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Search results

1000 results found for “Folate Receptor”

Name

Description

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  • View Data Sheet

    Name :

    SNTN Human

    Description:

    Sentan Cilia Apical Structure Protein Human Recombinant

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

    Product # :

    PRO-216

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    Description

    SNTN Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids (1-147a.a.) and having a molecular mass of 18.6kDa. The SNTN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGGCMHSTQD KSLHLEGDPN PSAAPTSTCA PRKMPKRISI SKQLASVKAL RKCSDLEKAI ATTALIFRNS SDSDGKLEKA IAKDLLQTQF RNFAEGQETK PKYREILSEL DEHTENKLDF EDFMILLLSI TVMSDLLQNI RNVKIMK

    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.

    Sntn Human
  • View Data Sheet

    Name :

    CXCL5 Human (8-78 a.a)

    Description:

    Epithelial Neutrophil-Activating Protein 78, 8-78 a.a. Human Recombinant (CXCL5)

    Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.

    Product # :

    CHM-265

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    Description

    Epithelial Neutrophil-Activating Protein 78 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids (8-78 a.a.) and having a molecular mass of 7.8kDa. The CXCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The biological activity was determined by 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 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils, and can be inhibited with the type II interferon IFN-?. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.

    • Synonyms

      Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ENA78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 ENA-78 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      LRELRCVCLQ TTQGVHPKMI SNLQVFAIGP QCSKVEVVAS LKNGKEICLD PEAPFLKKVI QKILDGGNKE N.

    • Background

      What is the molecular weight/Mw of CXCL5 HUMAN (8-78 A.A) Protein?
      CXCL5 HUMAN (8-78 A.A) Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CXCL5 HUMAN (8-78 A.A) Protein?
      Escherichia Coli.

      What is the Purity of CXCL5 HUMAN (8-78 A.A) Protein?
      CXCL5 HUMAN (8-78 A.A) Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL5 HUMAN (8-78 A.A) Protein?
      The biological activity was 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 CXCL5 HUMAN (8-78 A.A) Protein?
      LRELRCVCLQ TTQGVHPKMI SNLQVFAIGP QCSKVEVVAS LKNGKEICLD PEAPFLKKVI QKILDGGNKE N.

      What applications can CXCL5 HUMAN (8-78 A.A) Protein be used in?
      CXCL5 HUMAN (8-78 A.A) Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL5 HUMAN (8-78 A.A) Protein?
      The endotoxin level is minimal, CXCL5 HUMAN (8-78 A.A) 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.

    Ena 78 Human 8 78 Aa
  • View Data Sheet

    Name :

    PDGF BB Rat

    Description:

    Platelet-Derived Growth Factor BB Rat Recombinant

    Platelet-derived growth factor subunit B, PDGF subunit B, PDGF-2, Platelet-derived growth factor B chain, Platelet-derived growth factor beta polypeptide, Pdgfb, SIS, c-sis.

    Product # :

    CYT-740

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    Description

    PDGF-BB Rat Recombinant produced in E.coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide of two B chains containing 2x109 amino acids (218 amino acids in total) and having a molecular mass of 24.4 kDa.The PDGF-BB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PDGF-BB was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.0.

    Purity

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

    Biological Activity

    The ED50as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

    More Info

    • Introduction

      PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.

    • Synonyms

      Platelet-derived growth factor subunit B, PDGF subunit B, PDGF-2, Platelet-derived growth factor B chain, Platelet-derived growth factor beta polypeptide, Pdgfb, SIS, c-sis.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SLGSLAAAEP AVIAECKTRT EVFQISRNLI DRTNANFLVW PPCVEVQRCS GCCNNRNVQC RASQVQMRPV QVRKIEIVRK KPVFKKATVT LEDHLACKCE TVVTPRPVT.

    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.

    Pdgf Bb Rat
  • View Data Sheet

    Name :

    PFDN5 Human

    Description:

    Prefoldin Subunit 5 Human Recombinant

    Prefoldin subunit 5, C-Myc-binding protein Mm-1, Myc modulator 1, PFDN5, MM1, PFD5, MM-1.

    Product # :

    PRO-901

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    Description

    PFDN5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154 a.a.) and having a molecular mass of 19.5kDa.PFDN5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PFDN5 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PFDN5 is a member of the prefoldin alpha subunit family. Prefoldin (PFDN) being a ubiquitously expressed heterohexameric co-chaperone, is required for proper folding of nascent proteins, in particular, tubulin and actin. PFDN5 is one of 6 subunits of prefoldin, which is a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thus allowing them to fold properly. The PFDN5 protein may also limit the transcriptional activity of the proto-oncogene c-Myc.

    • Synonyms

      Prefoldin subunit 5, C-Myc-binding protein Mm-1, Myc modulator 1, PFDN5, MM1, PFD5, MM-1.

    • 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 MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK DFFKRKIDFL TKQMEKIQPA LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA TAKA.

    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.

    Pfdn5 Human
  • View Data Sheet

    Name :

    PHF11 Human

    Description:

    PHF11 Protein Human Recombinant

    PHD finger protein 11, BRCA1 C-terminus-associated protein, Renal carcinoma antigen NY-REN-34, PHF11, BCAP, APY, IGEL, IGER, IGHER, NYREN34, NY-REN-34, RP11-185C18.3.

    Product # :

    PRO-1268

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    Description

    PHF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 351 amino acids (1-331 a.a.) and having a molecular mass of 39.7kDa.PHF11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PHF11 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PHD finger protein 11 (PHF11) is a regulator of TH1-type cytokine gene expression. The decline in PHF11 expression observed with an AD-associated genotype may promote the intense TH2 reactions which characterize numerous allergic individuals. PHF11 is linked with raised total serum IgE levels, asthma and acute atopic dermatitis (AD) in children. Even though PHF11 includes a plant homeodomain, a motif frequently found in transcriptional regulators, PHF11 function of has yet been examined.

    • Synonyms

      PHD finger protein 11, BRCA1 C-terminus-associated protein, Renal carcinoma antigen NY-REN-34, PHF11, BCAP, APY, IGEL, IGER, IGHER, NYREN34, NY-REN-34, RP11-185C18.3.

    • 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 MAQASPPRPE RVLGASSPEA RPAQEALLLP TGVFQVAEKM EKRTCALCPK DVEYNVLYFA QSENIAAHEN CLLYSSGLVE CEDQDPLNPD RSFDVESVKK EIQRGRKLKC KFCHKRGATV GCDLKNCNKN YHFFCAKKDD AVPQSDGVRG IYKLLCQQHA QFPIIAQSAK FSGVKRKRGR KKPLSGNHVQ PPETMKCNTF IRQVKEEHGR HTDATVKVPF LKKCKEAGLL NYLLEEILDK VHSIPEKLMD ETTSESDYEE IGSALFDCRL FEDTFVNFQA AIEKKIHASQ QRWQQLKEEI ELLQDLKQTL CSFQENRDLM SSSTSISSLS Y.

    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.

    Phf11 Human
  • View Data Sheet

    Name :

    Flavokinase Human

    Description:

    Riboflavin Kinase Human Recombinant

    Riboflavin kinase, ATP:riboflavin 5'-phosphotransferase, Flavokinase, RFK, RIFK, FLJ11149, RP11-422N19.2.

    Product # :

    PKA-352

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    Description

    Flavokinase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids (1-162 a.a.) and having a molecular mass of 20.5kDa. Flavokinase is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Flavokinase solution containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Flavokinase is a transferases family member, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. Flavokinase is an enzyme that catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), which is an obligatory step in vitamin B2 utilization and flavin cofactor synthesis. It has been proposed that TNF, through the activation of the RFK gene, enhances the incorporation of FAD in NADPH oxidase enzymes, which is a critical step for the assembly and activation of NADPH oxidase.

    • Synonyms

      Riboflavin kinase, ATP:riboflavin 5'-phosphotransferase, Flavokinase, RFK, RIFK, FLJ11149, RP11-422N19.2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Flavokinase although stable at 4°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPRADCIMRH LPYFCRGQVV RGFGRGSKQL GIPTANFPEQ VVDNLPADIS TGIYYGWASV GSGDVHKMVV SIGWNPYYKN TKKSMETHIM HTFKEDFYGE ILNVAIVGYL RPEKNFDSLE SLISAIQGDI EEAKKRLELP EHLKIKEDNF FQVSKSKIMNGH.

    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.

    Flavokinase Human
  • View Data Sheet

    Name :

    PLAC8 Human

    Description:

    Placenta-Specific 8 Human Recombinant

     Placenta-Specific 8, C15, Onzin, Placenta-Specific Gene 8 Protein, Protein C15.

    Product # :

    PRO-1725

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    Description

    PLAC8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 14.9kDa.PLAC8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PLAC8 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0),0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Placenta-Specific 8 (PLAC8) is a member of the cornifelin family. The PLAC8 protein is expressed at high levels in the plasmacytoid dendritic cells, spleen, lymph nodes, peripheral blood leukocytes, and bone marrow.

    • Synonyms

      Placenta-Specific 8, C15, Onzin, Placenta-Specific Gene 8 Protein, Protein C15.

    • 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 MGSMQAQAPV VVVTQPGVGP GPAPQNSNWQ TGMCDCFSDC GVCLCGTFCF PCLGCQVAAD MNECCLCGTS VAMRTLYRTR YGIPGSICDD YMATLCCPHC TLCQIKRDIN RRRAMRTF.

    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.

    Plac8 Human
  • View Data Sheet

    Name :

    CDC123 Human

    Description:

    Cell Division Cycle 123 Human Recombinant

    C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

    Product # :

    PRO-1463

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    Description

    CDC123 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-336 a.a) and having a molecular mass of 41.5kDa.CDC123 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDC123 protein solution (0. 5mg/ml) 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

      CDC123 is a member of the CDC123 family. CDC123is required for S phase entry of the cell cycle. It is also broadly expressed in spleen,thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the uppermost expression in testis.

    • Synonyms

      C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

    • 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 MGSMKKEHVL HCQFSAWYPF FRGVTIKSVI LPLPQNVKDY LLDDGTLVVS GRDDPPTHSQ PDSDDEAEEI QWSDDENTAT LTAPEFPEFA TKVQEAINSL GGSVFPKLNW SAPRDAYWIA MNSSLKCKTL SDIFLLFKSS DFITRDFTQP FIHCTDDSPD PCIEYELVLR KWCELIPGAE FRCFVKENKL IGISQRDYTQ YYDHISKQKE EIRRCIQDFF KKHIQYKFLD EDFVFDIYRD SRGKVWLIDF NPFGEVTDSL LFTWEELISE NNLNGDFSEV DAQEQDSPAF RCTNSEVTVQ PSPYLSYRLP KDFVDLSTGE DAHKLIDFLK LKRNQQEDD

    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.

    Cdc123 Human
  • View Data Sheet

    Name :

    GP9 Human

    Description:

    Glycoprotein-9 Human Recombinant

    Platelet glycoprotein IX, GP-IX, GPIX, Glycoprotein 9, CD42a, Glycoprotein IX (Platelet).

    Product # :

    PRO-055

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    Description

    GP9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (17-147) and having a molecular mass of 16.8kDa. GP9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GP9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2M UREA and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycoprotein-9 (GP9) is a small membrane glycoprotein found on the surface of human platelets. GP9 forms a one to one noncovalent complex with glycoprotein Ib, a platelet surface membrane glycoprotein complex which functions as a receptor for von Willebrand factor. The complete receptor complex includes noncovalent association of the alpha and beta subunits with the protein and platelet glycoprotein V. GP9 gene defects cause the Bernard-Soulier syndrome, aka giant platelet disease whose patients have unusually large platelets and have a clinical bleeding tendency.

    • Synonyms

      Platelet glycoprotein IX, GP-IX, GPIX, Glycoprotein 9, CD42a, Glycoprotein IX (Platelet).

    • 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 MGSTKDCPSP CTCRALETMG LWVDCRGHGL TALPALPART RHLLLANNSL QSVPPGAFDH LPQLQTLDVT QNPWHCDCSL TYLRLWLEDR TPEALLQVRC ASPSLAAHGP LGRLTGYQLG SCGWQLQASW VRPG.

    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.

    Gp9 Human
  • View Data Sheet

    Name :

    CNTF Rat

    Description:

    Ciliary Neurotrophic Factor Rat Recombinant

    HCNTF, CNTF, Ciliary Neurotrophic Factor.

    Product # :

    CYT-654

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    Description

    CNTF Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids and having a molecular mass of 22834 Dalton. The CNTF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 0.025% NaHCO3.

    Purity

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

    Biological Activity

    Fully biologically active by its ability to phosphorylate STAT3 in several cells lines.

    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 CNTF 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 CNTF in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.

    • Amino Acid Sequence

      AFAEQTPLTL HRRDLSSRSIWLARKIRSDLTALMESYVKHQGLNKNI
      NLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRV
      HFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPA
      TVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESH
      YGAKDKQM.

    • Background

      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 >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of CNTF Protein?
      Fully biologically active by its ability to phosphorylate STAT3 in several cells lines.
      What is the amino acid sequence of CNTF Protein?
      AFAEQTPLTL HRRDLSSRSIWLARKIRSDLTALMESYVKHQGLNKNI
      NLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRV
      HFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPA
      TVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESH YGAKDKQM.


      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.

    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 Rat
  • View Data Sheet

    Name :

    CXCL7 95 a.a Human

    Description:

    Neutrophil Activating Protein-2 (CXCL7) Human Recombinant, 95 a.a.

    Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    Product # :

    CHM-277

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    Description

    NAP 2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (35-128) and having a molecular mass of 10.3 kDa.The NAP 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAP 2 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-7.5, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

    • Synonyms

      Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    • Physical Appearance

      NAP 2 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

      MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD

    • Background

      What is the molecular weight/Mw of CXCL7 95 A.A HUMAN Protein?
      CXCL7 95 A.A HUMAN Protein has a total Mw of 10.3kDa.

      What is the source or expression system of CXCL7 95 A.A HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL7 95 A.A HUMAN Protein?
      CXCL7 95 A.A HUMAN Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL7 95 A.A HUMAN Protein?
      The biological functionality of CXCL7 95 A.A HUMAN Protein will be determined in the future.

      What is the amino acid sequence of CXCL7 95 A.A HUMAN Protein?
      MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD

      What applications can CXCL7 95 A.A HUMAN Protein be used in?
      CXCL7 95 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL7 95 A.A HUMAN Protein?
      The endotoxin level is minimal, CXCL7 95 A.A 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.

    Nap 2 95 Aa Human
  • View Data Sheet

    Name :

    ErbB3 Mouse

    Description:

    Tyrosine Kinase ErbB-3 Mouse Recombinant

    Receptor tyrosine-protein kinase erbB-3, Glial growth factor receptor, Proto-oncogene-like protein c-ErbB-3.

    Product # :

    PKA-085

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    Description

    ErbB3 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 630 amino acids (20-641.a.) and having a molecular mass of 69.5kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). ErbB3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ErbB3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ErbB3, also called Her3 (human epidermal growth factor receptor 3), is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. Among ErbB family members, ErbB3 is unique in that it contains a defective kinase domain. ErbB3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric ErbB3 serves as a low affinity receptor for the heregulins (HRG). ErbB3 can induce specific antibody production in vivo, hence to inhibit tumor cell growth. ErbB-3 can be used to treat early, medium and advanced or post-operative breast cancer with over-expression of ErbB2. According to its mechanism of action, ErbB3 is classified as a therapeutic for cancer.

    • Synonyms

      Receptor tyrosine-protein kinase erbB-3, Glial growth factor receptor, Proto-oncogene-like protein c-ErbB-3.

    • 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

      SEMGNSQAVC PGTLNGLSVT GDADNQYQTL YKLYEKCEVV MGNLEIVLTG HNADLSFLQW IREVTGYVLV AMNEFSVLPL PNLRVVRGTQ VYDGKFAIFV MLNYNTNSSH ALRQLRFTQL TEILLGGVYI EKNDKLCHMD TIDWRDIVRV PDAEIVVKNN GGNCPPCHEV CKGRCWGPGP EDCQILTKTI CAPQCNGRCF GPNPNQCCHD ECAGGCSGPQ DTDCFACRHF NDSGACVPRC PAPLVYNKLT FQLEPNPHIK YQYGGVCVAS CPHNFVVDQT FCVRACPADK MEVDKNGLKM CEPCRGLCPK ACEGTGSGSR YQTVDSSNID GFVNCTKILG NLDFLITGLN GDPWHKIPAL DPEKLNVFRT VREITGYLNI QSWPPHMHNF SVFSNLTTIG GRSLYNRGFS LLIMKNLNVT SLGFRSLKEI SAGRVYISAN QQLCYHHSLN WTRLLRGPAE ERLDIKYNRP LGECVAEGKV CDPLCSSGGC WGPGPGQCLS CRNYSREGVC VTHCNVLQGE PREFVHEAHC FSCHPECQPM EGTSTCNGSG SDACARCAHF RDGPHCVNSC PHGILGAKGP IYKYPDAQNE CRPCHENCTQ GCKGPELQDC LGQAEVLMSK PHLEHHHHHH.

    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.

    Erbb3 Mouse
  • View Data Sheet

    Name :

    CRP Rat

    Description:

    C-Reactive Protein Rat Recombinant

    Ptx1, C-reactive protein, Pentraxin 1, C-Reactive Protein Pentraxin-Related.

    Product # :

    PRO-1421

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    Description

    CRP produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 217 amino acids (20-230 a.a.) and having a molecular mass of 24.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa).CRP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CRP protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically (up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.

    • Synonyms

      Ptx1, C-reactive protein, Pentraxin 1, C-Reactive Protein Pentraxin-Related.

    • 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

      HEDMSKQAFV FPGVSATAYV SLEAESKKPL EAFTVCLYAH ADVSRSFSIF SYATKTSFNE ILLFWTRGQG FSIAVGGPEI LFSASEIPEV PTHICATWES ATGIVELWLD GKPRVRKSLQ KGYIVGTNAS IILGQEQDSY GGGFDANQSL VGDIGDVNMW DFVLSPEQIN AVYVGRVFSP NVLNWRALKY ETHGDVFIKP QLWPLTDCCE SHHHHHH.

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    Crp Rat
  • View Data Sheet

    Name :

    Adiponectin Mouse, Trimeric

    Description:

    Adiponectin Mouse Recombinant, Trimeric form

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-247

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    Description

    Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.

    Source

    HEK293 (Human embryonic kidney cell line).

    Formulation

    Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.

    Purity

    Acrp30 Mouse purity is greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
      In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Physical Appearance

      Filtered white lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Acrp30 Mouse at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Mouse can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add deionized water to prepare a working stock solution of approximately 0.5 mg/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.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 26kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293

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

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

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

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

    Adiponectin Mouse Trimeric
  • View Data Sheet

    Name :

    GPNMB Human, Sf9

    Description:

    Glycoprotein Nmb Human Recombinant, Sf9

    Transmembrane glycoprotein NMB, Transmembrane glycoprotein HGFIN, GPNMB, HGFIN, NMB, Glycoprotein (transmembrane) nmb.

    Product # :

    PRO-2394

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    Description

    GPNMB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 462 amino acids (22-474a.a.) and having a molecular mass of 51.8kDa. GPNMB is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GPNMB protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycoprotein Nmb (GPNMB) is a member of the PMEL/NMB family. GPNMB is a type I transmembrane glycoprotein which exhibits homology to the pMEL17 precursor, a melanocyte-specific protein. GPNMB is expressed in the lowly metastatic human melanoma cell lines and xenografts but has no expression in the highly metastatic cell lines. GPNMB might be involved in growth delay and reduction of metastatic potential. GPNMB is up-regulated in a number of cancer cells, including in glioblastoma multiforme. GPNMB is expressed in many melanoma cells, as well as in tissue macrophages, including liver Kuppfer cells and lung alveolar macrophages, in podocytes and in some cells of the ciliary body of the eye (at protein level). GPNMB is hardly detectable in the healthy brain.

    • Synonyms

      Transmembrane glycoprotein NMB, Transmembrane glycoprotein HGFIN, GPNMB, HGFIN, NMB, Glycoprotein (transmembrane) nmb.

    • 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

      ADPAKRFHDV LGNERPSAYM REHNQLNGWS SDENDWNEKL YPVWKRGDMR WKNSWKGGRV QAVLTSDSPA LVGSNITFAV NLIFPRCQKE DANGNIVYEK NCRNEAGLSA DPYVYNWTAW SEDSDGENGT GQSHHNVFPD GKPFPHHPGW RRWNFIYVFH TLGQYFQKLG RCSVRVSVNT ANVTLGPQLM EVTVYRRHGR AYVPIAQVKD VYVVTDQIPV FVTMFQKNDR NSSDETFLKD LPIMFDVLIH DPSHFLNYST INYKWSFGDN TGLFVSTNHT VNHTYVLNGT FSLNLTVKAA APGPCPPPPP PPRPSKPTPS LGPAGDNPLE LSRIPDENCQ INRYGHFQAT ITIVEGILEV NIIQMTDVLM PVPWPESSLI DFVVTCQGSI PTEVCTIISD PTCEITQNTV CSPVDVDEMC LLTVRRTFNG SGTYCVNLTL GDDTSLALTS TLISVPHHHH HH.

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    Gpnmb Human Sf9
  • View Data Sheet

    Name :

    Adiponectin Human, Sf9

    Description:

    Adiponectin Human Recombinant, Sf9

    Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.

    Product # :

    CYT-1002

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    • sds-page

    Description

    Acrp30 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (106-242a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). Acrp30 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Acrp30 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    Adiponectin-sds-page - Product image 1

    More Info

    • Introduction

      The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
      Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
      The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
      Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.

    • Synonyms

      Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 16.9kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      Sf9, Baculovirus cells.

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

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.

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

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

    Acrp30 Human Sf9
  • View Data Sheet

    Name :

    AHCY Human, Sf9

    Description:

    Adenosylhomocysteinase Human Recombinant, Sf9

    EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.

    Product # :

    ENZ-1034

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    Description

    AHCY Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (1-432 a.a.) and having a molecular mass of 48.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). AHCY is fused to a 6 amino acids His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.

    • Synonyms

      EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.

    • 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

      ADLMSDKLPY KVADIGLAAW GRKALDIAEN EMPGLMRMRE RYSASKPLKG ARIAGCLHMT VETAVLIETL VTLGAEVQWS SCNIFSTQDH AAAAIAKAGI PVYAWKGETD EEYLWCIEQT LYFKDGPLNM ILDDGGDLTN LIHTKYPQLL PGIRGISEET TTGVHNLYKM MANGILKVPA INVNDSVTKS KFDNLYGCRE SLIDGIKRAT DVMIAGKVAV VAGYGDVGKG CAQALRGFGA RVIITEIDPI NALQAAMEGY EVTTMDEACQ EGNIFVTTTG CIDIILGRHF EQMKDDAIVC NIGHFDVEID VKWLNENAVE KVNIKPQVDR YRLKNGRRII LLAEGRLVNL GCAMGHPSFV MSNSFTNQVM AQIELWTHPD KYPVGVHFLP KKLDEAVAEA HLGKLNVKLT KLTEKQAQYL GMSCDGPFKP DHYRYHHHHH H.

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    Ahcy Human Sf9
  • View Data Sheet

    Name :

    NAIF1 Human

    Description:

    Nuclear Apoptosis Inducing Factor 1 Human Recombinant

    bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.

    Product # :

    PRO-1978

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    Description

    NAIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 37.6kDa. NAIF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAIF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.

    • Synonyms

      bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.

    • 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 MGSMAVPAKK RKMNFSEREV EIIVEELELK KHLLVNHFNA GVPLAAKSAA WHGILRRVNA VATCRRELPE VKKKWSDLKT EVRRKVAQVR AAVEGGEAPG PTEEDGAGGP GTGGGSGGGG PAVAPVLLTP MQQRICNLLG EATIISLPST TEIHPVALGP SATAAAATVT LTQIPTETTY HTLEEGVVEY CTAEAPPPLP PETPVDMMAQ HADTSVKPQA LKSRIALNSA KLIQEQRVTN LHVKEIAQHL EQQNDLLQMI RRSQEVQACA QERQAQAMEG TQAALSVLIQ VLRPMIKDFR RYLQSNTANP APASDPGQVA QNGQPDSIIQ.

    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.

    Naif1 Human
  • View Data Sheet

    Name :

    PF4 Human, His

    Description:

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

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

    Product # :

    CHM-015

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MEAEEDGDLQ CLCVKTTSQV RPRHITSLEV IKAGPHCPTA QLIATLKNGR KICLDLQAPL YKKIIKKLLE S.

    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.

    Pf4 Human His
  • View Data Sheet

    Name :

    LTF Holo Human

    Description:

    Lactoferrin Holo Human Recombinant

    Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    Product # :

    PRO-592

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    Description

    Recombinant Human Holo Lactoferrin produced in Plant is a glycosylated mature polypeptide sequence having an approximate molecular mass of 80 kDa.The Human Holo Lactoferrin is purified by proprietary chromatographic techniques.

    Source

    Rice Flour.

    Formulation

    The Human Holo lactoferrin was lyophilized with no additives.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.

    • Synonyms

      Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    • Physical Appearance

      Pink lyophilized powder.

    • Stability

      Recombinant Holo Lactoferrin although stable at room temperature for 5 days, should be stored desiccated below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized LTF Holo Human in sterile water at 10mg/ml, which can then be further diluted to other aqueous solutions.

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

    Lactoferrin Holo Human
  • View Data Sheet

    Name :

    BMP 7 Human, HEK

    Description:

    Bone Morphogenetic protein-7 Human Recombinant, HEK

    Osteogenic Protein 1, BMP-7.

    Product # :

    CYT-082

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    Description

    BMP-7 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 30-38kDa due to glycosylation.The BMP7 corresponds to amino acid residues 315 to 431 of the full-length BMP-7 precursor and is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The BMP7 was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) and is typically 50-250ng/ml.

    More Info

    • Introduction

      The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

    • Synonyms

      Osteogenic Protein 1, BMP-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-7 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 BMP-7 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAM AVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPR YHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLDSRTLWASE EGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKAT.

    • Background

      BMP-7 Bone Morphogenetic Protein-7 Human Recombinant: A Key Regulator of Osteogenesis and Beyond

      Abstract:

      BMP-7 (Bone Morphogenetic Protein-7), also known as Osteogenic Protein 1 or BMP-7, is a potent growth factor that plays a crucial role in various biological processes, particularly in osteogenesis and tissue regeneration.

      This research paper aims to comprehensively explore the molecular characteristics, signaling pathways, and diverse physiological functions of BMP-7.

      Additionally, it investigates the therapeutic implications of BMP-7 in different disorders. Synonyms such as Osteogenic Protein 1 and BMP-7 associated with the protein are discussed throughout the paper to highlight their relevance in scientific literature.

      Introduction:

      BMP-7, also known as Osteogenic Protein 1 or BMP-7, is a growth factor with multifaceted roles in osteogenesis, tissue regeneration, and disease. This section introduces BMP-7 and its synonyms, highlighting their significance and relevance in scientific research.

      Molecular Characteristics of BMP-7:

      This section explores the molecular characteristics of BMP-7, including its primary amino acid sequence, protein structure, post-translational modifications, and binding partners. The importance of these factors in determining BMP-7's biological activity and receptor specificity is discussed.

      Signaling Pathways Activated by BMP-7 :

      BMP-7 activates specific signaling pathways upon binding to its receptors, leading to diverse cellular responses. This section focuses on the canonical BMP signaling pathway, highlighting the activation of Smad-dependent and Smad-independent pathways. The downstream effectors and transcriptional regulators involved in mediating BMP-7's cellular responses are also discussed.

      Physiological Functions of BMP-7 :

      BMP-7 plays critical roles in various physiological processes, particularly in osteogenesis and tissue regeneration. This section provides an in-depth analysis of BMP-7's contributions to these processes, emphasizing its role in promoting bone formation, cartilage development, renal function, and wound healing.

      Therapeutic Implications of BMP-7 :

      The unique properties of BMP-7 make it a promising therapeutic candidate for various disorders. This section discusses the potential applications of BMP-7 in bone regeneration, cartilage repair, kidney disease, and tissue engineering. The challenges and future directions in utilizing BMP-7 as a therapeutic agent are also explored.

      BMP-7 in Disease Progression:

      BMP-7 is implicated in the progression of certain diseases, including fibrosis, cancer, and cardiovascular disorders. This section examines the role of BMP-7 in tissue fibrosis, tumor progression, angiogenesis, and cardiac remodeling. The therapeutic implications and targeting of BMP-7 in disease management are also discussed.

      Conclusion:

      BMP-7, also known as Osteogenic Protein 1 or BMP-7, is a critical growth factor involved in osteogenesis, tissue regeneration, and disease progression. Understanding the molecular characteristics, signaling pathways, and physiological functions of BMP-7 contributes to the exploration of its therapeutic potential in various disorders.

      What is the molecular weight/Mw of BMP7 Protein?
      BMP7 Protein has a total Mw of 38kDa.

      What is the source or expression system of BMP7 Protein?
      HEK.

      What is the Purity of BMP7 Protein?
      BMP7 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP7 Protein?
      The specific activity was determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) and is typically 50-250ng/ml.

      What is the amino acid sequence of BMP7 Protein?
      DFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAM AVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPR YHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLDSRTLWASE EGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKAT.


      What applications can BMP7 Protein be used in?
      BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP7 Protein?
      The endotoxin level is minimal, BMP7 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.

    Bmp 7 Human Hek
  • View Data Sheet

    Name :

    GDF5 Mouse, His

    Description:

    Growth differentiation factor 5 Mouse Recombinant, His Tag

    Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5.

    Product # :

    CYT-852

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    • sds-page

    Description

    GDF5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 143 amino acids (376-495 a.a) and having a molecular mass of 16kDa.GDF5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDF5 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    GDF5-sds-page - Product image 1

    More Info

    • Introduction

      GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.

    • Synonyms

      Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5.

    • 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 MGSAPLANRQ GKRPSKNLKA RCSRKALHVN FKDMGWDDWI IAPLEYEAFH CEGLCEFPLR SHLEPTNHAV IQTLMNSMDP ESTPPTCCVP TRLSPISILF IDSANNVVYK QYEDMVVESC GCR.

    • Background

      What is the molecular weight/Mw of GDF5 MOUSE Protein?
      GDF5 MOUSE Protein has a total Mw of 16kDa.

      What is the source or expression system of GDF5 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of GDF5 MOUSE Protein?
      GDF5 MOUSE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF5 MOUSE Protein?
      The biological functionality of GDF5 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of GDF5 MOUSE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSAPLANRQ GKRPSKNLKA RCSRKALHVN FKDMGWDDWI IAPLEYEAFH CEGLCEFPLR SHLEPTNHAV IQTLMNSMDP ESTPPTCCVP TRLSPISILF IDSANNVVYK QYEDMVVESC GCR.

      What applications can GDF5 MOUSE Protein be used in?
      GDF5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF5 MOUSE Protein?
      The endotoxin level is minimal, GDF5 MOUSE 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.

    Gdf5 Mouse
  • View Data Sheet

    Name :

    MIF Rat

    Description:

    Macrophage Migration Inhibitory Factor Rat Recombinant

    Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    Product # :

    CYT-193

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    Description

    MIF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa. The MIF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.

    Purity

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

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTSDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.

    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.

    Mif Rat
  • View Data Sheet

    Name :

    SDF 1a Human, His

    Description:

    Stromal Cell-Derived Factor-1 alpha Human Recombinant, His Tag

    SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.

    Product # :

    CHM-241

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    Description

    Stromal Cell-Derived Factor-1 alpha Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 78 amino acids, having a molecular mass of 9.2 kDa. The SDF-1a is fused to 10 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was filtered (0.4µm) and lyophilized from a concentrated (0.5mg/ml) solution containing 20mM Tris buffer pH-7.5 and 20mM sodium chloride.

    Purity

    Greater than 95.0% as determined SDS-PAGE.

    More Info

    • Introduction

      SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
      The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
      The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

    • Synonyms

      SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SDF1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK.

    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.

    Sdf 1A Human His
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