaling via phosphorylation of gp130. CLCF1 has a sequence of 225 amino acids with a 27 aa signal peptide, having a molecular mass of 22kDa in the mature form, and the maximum homology to cardiotrophin-1 and ciliary neurotrophic factor. CLCF1 is actively secreted from cells by forming a complex with soluble type I CRLF1 or soluble CNTFR. Defects in the CLCF1 gene cause cold-induced sweating syndrome 2 (CISS2). The CISS2 syndrome is typified by profuse sweating after exposure to cold as well as congenital physical abnormalities of the head and spine.

    • Synonyms

      Cardiotrophin-like cytokine factor 1, B-cell-stimulating factor 3, BSF-3, Novel neurotrophin-1, NNT-1, CLCF1, BSF3, CLC, NNT1, NR6, CISS2.

    • 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 MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

    • Background

      Cardiotrophin-Like Cytokine Factor 1 Human Recombinant: A Significant Player in Neuronal Development and Immune Regulation

      Cardiotrophin-like cytokine factor 1 (CLCF1) has emerged as a crucial player in neuronal development and immune regulation. As a heterodimeric neurotropic cytokine, CLCF1 in complex with cytokine-like factor-1 (CLF-1) has demonstrated vital roles in neuronal development. Studies show that mice lacking this heterodimer exhibit reduced motor neurons and die shortly after birth due to suckling defects. In humans, mutations in the genes encoding for CLCF1 and CLF-1 manifest as Sohar-Crisponi or cold-induced sweating syndrome, with individuals at high risk of early death​1​.

      CLCF1 also exhibits a significant role in the regulation of hematopoiesis, particularly skewing towards myeloid cell differentiation. It has been demonstrated that in mice, CLCF1 promotes B-cell expansion, enhances humoral responses, and triggers autoimmunity. Further, CLCF1 administration resulted in an increase in circulating myeloid cells, along with augmented hematopoietic progenitor cells in the bone marrow. These findings underscore CLCF1's crucial role in modulating the immune system, particularly in the context of bonemarrow transplants and recovery following sub-lethal irradiation​2​.

      Interestingly, CLCF1 is a member of the IL-6 family of cytokines, known for their significant roles in immune regulation and stem cell biology. Like other family members, CLCF1 is secreted as a composite cytokine with CRLF1 and signals through the heterodimerization of the signaling chains LIFRβ and gp130. This suggests overlapping functions with leukemia inhibitor factor (LIF), another IL-6 family member. Expression of CLCF1 is documented in lymph nodes, spleen, and circulating lymphocytes, further establishing its role in immune modulation. However, the comprehensive implications of CLCF1 in immune regulation and hematopoiesis remain an active area of investigation​3​.

      In summary, Cardiotrophin-like cytokine factor 1 human recombinant represents a promising area of research with potential therapeutic implications in neurodevelopmental disorders and immune regulation.

      What is the molecular weight/Mw of CLCF Protein?
      CLCF Protein has a total Mw of 24.6kDa.

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

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

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

      What is the amino acid sequence of CLCF Protein?
      MGSSHHHHHH SSGLVPRGSH MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

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

      What is the endotoxin level for CLCF Protein?
      The endotoxin level is minimal, CLCF Protein was purified using conventional chromatography techniqu

    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.

    Clcf1 Human
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