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Search results

1000 results found for “Calpain”

Name

Description

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  • View Data Sheet

    Name :

    NDP Human

    Description:

    Norrie Disease Human Recombinant

    800x600 Norrin, EVR2, FEVR, ND, Norrie disease protein, X-linked exudative vitreoretinopathy 2 protein, NDP, Norrie Disease. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

    Product # :

    PRO-1674

    Price :

    Quantity :

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    Description

    NDP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (25-133) and having a molecular mass of 14.8 kDa.NDP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Norrie Disease (NDP) is a secreted regulatory protein which activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. NDP takes part in retinal vascularization by acting as a ligand for FZD4 which signals through stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. NDP is involved in a pathway that regulates neural cell differentiation and proliferation and also in neuroectodermal cell-cell interaction.

    • Synonyms

      Norrin, EVR2, FEVR, ND, Norrie disease protein, X-linked exudative vitreoretinopathy 2 protein, NDP, Norrie Disease.

    • 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 MGSKTDSSFI MDSDPRRCMR HHYVDSISHP LYKCSSKMVL LARCEGHCSQ ASRSEPLVSF STVLKQPFRS SCHCCRPQTS KLKALRLRCS GGMRLTATYR YILSCHCEEC NS.

    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.

    Ndp Human
  • View Data Sheet

    Name :

    NRP1 Human

    Description:

    Neuropilin 1 Human Recombinant

    Neuropilin-1 isoform a, NRP1, BDCA4, CD304, NP1, NRP, VEGF165R, Vascular endothelial cell growth factor 165 receptor.

    Product # :

    CYT-1059

    Price :

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    Description

    NRP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 843 amino acids (22-856a.a.) and having a molecular mass of 94.8kDa. (Molecular size on SDS-PAGE will appear at approximately 100-150kDa).NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    NRP1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NRP1 is a coreceptor bound on membranes to tyrosine kinase receptors for semaphorin family proteins and endothelial growth factors, it is a type one transmembrane protein. Neuropilin-1 takes part in cell survival, angiogenesis, invasion, migration, and axon guidance. the protein is a potential target for cancer therapies as it interacts with VEGF (co-receptor).

    • Synonyms

      Neuropilin-1 isoform a, NRP1, BDCA4, CD304, NP1, NRP, VEGF165R, Vascular endothelial cell growth factor 165 receptor.

    • 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

      FRNDKCGDTI KIESPGYLTS PGYPHSYHPS EKCEWLIQAP DPYQRIMINF NPHFDLEDRD CKYDYVEVFD GENENGHFRG KFCGKIAPPP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TTPSGVIKSP GFPEKYPNSL ECTYIVFAPK MSEIILEFES FDLEPDSNPP
      GGMFCRYDRL EIWDGFPDVG PHIGRYCGQK TPGRIRSSSG ILSMVFYTDS AIAKEGFSAN YSVLQSSVSE DFKCMEALGM ESGEIHSDQI TASSQYSTNW SAERSRLNYP ENGWTPGEDS YREWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYKID VSSNGEDWIT IKEGNKPVLF
      QGNTNPTDVV VAVFPKPLIT RFVRIKPATW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITSSN QGDRNWMPEN IRLVTSRSGW ALPPAPHSYI NEWLQIDLGE EKIVRGIIIQ GGKHRENKVF MRKFKIGYSN NGSDWKMIMD DSKRKAKSFE GNNNYDTPEL RTFPALSTRF
      IRIYPERATH GGLGLRMELL GCEVEAPTAG PTTPNGNLVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTVIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDNHVQL KWSVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQNSAHC MTFWYHMSGS HVGTLRVKLR
      YQKPEEYDQL VWMAIGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHISQEDCAK PADLDKKNPE IKIDETGSTP GYEGEGEGDK NISRKPGNVL KTLDPLEHHH HHH.

    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.

    Nrp1 Human
  • View Data Sheet

    Name :

    C1QTNF8 Human

    Description:

    Complement C1q Tumor Necrosis Factor-Related Protein 8 Human Recombinant

    CTRP8, UNQ5829, C1q/TNF-related protein 8, Complement C1q tumor necrosis factor-related protein 8.

    Product # :

    PRO-134

    Price :

    Quantity :

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    • description
    • source
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    Description

    C1QTNF8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 255 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 28.4kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    C1QTNF8 filtered (0.4 µm) solution in 0.03M Acetate buffer pH-4.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      CTRP8, UNQ5829, C1q/TNF-related protein 8, Complement C1q tumor necrosis factor-related protein 8.

    • Physical Appearance

      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

      MKHHHHHHAS WPGLPRRPCV HCCRPAWPPG PYARVSDRDL WRGDLWRGLP RVRPTIDIEI LKGEKGEAGV RGRAGRSGKE GPPGARGLQG RRGQKGQVGP PGAACRRAYA AFSVGRRAYA AFSVGRREGL HSSDHFQAVP FDTELVNLDG AFDLAAGRFL CTVPGVYFLS LNVHTWNYKE TYLHIMLNRR PAAVLYAQPS ERSVMQAQSL MLLLAAGDAV WVRMFQRDRD NAIYGEHGDL YITFSGHLVK PAAEL.

    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.

    C1Qtnf8 Human
  • View Data Sheet

    Name :

    Follistatin Human, His

    Description:

    Follistatin Human Recombinant, His Tag

    FST, FS, Activin-binding protein.

    Product # :

    CYT-029

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • More Info

    Description

    FST His Protein is 36.0 kDa protein containing 325 amino acid residues of the FST His and the 10 aa N-Terminal His-tag.

    Source

    E. coli.

    Formulation

    FST His Tag was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in 20mM TRIS and 20mM NaCl, pH 7.5.

    More Info

    • Introduction

      Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).

    • Synonyms

      FST, FS, Activin-binding protein.

    • Stability

      Store lyophilized FST His at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted FST 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 GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.

    • Background

      What is the molecular weight/Mw of FOLLISTATIN HUMAN, HIS Protein?
      FOLLISTATIN HUMAN, HIS Protein has a total Mw of 36kDa.

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

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

      What is the amino acid sequence of FOLLISTATIN HUMAN, HIS Protein?
      MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.

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

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

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

    Fst His Human
  • View Data Sheet

    Name :

    GIMAP5 Human

    Description:

    GTPase, IMAP Family Member 5 Human Recombinant

    GTPase IMAP family member 5, Immunity-associated nucleotide 4-like 1 protein, Immunity-associated nucleotide 5 protein, IAN-5, hIAN5, Immunity-associated protein 3, GIMAP5, IAN4L1, IAN5, IMAP3, HIMAP3, IAN4, IROD.

    Product # :

    PRO-1695

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    Description

    GIMAP5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 307 amino acids (1-284) and having a molecular mass of 34.4 kDa.GIMAP5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GIMAP5 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GTPase, IMAP Family Member 5 (GIMAP5) is a part of the GTP-binding superfamily and the immuno-associated nucleotide subfamily of nucleotide-binding proteins. GIMAP5 is an antiapoptotic protein which is required for mitochondrial integrity and T-cell survival. Polymorphisms in GIMAP5 are related with systemic lupus erythematosus. Read-through transcription can be found between GIMAP5 and the neighboring upstream GIMAP1 (GTPase, IMAP family member 1) gene. GIMAP5 also contributes to T-cell quiescence.

    • Synonyms

      GTPase IMAP family member 5, Immunity-associated nucleotide 4-like 1 protein, Immunity-associated nucleotide 5 protein, IAN-5, hIAN5, Immunity-associated protein 3, GIMAP5, IAN4L1, IAN5, IMAP3, HIMAP3, IAN4, IROD.

    • 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 MGSMGGFQRG KYGTMAEGRS EDNLSATPPA LRIILVGKTG CGKSATGNSI LGQPVFESKL RAQSVTRTCQ VKTGTWNGRK VLVVDTPSIF ESQADTQELY KNIGDCYLLS APGPHVLLLV IQLGRFTAQD TVAIRKVKEV FGTGAMRHVV ILFTHKEDLG GQALDDYVAN TDNCSLKDLV RECERRYCAF NNWGSVEEQR QQQAELLAVI ERLGREREGS FHSNDLFLDA QLLQRTGAGA CQEDYRQYQA KVEWQVEKHK QELRENESNW AYKALLRVKH LMLLHYE.

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    Gimap5 Human
  • View Data Sheet

    Name :

    Midkine Human

    Description:

    Midkine Human Recombinant

    NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.

    Product # :

    CYT-192

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    Description

    Midkine Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 123 amino acids and having a molecular mass of 13.4kDa. The Midkine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml corresponding to a specific activity of 100,000-10,000,000IU/mg.

    More Info

    • Introduction

      Midkine (MK) is the product of a retinoic acid responsive gene. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
      Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
      The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
      Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
      Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
      Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.

    • Synonyms

      NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VAKKKDKVKK GGPGSECAEW AWGPCTPSSK DCGVGFREGT CGAQTQRIRC RVPCNWKKEF GADCKYKFEN WGACDGGTGT KVRQGTLKKA RYNAQCQETI RVTKPCTPKT KAKAKAKKGK GKD.

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    Midkine Human
  • View Data Sheet

    Name :

    CST11 Human

    Description:

    Cystatin 11 Human Recombinant

    CST8L, CTES2, dJ322G13.6, SC13.

    Product # :

    PRO-1475

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    Description

    CST11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (26-103 a.a.) and having a molecular mass of 11.8kDa.CST11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CST11 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystatin 11 (CST11) is a member of the Cystatin family. The Cystatin superfamily is comprised of proteins with multiple cystatin-like sequences. Several family members are active cysteine protease inhibitors, other family members have lost or perhaps never developed this inhibitory activity. The Cystatin superfamily consists of three inhibitory families, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. The majority of the type 2 cystatin genes and pseudogenes are contained in the cystatin locus on chromosome 20. CST11 is located in the cystatin locus and encodes an epididymal-specific protein whose specific function has not been verified yet.

    • Synonyms

      CST8L, CTES2, dJ322G13.6, SC13.

    • 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 MGSARKKTFL SVHEVMAVEN YAKDSLQWIT DQYNKESDDK YHFRIFRVLK VQRQQVNCFF SVFAVPWFEQ YKILNKSCSS D.

    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.

    Cst11 Human
  • View Data Sheet

    Name :

    S100A4 Mouse

    Description:

    S100 Calcium Binding Protein A4 Mouse Recombinant

    Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.

    Product # :

    PRO-229

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    Description

    S100A4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101 a.a) and having a molecular mass of 13.9kDa.S100A4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A4 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A4 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 belongs to the family of calcium binding proteins such as calmodulin and troponin C. S100A is composed of an alpha and beta chain whereas S100B is composed of two beta chains. S100 protein is also expressed in the antigen presenting cells such as the Langerhans cells in skin and interdigitating reticulum cells in the paracortex of lymph nodes. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100A4 may function in motility, invasion, and tubulin polymerization. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. Chromosomal rearrangements and altered expression of the S100A4 gene have been implicated in tumor metastasis.

    • Synonyms

      Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.

    • 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 MARPLEEALD VIVSTFHKYS GKEGDKFKLN KTELKELLTR ELPSFLGKRT DEAAFQKVMS NLDSNRDNEV DFQEYCVFLS CIAMMCNEFF EGCPDKEPRK K.

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    S100A4 Mouse
  • View Data Sheet

    Name :

    S100A5 Mouse

    Description:

    S100 Calcium Binding Protein A5 Mouse Recombinant

    Protein S100-A5, Protein S-100D, S100 calcium-binding protein A5, S100a5, S100d, S100D9.

    Product # :

    PRO-1084

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    Description

    S100A5 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (1-93) and having a molecular mass of 13.4kDa.The S100A5 is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A5 protein (1mg/ml) is supplied in 20mM Tris-HCl buffer, pH8.0, 40% glycerol, 3mM DTT and 200mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100 calcium binding protein A5 (S100A5) belongs to the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 family members are localized in the cytoplasm and/or nucleus of a wide range of cells, and are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100A5 has a Ca2+ affinity 20-100 fold higher than the other S100 proteins investigated under identical conditions. Furthermore, S100A5 protein binds Zn2+ and Cu2+, and Cu2+ strongly which harms the binding of Ca2+. S100A5 is expressed in very limited regions of the adult brain.

    • Synonyms

      Protein S100-A5, Protein S-100D, S100 calcium-binding protein A5, S100a5, S100d, S100D9.

    • Physical Appearance

      S100A9 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 MGSHMETPLE KALTTMVTTF HKYSGREGSK LTLSRKELKE LIKTELSLAE KMKESSIDNL MKSLDKNSDQ EIDFKEYSVF LTTLCMAYND FFLEDNK.

    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.

    S100A5 Mouse
  • View Data Sheet

    Name :

    CTDSPL Human

    Description:

    CTD Small Phosphatase-Like Human Recombinant

    CTD small phosphatase-like protein, CTDSP-like, Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3, NIF-like protein, Nuclear LIM interactor-interacting factor 1, NLI-interacting factor 1, Protein YA22, hYA22, RBSP3, Small C-terminal domain phosphatase 3, SCP3, Small CTD phosphatase 3, CTDSPL, C3orf8, NIF1, NIFL, SCP3, YA22, PSR1.

    Product # :

    ENZ-569

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    Description

    CTDSPL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (82-265) and having a molecular mass of 23.9kDa.CTDSPL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CTDSPL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CTD small phosphatase-like protein (CTDSPL) specially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the biggest RNA polymerase II subunit POLR2A. CTDSPL negatively regulates RNA polymerase II transcription, probably by directing the transition from initiation/capping to processive transcript elongation. CTDSPL is employed by REST to neuronal genes which contain RE-1 elements, directing to neuronal gene silencing in non-neuronal cells.

    • Synonyms

      CTD small phosphatase-like protein, CTDSP-like, Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3, NIF-like protein, Nuclear LIM interactor-interacting factor 1, NLI-interacting factor 1, Protein YA22, hYA22, RBSP3, Small C-terminal domain phosphatase 3, SCP3, Small CTD phosphatase 3, CTDSPL, C3orf8, NIF1, NIFL, SCP3, YA22, PSR1.

    • 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 MGSHMKYLLP EVTVLDYGKK CVVIDLDETL VHSSFKPISN ADFIVPVEID GTIHQVYVLK RPHVDEFLQR MGQLFECVLF TASLAKYADP VADLLDRWGV FRARLFRESC VFHRGNYVKD LSRLGRELSK VIIVDNSPAS YIFHPENAVP VQSWFDDMTD TELLDLIPFF EGLSREDDVY SMLHRLCNR.

    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.

    Ctdspl Human
  • View Data Sheet

    Name :

    ARPC3 Human

    Description:

    Actin Related Protein 2/3 Complex, Subunit 3 Human Recombinant

    ARC21, p21-Arc, Actin-related protein 2/3 complex subunit 3, Arp2/3 complex 21 kDa subunit, ARPC3.

    Product # :

    PRO-1413

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    Description

    ARPC3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-178 a.a) and having a molecular mass of 22.9kDa. ARPC3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    ARPC3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Actin-related protein 2/3 complex subunit 3 (ARPC3) which Belongs to the ARPC3 family is one of 7 subunits of the human Arp2/3 protein complex. The Arp2/3 complex is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. ARPC3 which is localized to the cytoplasm and cytoskeleton, interacts with p20-ARC and takes part in the structural integrity of the protein complex.

    • Synonyms

      ARC21, p21-Arc, Actin-related protein 2/3 complex subunit 3, Arp2/3 complex 21 kDa subunit, ARPC3.

    • 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 MGSMPAYHSS LMDPDTKLIG NMALLPIRSQ FKGPAPRETK DTDIVDEAIY YFKANVFFKN YEIKNEADRT LIYITLYISE CLKKLQKCNS KSQGEKEMYT LGITNFPIPG EPGFPLNAIY AKPANKQEDE VMRAYLQQLR QETGLRLCEK VFDPQNDKPS KWWTCFVKRQ FMNKSLSGPG Q.

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    Arpc3 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 :

    BAIAP2 Human

    Description:

    BAI1-Associated Protein 2 Human Recombinant

    Brain-specific angiogenesis inhibitor 1-associated protein 2, BAI1-associated protein 2, Protein BAP2, Fas ligand-associated factor 3, FLAF3, IRS-58, IRSp53/58, IRSP53.

    Product # :

    PRO-1022

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    Description

    BAIAP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 530 amino acids (1-522) and having a molecular mass of 58.4kDa.BAIAP2 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BAIAP2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      BAIAP2 is a ubiquitous regulator of the actin cytoskeleton. Controled by the Rho-family GTPases BAIAP2 facilitates filopodia development. BAIAP2 is expressed in the cytoplasm and binds small membrane-bound G-proteins to cytoplasmic effector proteins. BAIAP2 was identified as interacting with the dentatorubral-pallidoluysian atrophy gene, which is related to an autosomal dominant neurodegenerative disease.

    • Synonyms

      Brain-specific angiogenesis inhibitor 1-associated protein 2, BAI1-associated protein 2, Protein BAP2, Fas ligand-associated factor 3, FLAF3, IRS-58, IRSp53/58, IRSP53.

    • 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

      MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE LLTQLEQKVE LDSRYLSAAL KKYQTEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAISN KQGELENYVS DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPSKIPERA VQLMQQVASN GATLPSALSA SKSNLVISDP IPGAKPLPVP PELAPFVGRM SAQESTPIMN GVTGPDGEDY SPWADRKAAQ PKSLSPPQSQ SKLSDSYSNT LPVRKSVTPK NSYATTAENK TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG DLITLLVPEA RDGWHYGESE KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ GKSSSTGNLL DKDDLAIPPP DYGAASRAFP AQTASGFKQR PYSVAVPAFS QGLDDYGARS MSSGSGTLVS TVVEHHHHHH

    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.

    Baiap2 Human
  • View Data Sheet

    Name :

    LGALS10 Human

    Description:

    Charcot-Leyden Crystal Protein Human Recombinant

    Eosinophil lysophospholipase, Charcot-Leyden crystal protein, CLC, Galectin-10, Gal-10, Lysolecithin acylhydrolase, GAL10, LGALS10, LGALS10A.

    Product # :

    PRO-744

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    Description

    LGALS10 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (1-142 a.a.) and having a molecular mass of 18.6kDa.LGALS10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eosinophil lysophospholipase (CLC) acts on biological membranes to regulate the multifunctional lysophospholipids. CLC is a lysophospholipase expressed in eosinophils and basophils. CLC hydrolyzes lysophosphatidylcholine to glycerophosphocholine and a free fatty acid. The CLC protein may possess carbohydrate or IgE-binding activities. CLC is both structurally and functionally related to the galectin family of beta-galactoside binding proteins. CLC may be linked with inflammation and some myeloid leukemias.

    • Synonyms

      Eosinophil lysophospholipase, Charcot-Leyden crystal protein, CLC, Galectin-10, Gal-10, Lysolecithin acylhydrolase, GAL10, LGALS10, LGALS10A.

    • 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 MSLLPVPYTE AASLSTGSTV TIKGRPLACF LNEPYLQVDF HTEMKEESDI VFHFQVCFGR RVVMNSREYG AWKQQVESKN MPFQDGQEFE LSISVLPDKY QVMVNGQSSY TFDHRIKPEA VKMVQVWRDI SLTKFNVSYL KR.

    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.

    Lgals10 Human
  • View Data Sheet

    Name :

    CXCL1 Human

    Description:

    GRO-Alpha Human Recombinant (CXCL1)

    Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

    Product # :

    CHM-329

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    Description

    GRO Alpha Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7811 Dalton. The GRO-alpha is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/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, neutrophilsand 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 protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GRO-alpha 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 CXCL1 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 five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.

    • Background

      What is the molecular weight/Mw of CXCL1 HUMAN Protein?
      CXCL1 HUMAN Protein has a total Mw of 7.81kDa.

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

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

      What is the Biological Activity of CXCL1 HUMAN Protein?
      Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

      What is the amino acid sequence of CXCL1 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.

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

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


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

    Gro A Human
  • View Data Sheet

    Name :

    C3 Mouse

    Description:

    Complement C3 Mouse

    Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    Product # :

    PRO-2705

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    Description

    Mouse Complement C3 produced in Mouse plasma having a molecular weight of 185kDa.

    Source

    Mouse Plasma.

    Formulation

    C3 solution contains phosphate buffer saline.

    Purity

    Greater than 93.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C3 is central to the activation of all 3 pathways of complement activation. Initiation of each pathway generates proteolytic enzyme complexes which binds the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. Most of the C3 activated during complement activation never attaches to the surface due to its thioester reaction with water forming fluid phase C3b which is rapidly inactivated by factors H and I forming iC3b. Surface-bound C3b is necessary in all 3 pathways for efficient activation of C5 and formation of C5b-9 complexes that lyse the target cell membrane.

    • Synonyms

      Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      C3 Mouse is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    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.

    C3 Mouse
  • View Data Sheet

    Name :

    C3a Human

    Description:

    Complement C3a Human

    Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    Product # :

    PRO-2685

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    Description

    Human Complement C3a produced in Human plasma is an non glycosylated polypeptide chain containing 77 amino acids having a molecular weight of 9,089 daltons.

    Source

    Human Plasma.

    Formulation

    C3a solution contains Phosphate buffered saline, pH 7.2.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Native human C3a is created by cleavage of human C3 protein by a human C3 convertase. C3a is a member of the anaphylatoxin family of three proteins (C3a, C4a and C5a) created by the activation of complement. C3a mediates various inflammatory responses including smooth muscle contraction, increased vascular permeability, vasodilation and release of histamine from mast cells and basophils. C3a (In contrast to C5a) does not exhibit significant neutrophil stimulating activities and does not induce chemotaxis, granule release or superoxide production. C3a acts through the C3a Receptor which is a G-protein coupled receptor found mainly on peripheral tissues, lymphoid cells and in the central nervous system. These activities of C3a are inactivated by removal of the C-terminal arginine which happens rapidly in plasma due to the action of carboxypeptidase N.

    • Synonyms

      Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

      C3a Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HTLV-I &II and HBSAG.

    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.

    C3A Human
  • View Data Sheet

    Name :

    ALPP Human, Active

    Description:

    Alkaline Phosphatase Placental Human Recombinant, BioActive

    3 ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1, ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.

    Product # :

    ENZ-1133

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    Description

    ALPP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 494 amino acids (23-506 a.a.) and having a molecular mass of 53.9kDa. ALPP is expressed with a 10 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ALPP protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,500unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0nmole of pnitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.

    More Info

    • Introduction

      Placental alkaline phosphatase also known as PLAP is a membranal siaglycoprotein enzyme typicallyfoundin high concentration in syncytiotrophoblasts in the placenta amid the 3th trimester of gestation. The expression of PLAP was at firstconsidered to be onlyin the term placenta, though, a human PLAP-like variant has been found,thathas more than 85% homology with PLAP itself. PLAP is expressed strictly in normal term placenta, endocervix & fallopian tube and in ovarian and proximal gastrointestinal tumors. It is also widely expressed in germ cell tumors and more recently found in seminomas.

    • Synonyms

      3 ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1, ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.

    • 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

      ADLMIIPVEE ENPDFWNREA AEALGAAKKL QPAQTAAKNL IIFLGDGMGV STVTAARILK GQKKDKLGPE LPLAMDRFPY VALSKTYNVD KHVPDSGATA TAYLCGVKGN FQTIGLSAAA RFNQCNTTRG NEVISVMNRA KKAGKSVGVV TTTRVQHASP AGTYAHTVNR NWYSDADVPA SARQEGCQDI ATQLISNMDI DVILGGGRKY MFRMGTPDPE YPDDYSQGGT RLDGKNLVQE WLAKRQGARY VWNRTELMQA SLDPSVTHLM GLFEPGDMKY EIHRDSTLDP SLMEMTEAAL RLLSRNPRGF FLFVEGGRID HGHHESRAYR ALTETIMFDD AIERAGQLTS EEDTLSLVTA DHSHVFSFGG YPLRGSSIFG LAPGKARDRK AYTVLLYGNG PGYVLKDGAR PDVTESESGS PEYRQQSAVP LDEETHAGED VAVFARGPQA HLVHGVQEQT FIAHVMAFAA CLEPYTACDL APPAGTTDHH HHHH.

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

    Alpp Human
  • View Data Sheet

    Name :

    Troponin C-I Human

    Description:

    Cardiac Troponin C-I Complex Human Recombinant

    Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.

    Product # :

    PRO-345

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    Description

    Recombinant Human Cardiac Troponin C-I complex produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of approximately 50kDa. The Molar ratio on cTnC to cTnI is 1:1. The Cardiac Troponin C-I is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Human Cardiac Troponin C-I complex solution contains 500 mM Nacl, 20mM Tris-HCl and 60 mM B-mercaptoethanol, pH 7.5.

    Purity

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

    More Info

    • Introduction

      Troponin Complex is a heteromeric protein playing an important role in the regulation of skeletal and cardiac muscle contraction. It consists of three subunits, Troponin I, Troponin T and TroponinC. Each subunit is responsible for part of Troponin Complex function. E.g. Troponin I inhibits ATP-ase activity of acto-myosin.Troponin T and Troponin Iare presented in cardiac muscles in different forms than in skeletal muscles. Purified subunits of rcTnI, rcTnC and rcTnT are recomplexed in vitro under appropriate conditions.

    • Synonyms

      Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.

    • Physical Appearance

      Sterile Filtered colourless liquid formualtion.

    • 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.

    Troponin Ic
  • View Data Sheet

    Name :

    Thromboplastin Bovine

    Description:

    Thromboplastin Bovine

    Tissue factor, Coagulation factor III, Thromboplastin, CD142, TF, F3, TFA.

    Product # :

    PRO-2760

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    Description

    Thromboplastin bovine native

    Source

    Bovine Lung.

    Formulation

    The bovine thromboplastin was lyophilized with no additives.

    More Info

    • Introduction

      Tissue factor is well-known as the main cellular initiator of blood coagulation. The Tissue factor gene encodes coagulation factor III which is a cell surface glycoprotein that enables cells to initiate the blood coagulation cascades, and functions as the high-affinity receptor for the coagulation factor VII. Following vessel injury, the Tissue Factor and Factor VIIa complex activates the coagulation protease cascade, which leads to fibrin deposition and activation of platelets. The ensuing complex presents a catalytic event, which is responsible for initiation of the coagulation protease cascades by specific limited proteolysis. Therefore, Tissue factor has a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. Tissue Factor can also be stimulated by the inflammatory mediators interleukin 1 and TNF, as well as by endotoxin, to appear on monocytes and vascular endothelial cells as a component of cellular immune response.
      Tissue factor is the only one in the coagulation pathway for which a congenital deficiency has not been described. Certain levels of Tissue Factor are essential for the maintained viability and growth of endothelium and Tissue Factor-expressing tumor cells. Additionally, abnormal Tissue Factor expression inside the vasculature initiates life threatening thrombosis in various diseases, for example sepsis, atherosclerosis, and cancer. Alternative spliced Tissue Factor expression advances tumor growth, and is linked to increased tumor cell proliferation and angiogenesis in pancreatic cancer.

    • Synonyms

      Tissue factor, Coagulation factor III, Thromboplastin, CD142, TF, F3, TFA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bovine Thromboplastin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Prothrombin should be stored at 4C between 2-7 days and for future use below -18C.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 Bovine Thromboplastin in sterile 0.9% NaCl

    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.

    Thromboplastin Bovine
  • View Data Sheet

    Name :

    Fibronectin Recombinant, Oryza

    Description:

    Fibronectin, Oryza Human Recombinant

    Product # :

    PRO-2841

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    Description

    Fibronectin Human Recombinant is a single, non-glycosylated polypeptide chain having a molecular mass of 216kDa. The Fibronectin is purified by proprietary chromatographic techniques.

    Source

    Oryza sativa (rice).

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Fibronectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibronectin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

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

    • Background

      Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism mainly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.

    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.

    Fibronectin Human Protein
  • View Data Sheet

    Name :

    GDNF Rat

    Description:

    Glial-Derived Neurotrophic Factor Rat Recombinant

    ATF1, ATF2, HFB1-GDNF, GDNF.

    Product # :

    CYT-403

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    Description

    Glial derived Neurotrophic Factor Rat Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 134 amino acids and having a total molecular mass of 29.8 kDa.

    Source

    Escherichia Coli.

    Formulation

    GDNF was lyophilized from a sterile solution containing 1xPBS, pH 7.4.

    Purity

    Greater than 98.0% as determined by HPLC analysis and by SDS-PAGE.

    Biological Activity

    Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

    More Info

    • Introduction

      GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
      GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.

    • Synonyms

      ATF1, ATF2, HFB1-GDNF, GDNF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI

    • Background

      What is the molecular weight/Mw of GDNF RAT Protein?
      GDNF RAT Protein has a total Mw of 29.8kDa.

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

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

      What is the Biological Activity of GDNF RAT Protein?
      Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

      What is the amino acid sequence of GDNF RAT Protein?
      SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI

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

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

    Gdnf Rat
  • View Data Sheet

    Name :

    Streptavidin

    Description:

    Streptavidin Recombinant

    Product # :

    PRO-791

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    Description

    Streptavidin Streptomyces Avidinii Recombinant produced in E.Coli. The molecular weight per tetramer is approximately 52kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized in 10mM potassium phosphate buffer pH 6.5.

    Purity

    Greater than 98.0% as determined by SDS-PAGE and HPLC.

    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 White lyophilized (freeze-dried) powder.

    • Stability

      Streptavidin is shipped at ambient temperature, upon arrival store at -20°C.

    • Solubility

      It is recommended to reconstitute the lyophilized Streptavidin in sterile 18MΩ-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLT
      GRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGA
      EARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAAS.

    • Proteolytic Activity

      < 10-3 U/mg protein (Azocoll, 25 °C, 24 h, pH 8.0).

    • Specific Activity

      > 17U/mg (one unit binds 1 μg D-biotin).

    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.

    Streptavidin Recombinant
  • View Data Sheet

    Name :

    CNTF Human

    Description:

    Ciliary-Neurotrophic Factor Human Recombinant

    HCNTF, CNTF, Ciliary Neurotrophic Factor.

    Product # :

    CYT-272

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 22706 Dalton. The CNTF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 5mM sodium Phosphate buffer pH=7.5 and 5mM sodium chloride.

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

      HCNTF, CNTF, Ciliary Neurotrophic Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Ciliary Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized HCNTF 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 five N-terminal amino acids was determined and was found to be Met-Ala-Phe-Thr-Glu.

    • Background

      Exploring the Potential of Human Recombinant Ciliary-Neurotrophic Factor: Implications and Applications

      Abstract:

      Ciliary-Neurotrophic Factor (CNTF) holds remarkable promise in neurobiology and therapeutic development due to its neuroprotective and regenerative properties. This paper delves into the significance of Human Recombinant CNTF, its production methodologies, and its potential applications in treating neurodegenerative disorders. The review sheds light on the therapeutic potential of CNTF and its role in advancing neuroregeneration research.

      Introduction:

      CNTF, a neurotrophic cytokine, is known for its pivotal role in neuronal survival and growth. The availability of Human Recombinant CNTF allows researchers to investigate its therapeutic potential and explore avenues for developing novel treatments for neurodegenerative diseases. CNTF's ability to support neuronal health and promote regeneration makes it a promising candidate for medical interventions.

      Mechanisms of Action:

      CNTF interacts with specific receptor complexes, activating various downstream signaling pathways, including Janus kinase (JAK) and Signal Transducer and Activator of Transcription (STAT) pathways. These pathways contribute to cell survival, differentiation, and axonal growth, forming the foundation for CNTF's neuroprotective effects.

      Production Methods:

      Human Recombinant CNTF is produced by introducing the CNTF gene into suitable expression systems, often employing bacterial or mammalian cells. Ensuring proper post-translational modifications is essential for maintaining the protein's biological activity and therapeutic potential.

      Therapeutic Applications:

      CNTF's neuroprotective and regenerative effects offer potential therapeutic applications in neurodegenerative disorders, such as amyotrophic lateral sclerosis (ALS), retinal degeneration, and Parkinson's disease. It holds promise for preserving and restoring neuronal function, thereby improving the quality of life for affected individuals.

      Challenges and Future Directions:

      While Human Recombinant CNTF shows great potential, challenges include precise dosing, delivery methods, and potential side effects. Further research is needed to optimize CNTF-based therapies and assess their long-term safety and efficacy in clinical settings.

      Conclusion:

      Human Recombinant Ciliary-Neurotrophic Factor emerges as a critical tool in advancing our understanding of neuroprotection and neuroregeneration. Its potential in treating neurodegenerative disorders highlights the ongoing quest for innovative therapeutic approaches that harness the body's inherent ability to heal and regenerate.

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 22kDa.

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

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

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

      What is the amino acid sequence of CNTF Protein?
      CNTF Protein is composed from 199 amino acids.

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

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

    • Protein content

      CNTF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.28 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 CNTF Recombinant 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.

    Cntf Human
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